DETAILED CORRESPONDENCE
Status of the Application
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Claims 1-20 are pending in the application.
Applicant’s claim listing filed March 25, 2026 is acknowledged. This listing of the claims replaces all prior versions and listings of the claims.
Restriction/Election
Applicant's election with traverse of:
Group I, claims 1-11 and 15-18, drawn to the technical feature of an alpha-amylase variant of a parent alpha-amylase and a composition thereof,
Species election A: amino acid alteration at position 25,
Species election B: SEQ ID NO: 1,
Species election C: X25H+X176K+X186E, and
Species election D: further comprising a deletion at position 183
in the reply filed March 25, 2026 is acknowledged. The traversal is on the grounds that the inventions of Groups I-III are inexorably linked and that no additional search burden would be required to search and co-examined the inventions of Groups I-III together.
This is not found persuasive because the instant application is filed under 35 U.S.C. 371 and the "unity of invention" standard applies, not the "independent and distinct" standard for non-provisional applications filed under 35 U.S.C. 111(a) (see MPEP 1893.03(d)). As such, lack of a serious burden is not a proper basis of traversal in a national stage application filed under 35 U.S.C. 371.
The requirement is still deemed proper and is therefore made FINAL.
Claim 11 is withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected species, there being no allowable generic or linking claim.
Claims 12-14, 19, and 20 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to nonelected inventions, there being no allowable generic or linking claim.
Claims 1-10 and 15-18 are being examined on the merits with claims 1-3 and 8-10 being examined only to the extent the claims read on the elected subject matter as stated above. In the interest of clarity, it is noted that at least one of the following rejections is directed to a non-elected species. However, the non-elected species has yet to be searched and examined on the merits because the prior art directed to the non-elected species was identified during a search of the elected species.
Priority
This application is filed under 35 U.S.C. 371 as a national stage of international application PCT/EP2022/054045, filed February 18, 2022, which claims foreign priority under 35 U.S.C. 119(a-d) to European applications 21158484.2 and 21213738.4, filed February 22, 2021 and December 10, 2021, respectively. A certified copy of each of the foreign priority documents has been filed in this application on July 25, 2023.
Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. 119(e) or under 35 U.S.C. 120, 121, 365(c), or 386(c) is acknowledged. Applicant has not complied with one or more conditions for receiving the benefit of an earlier filing date under 35 U.S.C. 365(c) as follows:
The later-filed application must be an application for a patent for an invention which is also disclosed in the prior application (the parent or original nonprovisional application or provisional application). The disclosure of the invention in the parent application and in the later-filed application must be sufficient to comply with the requirements of 35 U.S.C. 112(a) or the first paragraph of pre-AIA 35 U.S.C. 112, except for the best mode requirement. See Transco Products, Inc. v. Performance Contracting, Inc., 38 F.3d 551, 32 USPQ2d 1077 (Fed. Cir. 1994).
The disclosure of the prior-filed application, foreign priority application no. 21158484.2, fails to provide adequate support or enablement in the manner provided by 35 U.S.C. 112(a) for one or more claims of this application because foreign priority application no. 21158484.2 fails to disclose all sequences recited in claim 1 of this application, e.g., SEQ ID NO: 41.
The effective filing date for claims 1-10 and 15-18 of this application is December 10, 2021.
Information Disclosure Statement
The information disclosure statements (IDSs) submitted on July 25, 2023, August 14, 2023, and April 13, 2026 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the IDSs have been considered by the examiner.
The IDS filed April 10, 2026 has been lined through because there is/are no cited reference(s).
Specification/Informalities
The use of the term “NCBI,” which is a trade name or a mark used in commerce, has been noted in this application (p. 7, line 6). The term should be accompanied by the generic terminology; furthermore the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks.
Claim Objections
Claims 1, 4, and 5 are objected to because of the following informalities:
Claim 1 is objected to in the recitation of “(ii) said variant has at least 60%” and in the interest of improving claim form, it is suggested that the noted phrase be amended to recite “said variant comprises an amino acid sequence having at least 60%.”
Claim 1 is also objected to in the recitation of “the amino acid sequence set forth in SEQ ID NO: 1, 3, 4, or in any of SEQ ID NO: 15-41” and in the interest of improving claim form, it is suggested that the noted phrase be amended to recite “the amino acid sequence set forth in any one of SEQ ID NO: 1, 3, 4, and 15-41.”
Claim 4 is objected to in the recitation of “wherein the variant has at least 85%” and in the interest of improving claim form, it is suggested that the noted phrase be amended to recite “wherein the variant comprises an amino acid sequence having at least 85%.”
Claim 5 is objected to in the recitation of “wherein the amino acid sequence of the A and B domain is at least 75%, but less than 100%, identical to the amino acid sequence of SEQ ID NO: 6 and the amino acid sequence of the C domain is at least 75%, but less than 100%, identical to the amino acid sequence of SEQ ID NO: 8” and in the interest of improving claim form, it is suggested that the noted phrase be amended to recite “wherein the amino acid sequence of the A and B domain has at least 75%, but less than 100%, sequence identity to the amino acid sequence of SEQ ID NO: 6 and the amino acid sequence of the C domain has at least 75%, but less than 100%, sequence identity to the amino acid sequence of SEQ ID NO: 8.”
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
Claims 1, 2, 4, 6, 7, 10, and 15-18 are rejected under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception (i.e., a law of nature, a natural phenomenon, or an abstract idea) without significantly more. Applicant’s attention is directed to the "Guidance for Determining Subject Matter Eligibility Of Claims Reciting Or Involving Laws of Nature, Natural Phenomena, & Natural Products”, released on December 16, 2014.
Claims 1, 2, 4, 6, 7, 10, 15, 16, and 18
Claim Interpretation: Claim 1 is drawn to (in relevant part) an alpha-amylase variant of a parent alpha-amylase, wherein said variant comprises:
(i) an amino acid alteration at a position corresponding to position 25 according to the numbering of the amino acid sequence set forth in SEQ ID NO: 3,
(ii) said variant has at least 60% but less than 100% sequence identity with the amino acid sequence set forth in SEQ ID NO: 1, and
(iii) said variant has alpha-amylase activity.
Claim 2 is drawn to (in relevant part) the alpha-amylase variant according to claim 1, wherein said variant comprises one or more amino acid substitutions selected from the group consisting of X25H, X25A, X25C, X25D, X25F, X25G, X25K, X25L, X25M, X25Q, X25S, X25W, and X25Y.
Claim 10 is drawn to (in relevant part) the alpha-amylase variant according to claim 1, wherein said variant comprises or consists of the amino acid sequence set forth in SEQ ID NO: 1 with one or more of the amino acid substitutions selected from the group consisting of X25H, X25A, X25C, X25D, X25F, X25G, X25K, X25L, X25M, X25Q, X25S, X25W, and X25Y.
Regarding claims 1, 2, 4, and 10, GenPept Database Accession Number WP_204204294 (February 17, 2021; 1 page; cited on the attached Form PTO-892; hereafter “GenPept WP_204204294”) discloses an alpha-amylase from Bacillus suaedaesalsae, the amino acid sequence of which has S at the position corresponding to N25 of instant SEQ ID NO: 3 of this application (see Appendix A for sequence alignment; N25 of SEQ ID NO: 3 and the corresponding position of GenPept WP_204204294 are highlighted with a box) and has 72% sequence identity to instant SEQ ID NO: 1 of this application (see Appendix B for sequence alignment). Also, GenPept Database Accession Number A27705 (June 1999, 2 pages; cited on the attached Form PTO-892; hereafter “GenPept A27705”) discloses an alpha-amylase from Bacillus sp., the amino acid sequence of which has S at the position corresponding to D36 of instant SEQ ID NO: 3 of this application and has 90% sequence identity to instant SEQ ID NO: 1 of this application (see Appendix G for sequence alignment).
Given a broadest reasonable interpretation, claims 1, 2, and 10 encompass a naturally-occurring alpha-amylase.
Claim 6 is drawn to the alpha-amylase variant according to claim 1, wherein the variant exhibits one or more improved property relative to said parent alpha-amylase.
Claim 7 is drawn to the alpha-amylase variant according to claim 6, wherein said improved property is expressed as an Improvement Factor (IF) of >1.0.
According to MPEP 2112.01, when the structure recited in the reference is substantially identical to that of the claims, claimed properties or functions are presumed to be inherent. Since the structure of the alpha-amylase of GenPept WP_204204294 is encompassed by claims 6 and 7 and “said parent alpha-amylase” is unlimited, it is presumed that the alpha-amylase of GenPept WP_204204294 exhibits the properties recited in claims 6 and 7 and given a broadest reasonable interpretation, claims 6 and 7 encompass a naturally-occurring alpha-amylase.
Claim 15 is drawn to a composition comprising the alpha-amylase variant according to claim 1 and at least one additional component.
Given a broadest reasonable interpretation, claim 15 encompasses a composition comprising a naturally-occurring alpha-amylase and a naturally occurring “additional component,” e.g., water.
Claim 16 is drawn to the composition according to claim 15, which is a detergent composition.
Given a broadest reasonable interpretation, the recitation of “detergent” in the phrase “detergent composition” does not structurally and/or functionally limit the claimed composition and claim 16 encompasses a composition comprising a naturally-occurring alpha-amylase and a naturally occurring “additional component.”
Claim 18 is drawn to the composition according to claim 15, wherein the composition comprises one or more second enzyme different from the alpha-amylase variant.
Patent Eligibility Analysis Step 1: The claims are drawn to an alpha-amylase variant and a composition thereof, which are compositions of matter and are one of the statutory categories of invention.
Patent Eligibility Analysis Step 2A Prong 1: The claimed alpha-amylase variant and composition thereof, which, given a broadest reasonably interpretation, encompass a naturally occurring alpha-amylase and composition thereof, are not considered to have markedly different characteristics from what occurs in nature, and are considered to be law of nature exceptions. Accordingly, the alpha-amylase variant and composition thereof are directed to judicial exceptions.
Patent Eligibility Analysis Step 2A Prong 2: There are no additional elements recited in the claims beyond the judicial exceptions.
Patent Eligibility Analysis Step 2B: The claims only recite laws of nature and do not include any additional elements that could add significantly more to the judicial exceptions.
Claim 17
Claim 17 is drawn to the composition according to claim 16, wherein the composition comprises one or more surfactants and/or one or more builder.
Given a broadest reasonable interpretation, claim 17 encompasses a composition comprising a naturally-occurring alpha-amylase and a naturally occurring surfactant.
Patent Eligibility Analysis Step 1: The claims are drawn to a detergent composition comprising an alpha-amylase variant and one or more surfactants and/or one or more builder, which is a composition of matter and are one of the statutory categories of invention.
Patent Eligibility Analysis Step 2A Prong 1: The claims recite a combination of naturally occurring components, which is considered to be a law of nature or a natural phenomenon (a natural product). There is no evidence of record of a naturally occurring counterpart to the claimed combination, so the combination is compared to the individual components as they occur in nature (see MPEP 2106.04(c).II.A). There is no indication in the specification or evidence of record that the combination of components has any characteristics (structural, functional, or otherwise) that are different from the corresponding individual components as each occurs in nature. Furthermore, there is no indication in the specification or evidence of record that combining these components changes the structure, function, or other properties of the naturally occurring components. In other words, the overall combination of components does not render the resulting composition different from each of the individual components. Thus, the detergent composition recited in claim 17 is not considered to have markedly different characteristics from what occurs in nature, and is considered to be a "product of nature" exception. Accordingly, the claim is directed to a judicial exception.
Patent Eligibility Analysis Step 2A Prong 2: There are no additional elements recited in the claim beyond the judicial exceptions.
Patent Eligibility Analysis Step 2B: The claim only recites a law of nature and does not include any additional elements that could add significantly more to the judicial exceptions.
As such, the claims do not qualify as eligible subject matter. For these reasons the claims are rejected under section 101 as being directed to non-statutory subject matter.
Claim Rejections - 35 USC § 112(a)
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
Claims 1-3 and 5-18 are rejected under 35 U.S.C. 112(a) as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor at the time the application was filed, had possession of the claimed invention.
MPEP 2163.II.A.2.(a).i) states, “Whether the specification shows that applicant was in possession of the claimed invention is not a single, simple determination, but rather is a factual determination reached by considering a number of factors. Factors to be considered in determining whether there is sufficient evidence of possession include the level of skill and knowledge in the art, partial structure, physical and/or chemical properties, functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the method of making the claimed invention”.
For claims drawn to a genus, MPEP § 2163 states the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406.
MPEP § 2163 further states that “[s]atisfactory disclosure of a ‘representative number’ depends on whether one of skill in the art would recognize that the applicant was in possession of the necessary common attributes or features possessed by the members of the genus in view of the species disclosed. For inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus…Instead, the disclosure must adequately reflect the structural diversity of the claimed genus, either through the disclosure of sufficient species that are ‘representative of the full variety or scope of the genus,’ or by the establishment of ‘a reasonable structure-function correlation.’ Such correlations may be established ‘by the inventor as described in the specification,’ or they may be ‘known in the art at the time of the filing date.’"
The factors considered in the Written Description requirement are (1) level of skill and knowledge in the art, (2) partial structure, (3) physical and/or chemical properties, (4) functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the (5) method of making the claimed invention. Disclosure of any combination of such identifying characteristics that distinguish the claimed invention from other materials and would lead one of skill in the art to the conclusion that the applicant was in possession of the claimed species is sufficient." MPEP § 2163.
The claims are drawn to or recite (in relevant part) a genus of alpha-amylase variants of a parent alpha-amylase, wherein said variant comprises:
(i) an amino acid alteration at a position corresponding to position 25 according to the numbering of the amino acid sequence set forth in SEQ ID NO: 3,
(ii) said variant has at least 60% but less than 100% sequence identity with the amino acid sequence set forth in SEQ ID NO: 1, and
(iii) said variant has alpha-amylase activity.
Given that the genus of alpha-amylase variants includes species having amino acid modifications (substitutions, deletions, additions, and/or insertions) of up to 40% of the amino acids of SEQ ID NO: 1, the genus is considered to encompass polypeptides with widely variant amino acid sequences.
The specification discloses the actual reduction to practice of the following representative species of the genus of alpha-amylase variants – an alpha-amylase comprising the amino acid sequence of SEQ ID NO: 3 except N25 is substituted with H, A, C, D, F, G, K, L, M, Q, S, W, or Y or an alpha-amylase comprising the amino acid sequence of SEQ ID NO: 3 except for the combinations of substitutions recited in claim 3, which has improved temperature stability or storage stability relative to the parent alpha-amylase of SEQ ID NO: 3.
Regarding the level of skill and knowledge in the art of amino acid modification, the reference of Singh et al. (Curr. Protein Pept. Sci. 18:1-11, 2017; cited on the attached Form PTO-892) reviews various protein engineering methods and discloses that despite the availability of an ever-growing database of protein structures and highly sophisticated computational algorithms, protein engineering is still limited by the incomplete understanding of protein functions, folding, flexibility, and conformational changes (see p. 7, column 1, top). Also, the unpredictability associated with surface residue substitution is exemplified by the reference of Zhang et al. (Structure 26:1474-1485, 2018; cited on the attached Form PTO-892), which discloses that even a substitution of a surface residue that was predicted to be benign caused significant structural changes and unexpected effects on the function of a polypeptide (p. 1475, column 1).
Given that the specification discloses only a relative few representative species of a widely variant genus of polypeptides, and there is a high level of unpredictability in the art of amino acid modification, the disclosed representative species are considered to be insufficient to describe the widely variant genus. One of skill in the art would reasonably conclude that the disclosure fails to provide a representative number of species to describe the genus, and thus, that the applicant was not in possession of the recited genus. The claimed subject matter is not supported by an adequate written description because a representative number of species has not been described.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1, 2, 6, 7, and 10 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by GenPept WP_204204294.
Claims 1, 2, 6, 7, and 10 are drawn to (in relevant part) an alpha-amylase variant of a parent alpha-amylase, wherein said variant comprises:
(i) an amino acid alteration at a position corresponding to position 25 according to the numbering of the amino acid sequence set forth in SEQ ID NO: 3,
(ii) said variant has at least 60% but less than 100% sequence identity with the amino acid sequence set forth in SEQ ID NO: 1, and
(iii) said variant has alpha-amylase activity.
Regarding claims 1, 2, and 10, GenPept WP_204204294 discloses an alpha-amylase from Bacillus suaedaesalsae, the amino acid sequence of which has S at the position corresponding to N25 of instant SEQ ID NO: 3 of this application (see Appendix A for sequence alignment; N25 of SEQ ID NO: 3 and the corresponding position of WP_204204294 are highlighted with a box) and has 72% sequence identity to instant SEQ ID NO: 1 of this application (see Appendix B for sequence alignment).
Regarding claims 6 and 7, GenPept WP_204204294 does not teach one or more improved property relative to said parent alpha-amylase, and does not teach said improved property is expressed as an Improvement Factor (IF) of >1.0. However, according to MPEP 2112.01, when the structure recited in the reference is substantially identical to that of the claims, claimed properties or functions are presumed to be inherent, and since the structure of the alpha-amylase of GenPept WP_204204294 is encompassed by claims 6 and 7 and “said parent alpha-amylase” is unlimited, it is presumed that the alpha-amylase of GenPept WP_204204294 exhibits the properties recited in claims 6 and 7.
Therefore, GenPept WP_204204294 anticipates claims 1, 2, 6, 7, and 10 as written.
Claims 1, 2, 4-8, 10, and 15-18 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Andersen et al. (WO 2014/183921 A1; cited on the IDS filed August 14, 2023; hereafter “Andersen”).
Regarding instant claims 1, 4-6, and 8, Andersen teaches a polypeptide having alpha-amylase activity comprising an A and B domain and a C domain wherein the amino acid sequence of the A and B domain is SEQ ID NO: 2 and the amino acid sequence of the C domain is SEQ ID NO: 6 (p. 11, line 24 to p. 12, line 9). The amino acid sequence of the alpha-amylase polypeptide of Andersen has 89% sequence identity to instant SEQ ID NO: 1 (see Appendix F for sequence alignment). Andersen teaches the amylase can be mutated to improve its wash performance and/or stability by deletion at amino acid 182 or 184 (p. 21, lines 16-19). The polypeptide of Andersen with a deletion of amino acid 182 or 184 satisfies the structural limitations of (i) and (ii) of instant claim 1 and the structural limitations of instant claims 4, 5, and 8.
Regarding instant claims 2 and 10, the amino acid sequence of the alpha-amylase polypeptide of Andersen has S at the position corresponding to D36 of instant SEQ ID NO: 3 of this application (see Appendix F for sequence alignment).
Regarding instant claim 7, according to MPEP 2112.01, when the structure recited in the reference is substantially identical to that of the claims, claimed properties or functions are presumed to be inherent. Since the structure of the alpha-amylase of Andersen is encompassed by claim 7 and “said parent alpha-amylase” is unlimited, it is presumed that the alpha-amylase of Andersen exhibits the property recited in claim 7.
Regarding instant claims 15-18, Andersen teaches a detergent composition comprising the alpha-amylase (p. 59, lines 13-15), one or more additional enzymes (p. 66, lines 5-8), and a surfactant (p. 60, line 35).
Therefore, Andersen anticipates claims 1, 2, 4-8, 10, and 15-18 as written.
Claims 1, 4-9, and 15-18 are rejected under 35 U.S.C. 102(a)(1) or 35 U.S.C. 102(a)(2) as being anticipated by Jenewein et al. (WO 2021/032881 A1; cited on the attached Form PTO-892; hereafter “Jenewein”).
Regarding instant claims 1, 4, 8, and 9, Jenewein teaches an isolated, synthetic, or recombinant hybrid polypeptide having alpha-amylase activity comprising an A and B domain of a first alpha amylase and a C domain of a second alpha amylase (p. 1, lines 17-18). Jenewein teaches preferably, the isolated, synthetic, or recombinant polypeptide having alpha-amylase activity comprises SEQ ID NO: 54 with deletion of one or more amino acids corresponding to positions 181, 182, 183, and 184 of SEQ ID NO: 39 including amino acids 181 and 182 or amino acids 182 and 183 with reference to SEQ ID NO: 39 (p. 52, line 28 to p. 53, line 2). Given that SEQ ID NO: 39 of Jenewein is identical to instant SEQ ID NO: 3 and SEQ ID NO: 54 of Jenewein is identical to instant SEQ ID NO: 1, SEQ ID NO: 54 of Jenewein with a deletion of amino acids 181 and 182 or amino acids 182 and 183 with reference to SEQ ID NO: 39 satisfies the structural limitations of (i) and (ii) of instant claim 1 and the structural limitations of instant claims 4, 8, and 9.
Regarding instant claim 5, SEQ ID NO: 54 of Jenewein has 99% identity to instant SEQ ID NO: 6 and has 98% identity to instant SEQ ID NO: 8. As such, SEQ ID NO: 54 of Jenewein with a deletion of amino acids 181 and 182 or amino acids 182 and 183 with reference to SEQ ID NO: 39 satisfies the structural limitations of claim 5.
Regarding instant claim 6, Jenewein teaches deletion of amino acids corresponding to positions 182 and 183 is a stability improving mutation (p. 17, lines 9-11).
Regarding instant claim 7, according to MPEP 2112.01, when the structure recited in the reference is substantially identical to that of the claims, claimed properties or functions are presumed to be inherent. Since the structure of the alpha-amylase of Jenewein (i.e., SEQ ID NO: 54 of Jenewein with a deletion of amino acids 181 and 182 or amino acids 182 and 183 with reference to SEQ ID NO: 39) is encompassed by claim 7 and “said parent alpha-amylase” is unlimited, it is presumed that the alpha-amylase of Jenewein exhibits the property recited in claim 7.
Regarding instant claims 15-17, Jenewein teaches the alpha-amylase is used in a detergent formulation (p. 80, lines 30-31) and teaches detergent formulations may comprise one or more surfactants (p. 83, line 27).
Regarding instant claim 18, Jenewein teaches a composition comprising the alpha-amylase, which may include another enzyme (p. 64, lines 3-7).
Therefore, Jenewein anticipates claims 1, 4-9, and 15-18 as written.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
Claims 8 and 15-18 are rejected under 35 U.S.C. 103 as being unpatentable over GenPept WP_204204294 in view of Cascao-Pereira et al. (WO 2013/063460 A2; cited on Form PTO-892; hereafter “Cascao-Pereira”).
Claim 8 is drawn to (in relevant part) the alpha-amylase variant according to claim 1, further comprising a deletion at an amino acid corresponding to position 183 wherein the numbering is according to the amino acid sequence set forth in SEQ ID NO: 3.
Claim 15 is drawn to a composition comprising the alpha-amylase variant according to claim 1 and at least one additional component.
Claim 16 is drawn to the composition according to claim 15, which is a detergent composition.
Claim 17 is drawn to the composition according to claim 16, wherein the composition comprises one or more surfactants and/or one or more builder.
Claim 18 is drawn to the composition according to claim 15, wherein the composition comprises one or more second enzyme different from the alpha-amylase variant.
The teachings of GenPept WP_204204294 as applied to claims 1, 2, 6, 7, and 10 are stated above.
GenPept WP_204204294 does not teach or suggest the limitations of claims 8 and 15-18.
Regarding claim 8, Cascao-Pereira teaches alpha-amylase mutations that provide a performance or stability benefit including at least one mutation in the calcium binding loop including a deletion of the amino acid corresponding to His-183 of SEQ ID NO: 3, and homologous residues in other amylases can be determined by structural alignment (paragraphs [00104] to [00105]).
In view of the combined teachings of GenPept WP_204204294 and Cascao-Pereira, it would have been obvious to one of ordinary skill in the art before the effective filing date to modify the alpha-amylase of GenPept WP_204204294 by deleting the amino acid corresponding to Gly-182 of SEQ ID NO: 3 of Cascao-Pereira. Gly-182 of SEQ ID NO: 3 of Cascao-Pereira corresponds to amino acid 209 of GenPept WP_204204294 (see Appendix E for sequence alignment), and amino acid 209 of GenPept WP_204204294 corresponds to amino acid 182 of instant SEQ ID NO: 3 (see Appendix A for sequence alignment). One would have been motivated and would have expected success to do so because GenPept WP_204204294 taught an alpha-amylase and Cascao-Pereira taught deleting the amino acid corresponding to Gly-182 of SEQ ID NO: 3 provides a performance or stability benefit to an alpha-amylase.
Regarding claims 15-18, Cascao-Pereira teaches alpha-amylases, particularly from Bacilli have been used for a variety of different purposes and can be used to remove starchy soils and stains during laundry washing (paragraphs [005] and [00223]). Cascao-Pereira teaches an alpha-amylase can be used as a component in a detergent composition with other enzymes (paragraphs [00225] and [00228]) and one or more surfactants (paragraph [00227]).
In view of the combined teachings of GenPept WP_204204294 and Cascao-Pereira, it would have been obvious to one of ordinary skill in the art before the effective filing date to include the alpha-amylase of GenPept WP_204204294 in a detergent composition of Cascao-Pereira. One would have been motivated and would have expected success to do so because GenPept WP_204204294 taught an alpha-amylase from Bacillus suaedaesalsae and Cascao-Pereira taught alpha-amylases, particularly from Bacilli can be used to remove starchy soils and stains during laundry washing and taught a detergent composition including alpha-amylase, other enzymes, and one or more surfactants for laundry washing.
Therefore, claims 8 and 15-18 would have been obvious to one of ordinary skill in the art before the effective filing date.
Claims 2 and 10 are rejected under 35 U.S.C. 103 as being unpatentable over Jenewein.
The relevant teachings of Jenewein as applied to claims 1, 4-9, and 15-18 are set forth above.
Regarding instant claims 2 and 10, Jenewein teaches a variant of the amylase of SEQ ID NO: 54 comprising a substitution at one or more positions, preferably conservative substitution (p. 24, lines 14-18). Jenewein teaches the amino acid residue at one or more of the amino acid positions selected from the group consisting of positions 1, 2, 3, 4, 5, 9, 17, 25, 28, 29, 32, 35, 36, 41, 48, 51, 52, 82, 83, 86, 87, 89, 90, 93, 94, 95, 96, 98, 113, 116, 118, 123, 124, 125, 129, 136, 138, 142, 144, 150, 158, 165, 169, 170, 172, 174, 183, 186, 192, 193, 206, 208, 212, 214, 217, 218, 222, 225, 227, 229, 235, 242, 243, 244, 245, 246, 250, 251, 255, 256, 260, 263, 267, 269, 273, 274, 275, 276, 280, 282, 284, 286, 291, 297, 298, 299, 302, 303, 304, 311, 313, 318, 320, 323, 324, 328, 330, 337, 338, 339, 343, 345, 346, 355, 356, 360, 361, 374, 375, 376, 377, 378, 379, 382, 384, 391, 394, 395, and 396 according to the numbering of SEQ ID NO: 39 is exchanged (p. 21, line 29 to p. 22, line 9). Jenewein also teaches preferred substitutions at positions 309, 313, 347, 348, 350, 351, 354, 355, 358, 359, 388, 389, 392 and 396 (p. 26, lines 5-16). Jenewein teaches the amino acid changes may be conservative amino acid substitutions (p. 24, lines 7-8), teaches a “conservative mutation” is exchange of one amino acid with a similar amino acid (p. 9, lines 26-27), and teaches similar amino acids (p. 10, top).
Jenewein does not explicitly teach a substitution recited in claims 2 and 10.
However, in view of the teachings of Jenewein, it would have been obvious to one of ordinary skill in the art before the effective filing date to perform the amino acid substitution taught by Jenewein with a similar amino acid, e.g., substituting asparagine at position 25 of SEQ ID NO: 54 of Jenewein with aspartate, histidine, or serine. One would have been motivated and would have expected success to do so because Jenewein taught a variant of the amylase of SEQ ID NO: 54 comprising a substitution, taught preferred substitution positions, taught the substitution is a conservative substitution, and taught amino acids that are suitable for a conservative substitution, e.g., Jenewein taught a variant of the amylase of SEQ ID NO: 54, taught asparagine at amino acid position 25 as a preferred substitution position, and taught aspartate, histidine, or serine for a conservative substitution of asparagine.
Therefore, claims 2 and 10 would have been obvious to one of ordinary skill in the art before the effective filing date.
Claim Rejections - Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Co-Pending Application No. 19/103,190
Claims 1-10 and 15-18 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 5, 7-9, and 11-14 of co-pending application no. 19/103,190 (reference application).
Regarding instant claims 1, 4, and 5, claim 1 of the reference application recites (in relevant part) an amylase variant of a parent amylase, wherein said amylase variant
(i) comprises an amino acid substitution at position 4 according to the numbering of SEQ ID NO: 3,
(ii) comprises an amino acid substitution at amino acid position corresponding to amino acid position 25 according to the numbering of SEQ ID NO: 3, and
(iii) has at least 60%, but less than 100% sequence identity with SEQ ID NO: 1.
SEQ ID NO: 3 of the reference application is identical to instant SEQ ID NO: 3 and SEQ ID NO: 1 of the reference application is identical to instant SEQ ID NO: 1.
Regarding instant claims 2, 3, and 10, claim 5 of the reference application recites (in relevant part) the amylase variant according to claim 1,
wherein said amylase variant comprises
a) a substitution at one or more positions selected from 25, 176, and 186; optionally one or more substitutions selected from X25H, X176K, and X186E.
Regarding instant claim 6, claim 9 of the reference application recites the amylase variant according to claim 1, wherein the amylase variant exhibits improved storage stability and/or improved wash performance, optionally the amylase variant exhibits improved storage stability in a detergent composition.
Regarding instant claim 7, according to MPEP 2112.01, when the structure recited in the reference is substantially identical to that of the claims, claimed properties or functions are presumed to be inherent. Since the structure of the alpha-amylase of the claims of the reference application is encompassed by instant claim 7 and “said parent alpha-amylase” is unlimited, it is presumed that the alpha-amylase of the reference application exhibits the property recited in claim 7.
Regarding instant claim 8, claim 7 of the reference application recites the amylase variant according to claim 1, further comprising a deletion at one or more amino acids corresponding to positions selected from the group consisting of 181, 182, 183 and 184, optionally a deletion of two or more amino acids corresponding to positions selected from the group consisting of 181, 182, 183 and 184, optionally a deletion of amino acids corresponding to positions 181 and 182, 182 and 183, or 183 and 184, wherein the numbering is according to the amino acid sequence set forth in SEQ ID NO: 3.
Regarding instant claim 9, claim 8 of the reference application recites (in relevant part) the amylase variant according to claim 1, wherein the amylase variant has at least 91.5%, at least 92%, at least 92.5%, at least 93%, at least 93.5%, at least 94%, at least 94.5%, at least 95%, at least 95.5%, at least 96%, at least 96.5%, at least 97%, at least 97.5%, at least 98%, at least 98.5%, at least 99%, or at least 99.5%, but less than 100% sequence identity to SEQ ID NO: 1.
Regarding instant claim 15, claim 11 of the reference application recites a composition comprising the amylase variant according to claim 1 and at least one additional component.
Regarding instant claim 16, claim 13 of the reference application recites the composition according to claim 11, wherein the composition is a detergent composition, optionally a laundry detergent composition or a hard surface cleaning detergent composition.
Regarding instant claim 17, claim 14 of the reference application recites the composition according to claim 11, wherein composition comprises one or more surfactants and/or one or more builders, optionally one or more strong sequestering builders.
Regarding instant claim 18, claim 12 of the reference application recites the composition according to claim 11, wherein the composition comprises one or more second enzyme different from the amylase variant, optionally one or more second enzyme selected from the group consisting of proteases, second amylases, lipases, cellulases, hemicellulases, mannanases, xylanases, DNases, dispersins, pectinases, oxidoreductases, and cutinases.
Therefore, claims 1-10 and 15-18 of this application are unpatentable over claims 1, 5, 7-9, and 11-14 of the reference application.
U.S. Patent No. 12,595,471 B2
Claims 1, 4-9, 15, and 18 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 11, and 13-16 of U.S. Patent No. 12,595,471 B2 (cited on the attached Form PTO-892).
Regarding instant claims 1, 4, 8, and 9, claim 1 of the patent recites an isolated, synthetic, or recombinant polypeptide having alpha-amylase activity comprising an A and B domain and a C domain wherein the amino acid sequence of the A and B domain is at least 90% identical to the amino acid sequence of SEQ ID NO: 42 and the amino acid sequence of the C domain is at least 90% identical to the amino acid sequence of SEQ ID NO: 44;
claim 11 of the patent recites (in relevant part) the polypeptide according to claim 1 comprising a deletion of amino acid position 183 corresponding to the numbering of SEQ ID NO: 39; and
claim 13 of the patent recites the polypeptide according to claim 1 comprising: an amino acid sequence having at least 90% sequence identity to SEQ ID NO:54.
SEQ ID NO: 39 of the patent is identical to instant SEQ ID NO: 3 and SEQ ID NO: 54 of the patent is identical to instant SEQ ID NO: 1. As such, the alpha-amylase polypeptide of the claims of the patent comprising the amino acid sequence of SEQ ID NO:54 and comprising a deletion of amino acid position 183 corresponding to the numbering of SEQ ID NO: 39 satisfies the structural limitations of (i) and (ii) of instant claim 1 and the structural limitations of instant claims 4, 8, and 9.
Regarding instant claim 5, SEQ ID NO: 54 of the patent has 99% identity to instant SEQ ID NO: 6 and has 98% identity to instant SEQ ID NO: 8. As such, the alpha-amylase polypeptide of the claims of the patent comprising the amino acid sequence of SEQ ID NO:54 and comprising a deletion of amino acid position 183 corresponding to the numbering of SEQ ID NO: 39 satisfies the structural limitations of claim 5.
Regarding instant claim 6, claim 14 of the patent recites the polypeptide according to claim 1, wherein the amylase has an increase in expression, activity, thermostability, stability, performance in laundry, specific activity, substrate specificity, pH-dependent activity, pH-dependent stability, oxidative stability, Ca2+ dependency, or any combination thereof compared to the amylase having the amino acid sequence of SEQ ID NO: 39 or SEQ ID NO: 40.
Regarding instant claim 7, according to MPEP 2112.01, when the structure recited in the reference is substantially identical to that of the claims, claimed properties or functions are presumed to be inherent. Since the structure of the alpha-amylase of the claims of the patent is encompassed by instant claim 7 and “said parent alpha-amylase” is unlimited, it is presumed that the alpha-amylase of the patent exhibits the property recited in claim 7.
Regarding instant claims 15 and 18, claim 15 of the patent recites a composition comprising the isolated, synthetic, or recombinant polypeptide having alpha-amylase activity according to claim 1; and
claim 16 of the patent recites the composition of claim 15, further comprising at least one second enzyme selected from the group consisting of: a second amylase, a lipase, a protease, a cellulase, a laccase, a mannanase, a pectinase, xylanase, and a nuclease.
Therefore, claims 1, 4-9, 15, and 18 of this application are unpatentable over claims 1, 11, and 13-16 of the patent.
Claims 2, 10, 16, and 17 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 11, and 13-16 of U.S. Patent No. 12,595,471 B2 as applied to claims 1, 4-9, 15, and 18 in view of Jenewein.
The claims of the patent do not recite the limitations of instant claims 2, 10, 16, and 17.
Regarding instant claims 2 and 10, Jenewein teaches a variant of the amylase of SEQ ID NO: 54 comprising a substitution at one or more positions, preferably conservative substitution (p. 24, lines 14-18). SEQ ID NO: 54 of the patent is identical to SEQ ID NO: 54 of Jenewein. Jenewein teaches the amino acid residue at one or more of the amino acid positions selected from the group consisting of positions 1, 2, 3, 4, 5, 9, 17, 25, 28, 29, 32, 35, 36, 41, 48, 51, 52, 82, 83, 86, 87, 89, 90, 93, 94, 95, 96, 98, 113, 116, 118, 123, 124, 125, 129, 136, 138, 142, 144, 150, 158, 165, 169, 170, 172, 174, 183, 186, 192, 193, 206, 208, 212, 214, 217, 218, 222, 225, 227, 229, 235, 242, 243, 244, 245, 246, 250, 251, 255, 256, 260, 263, 267, 269, 273, 274, 275, 276, 280, 282, 284, 286, 291, 297, 298, 299, 302, 303, 304, 311, 313, 318, 320, 323, 324, 328, 330, 337, 338, 339, 343, 345, 346, 355, 356, 360, 361, 374, 375, 376, 377, 378, 379, 382, 384, 391, 394, 395, and 396 according to the numbering of SEQ ID NO: 39 is exchanged (p. 21, line 29 to p. 22, line 9). SEQ ID NO: 39 of the patent is identical to SEQ ID NO: 39 of Jenewein. Jenewein also teaches preferred substitutions at positions 309, 313, 347, 348, 350, 351, 354, 355, 358, 359, 388, 389, 392 and 396 (p. 26, lines 5-16). Jenewein teaches the amino acid changes may be conservative amino acid substitutions (p. 24, lines 7-8), teaches a “conservative mutation” is exchange of one amino acid with a similar amino acid (p. 9, lines 26-27), and teaches similar amino acids (p. 10, top).
In view of the teachings of Jenewein, it would have been obvious to one of ordinary skill in the art before the effective filing date to modify the alpha-amylase of the claims of the patent by performing the amino acid substitution taught by Jenewein with a similar amino acid, e.g., substituting asparagine at position 25 of SEQ ID NO: 54 with aspartate, histidine, or serine. One would have been motivated and would have expected success to do so because the claims of the patent recite an alpha-amylase having at least 90% sequence identity to SEQ ID NO:54 and Jenewein taught the following: a variant of the amylase of SEQ ID NO: 54 comprising a substitution, preferred substitution positions, the substitution is a conservative substitution, and amino acids that are suitable for a conservative substitution, e.g., Jenewein taught a variant of the amylase of SEQ ID NO: 54, taught asparagine at amino acid position 25 as a preferred substitution position, and taught aspartate, histidine, or serine for a conservative substitution of asparagine.
Regarding instant claims 16 and 17, as stated above, claim 14 of the patent recites (in relevant part) the polypeptide according to claim 1, wherein the amylase has an increase in performance in laundry.
Jenewein teaches the alpha-amylase is used in a detergent formulation (p. 80, lines 30-31) and teaches detergent formulations may comprise one or more surfactants (p. 83, line 27).
In view of the teachings of Jenewein, it would have been obvious to one of ordinary skill in the art before the effective filing date to include the alpha-amylase of the claims of the patent in a detergent composition of Jenewein. One would have been motivated and would have expected success to do so because the claims of the patent recite an alpha-amylase that has an increase in performance in laundry, and Jenewein taught the alpha-amylase is used in a detergent formulation with one or more surfactants.
Therefore, claims 2, 10, 16, and 17 of this application are unpatentable over claims 1, 11, and 13-16 of the patent in view of Jenewein.
Claims 16 and 17 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 11, and 13-16 of U.S. Patent No. 12,595,471 B2 as applied to claims 1, 4-9, 15, and 18 in view of Cascao-Pereira.
Regarding instant claims 16 and 17, as stated above, claim 14 of the patent recites (in relevant part) the polypeptide according to claim 1, wherein the amylase has an increase in performance in laundry.
The claims of the patent do not recite the limitations of instant claims 16 and 17.
Cascao-Pereira teaches alpha-amylases have been used for a variety of different purposes and can be used to remove starchy soils and stains during laundry washing (paragraphs [005] and [00223]). Cascao-Pereira teaches an alpha-amylase can be used as a component in a detergent composition (paragraphs [00225] and [00228]) with one or more surfactants (paragraph [00227]).
In view of the teachings of Cascao-Pereira, it would have been obvious to one of ordinary skill in the art before the effective filing date to include the alpha-amylase of the claims of the patent in a detergent composition of Cascao-Pereira. One would have been motivated and would have expected success to do so because the claims of the patent recite an alpha-amylase that has an increase in performance in laundry, and Cascao-Pereira taught alpha-amylases can be used to remove starchy soils and stains during laundry washing and taught a detergent composition including alpha-amylase and one or more surfactants for laundry washing.
Therefore, claims 16 and 17 of this application are unpatentable over claims 1, 11, and 13-16 of the patent in view of Cascao-Pereira.
Conclusion
Status of the claims:
Claims 1-20 are pending.
Claims 11-14, 19, and 20 are withdrawn.
Claims 1-10 and 15-18 are rejected.
No claim is in condition for allowance.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to DAVID J STEADMAN whose telephone number is (571)272-0942. The examiner can normally be reached Monday to Friday, 7:30 AM to 4:00 PM.
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/David Steadman/Primary Examiner, Art Unit 1656
APPENDIX A
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APPENDIX B
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APPENDIX C
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APPENDIX D
BIZ83469
ID BIZ83469 standard; protein; 483 AA.
XX
AC BIZ83469;
XX
DT 15-APR-2021 (first entry)
XX
DE Bacillus subtilis amylase variant, SEQ 54.
XX
KW Amylase; baking; enzyme engineering; ethanol; mutein; paper; pulp;
KW starch; surfactant; textile.
XX
OS Bacillus subtilis.
OS Synthetic.
XX
CC PN WO2021032881-A1.
XX
CC PD 25-FEB-2021.
XX
CC PF 21-AUG-2020; 2020WO-EP073514.
XX
PR 22-AUG-2019; 2019US-0890325P.
PR 25-SEP-2019; 2019US-0905893P.
PR 05-NOV-2019; 2019US-0930806P.
XX
CC PA (BADI ) BASF SE.
XX
CC PI Jenewein S, Miles ZD, Anand P;
XX
DR WPI; 2021-192366/022.
DR N-PSDB; BIZ83470.
XX
CC PT New isolated, synthetic, or recombinant polypeptide having alpha-amylase
CC PT activity, useful for preparing dough or baked product, cleaning or
CC PT washing textiles, hard surfaces, or dishes, processing starch, pulp or
CC PT paper, and making ethanol.
XX
CC PS Claim 13; SEQ ID NO 54; 105pp; English.
XX
CC The present invention relates to a novel isolated, synthetic, or
CC recombinant polypeptide having alpha-amylase activity, useful for
CC preparing dough or baked product, cleaning or washing textiles, hard
CC surfaces, or dishes, processing starch, pulp or paper, and making
CC ethanol. The invention also provides: an isolated, synthetic, or
CC recombinant nucleic acid encoding the polypeptide; a nucleic acid
CC construct comprising the polynucleotide; an expression vector comprising
CC the polynucleotide or nucleic acid construct; a host cell comprising the
CC polynucleotide, nucleic acid construct, or expression vector; a
CC composition comprising the isolated, synthetic, or recombinant
CC polypeptide having alpha-amylase activity; a method for preparing the
CC isolated, synthetic, or recombinant polypeptide having alpha-amylase
CC activity; a method for preparing a dough or a baked product prepared from
CC the dough; and a method for using a C domain of a first amylase. Note:
CC The present sequence is used as a parent sequence for generating variants
CC (see BIZ83472-BIZ83483) and the information is given in example 5.
XX
SQ Sequence 483 AA;
Query Match 100.0%; Score 2698; Length 483;
Best Local Similarity 100.0%;
Matches 483; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 HHNGTNGTMMQYFEWYLPNDGNHWNRLRSDASNLKDKGITAVWIPPAWKGASQNDVGYGA 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 HHNGTNGTMMQYFEWYLPNDGNHWNRLRSDASNLKDKGITAVWIPPAWKGASQNDVGYGA 60
Qy 61 YDLYDLGEFNQKGTVRTKYGTRNQLQAAVTALKSNGIQVYGDVVMNHKGGADATEWVRAV 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 YDLYDLGEFNQKGTVRTKYGTRNQLQAAVTALKSNGIQVYGDVVMNHKGGADATEWVRAV 120
Qy 121 EVNPSNRNQEVSGDYTIEAWTKFDFPGRGNTHSNFKWRWYHFDGVDWDQSRQLQNRIYKF 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 EVNPSNRNQEVSGDYTIEAWTKFDFPGRGNTHSNFKWRWYHFDGVDWDQSRQLQNRIYKF 180
Qy 181 RGKGWDWEVDTENGNYDYLMYADIDMDHPEVVNELRNWGVWYTNTLGLDGFRIDAVKHIK 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 RGKGWDWEVDTENGNYDYLMYADIDMDHPEVVNELRNWGVWYTNTLGLDGFRIDAVKHIK 240
Qy 241 YSFTRDWLTHVRNTTGKNMFAVAEFWKNDIGAIENYLSKTNWNHSVFDVPLHYNLYNASR 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 YSFTRDWLTHVRNTTGKNMFAVAEFWKNDIGAIENYLSKTNWNHSVFDVPLHYNLYNASR 300
Qy 301 SGGNYDMRQIFNGTVVQRHPTHAVTFVDNHDSQPEEALESFVEEWFKPLAYALTLTRDQG 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 SGGNYDMRQIFNGTVVQRHPTHAVTFVDNHDSQPEEALESFVEEWFKPLAYALTLTRDQG 360
Qy 361 YPSVFYGDYYGIPTHGVPAMKSKIDPILEARQKYAYGTQRDYLDHPDVIGWTREGDGVHA 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 YPSVFYGDYYGIPTHGVPAMKSKIDPILEARQKYAYGTQRDYLDHPDVIGWTREGDGVHA 420
Qy 421 DSGLATLMSDGPGGSKWMEVGKNNAGEVWYDITGNQTNTVTINKDGWGQFHVSGGSVSIY 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 DSGLATLMSDGPGGSKWMEVGKNNAGEVWYDITGNQTNTVTINKDGWGQFHVSGGSVSIY 480
Qy 481 VQQ 483
|||
Db 481 VQQ 483
APPENDIX E
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696
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APPENDIX F
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APPENDIX G
A27705
alpha-amylase (EC 3.2.1.1) precursor - Bacillus sp.
N;Alternate names: 1,4-alpha-D-glucan glucanohydrolase; G6-amylase
C;Species: Bacillus sp.
C;Date: 31-Mar-1989 #sequence_revision 18-Aug-1995 #text_change 31-Dec-2004
C;Accession: A27705
R;Tsukamoto, A.; Kimura, K.; Ishii, Y.; Takano, T.; Yamane, K.
Biochem. Biophys. Res. Commun. 151, 25-31, 1988
A;Title: Nucleotide sequence of the maltohexaose-producing amylase gene from an alkalophilic Bacillus sp. 707 and structural similarity to liquefying type alpha-amylases.
A;Reference number: A27705; MUID:88162814; PMID:3258152
A;Accession: A27705
A;Molecule type: DNA
A;Residues: 1-518 <TSU>
A;Cross-references: UNIPROT:P19571; UNIPARC:UPI0000125A43; GB:M18862; NID:g142496; PIDN:AAA22231.1; PID:g142497
A;Experimental source: chromosomal DNA of strain 707
A;Note: amino end of mature protein also determined
C;Comment: This is the smallest of five starch-hydrolyzing enzymes from this organism.
C;Function:
A;Description: catalyzes the hydrolysis of internal 1,4-alpha-D-glucosidic bonds
A;Pathway: glycogen/starch degradation
C;Superfamily: alpha-amylase, thermostable type; alpha-amylase core homology
C;Keywords: extracellular protein; glycosidase; hydrolase; polysaccharide degradation
F;1-33/Domain: signal sequence #status predicted <SIG>
F;34-518/Product: alpha-amylase #status experimental <MAT>
F;236-369/Domain: alpha-amylase core homology <AMY>
F;139,238,273/Binding site: calcium (Asn, Asp, His) #status predicted
F;269,299,366/Active site: Asp, Glu, Asp #status predicted
Query Match 90.4%; Score 2439; Length 518;
Best Local Similarity 89.1%;
Matches 432; Conservative 27; Mismatches 24; Indels 2; Gaps 1;
Qy 1 HHNGTNGTMMQYFEWYLPNDGNHWNRLRSDASNLKDKGITAVWIPPAWKGASQNDVGYGA 60
||||||||||||||||||||||||||| ||||||| ||||||||||||||||||||||||
Db 34 HHNGTNGTMMQYFEWYLPNDGNHWNRLNSDASNLKSKGITAVWIPPAWKGASQNDVGYGA 93
Qy 61 YDLYDLGEFNQKGTVRTKYGTRNQLQAAVTALKSNGIQVYGDVVMNHKGGADATEWVRAV 120
||||||||||||||||||||||:|||||||:||:||||||||||||||||||||| ||||
Db 94 YDLYDLGEFNQKGTVRTKYGTRSQLQAAVTSLKNNGIQVYGDVVMNHKGGADATEMVRAV 153
Qy 121 EVNPSNRNQEVSGDYTIEAWTKFDFPGRGNTHSNFKWRWYHFDGVDWDQSRQLQNRIYKF 180
||||:||||||:|:|||||||:|||||||||||:|||||||||||||||||:| ||||||
Db 154 EVNPNNRNQEVTGEYTIEAWTRFDFPGRGNTHSSFKWRWYHFDGVDWDQSRRLNNRIYKF 213
Qy 181 R--GKGWDWEVDTENGNYDYLMYADIDMDHPEVVNELRNWGVWYTNTLGLDGFRIDAVKH 238
| || ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 214 RGHGKAWDWEVDTENGNYDYLMYADIDMDHPEVVNELRNWGVWYTNTLGLDGFRIDAVKH 273
Qy 239 IKYSFTRDWLTHVRNTTGKNMFAVAEFWKNDIGAIENYLSKTNWNHSVFDVPLHYNLYNA 298
|||||||||: |||: |||||||||||||||:||||||| ||||||||||||||||||||
Db 274 IKYSFTRDWINHVRSATGKNMFAVAEFWKNDLGAIENYLQKTNWNHSVFDVPLHYNLYNA 333
Qy 299 SRSGGNYDMRQIFNGTVVQRHPTHAVTFVDNHDSQPEEALESFVEEWFKPLAYALTLTRD 358
|:|||||||| |||||||||||:||||||||||||||||||||||||||||||||||||:
Db 334 SKSGGNYDMRNIFNGTVVQRHPSHAVTFVDNHDSQPEEALESFVEEWFKPLAYALTLTRE 393
Qy 359 QGYPSVFYGDYYGIPTHGVPAMKSKIDPILEARQKYAYGTQRDYLDHPDVIGWTREGDGV 418
||||||||||||||||||||||:|||||||||||||||| | ||||| ::|||||||:
Db 394 QGYPSVFYGDYYGIPTHGVPAMRSKIDPILEARQKYAYGKQNDYLDHHNIIGWTREGNTA 453
Qy 419 HADSGLATLMSDGPGGSKWMEVGKNNAGEVWYDITGNQTNTVTINKDGWGQFHVSGGSVS 478
| :|||||:|||| |||||| ||:| ||:|| |||||:| ||||| |||| | |:|||||
Db 454 HPNSGLATIMSDGAGGSKWMFVGRNKAGQVWSDITGNRTGTVTINADGWGNFSVNGGSVS 513
Qy 479 IYVQQ 483
|:| :
Db 514 IWVNK 518
Prosecution Insights