Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
DETAILED ACTION
This application is a 371 of PCT/CN2021/104841.
The amendment filed on November 14, 2025 has been entered.
Election/Restrictions
Applicant's election with traverse of Group I (claims 1 and 10-11) with a species election of (1) SEQ ID NO:2 as the parent and (2) mutation of amino acids selected from the table on at pages 13-18 in the reply filed on November 14, 2025 is acknowledged.
The traversal is on the ground(s) that (1) Hong does not disclose that the amino acid sequence of SEQ ID NO:2 of the instant application serves as the parent transaminase and (2) Hong does not disclose a mutation site and a mutation type based on F88. This is not found persuasive because (1) MPEP 2113 states that the “patentability of a product does not depend on its method of production.”. In the instant case, the structure of the claimed transaminase mutant implied is the same whether the transaminase mutant is obtained from recombinant engineering of SEQ ID NO:2 of the instant application or is obtained from any source, as long as the resulting product has the structural limitations recited in the claims. The claims do not recite any limitation that the transaminase mutant of SEQ ID NO:2 has only the amino acid substitution(s) recited in claim 1. Therefore, claim 1 allows for other amino acid modifications. (2) Regarding the F88 mutation, the technical feature linking Groups I-III is not a transaminase mutant of SEQ ID NO:2, wherein the mutant has an F88A amino acid substitution. Instead, the technical feature linking Groups I-III is a transaminase mutant of SEQ ID NO:1 or 2, wherein the transaminase mutant has one or more amino acid substitutions recited in claim 1, such as having an Ala residue at the position corresponding to 417. Claim 1 does recite any limitation that the transaminase mutant must have F88A mutation, but having the F88A mutation is recited in the alternative.
The traversal is on the ground(s) that the parent transaminase of Hong differs from the transaminase of SEQ ID NO:1 of the instant application by one residue, which can lead to significantly difference in enzyme function and its potential for improvement and the K90G mutation is not entirely equivalent to the enzyme of Hong and will have not necessarily have similarities in terms of catalytic performance, substrate spectrum, thermal stability, and industrial adaptability. This is not found persuasive. Hong discloses a parent polypeptide having transaminase activity and a mutant (K90G) having transaminase activity. Therefore, the limitations of claim 1 or the technical feature has been met. Further, it is noted that the features upon which applicant relies (i.e., degree of enzymatic activity, potential for improvement, catalytic performance, substrate spectrum, thermal stability, and industrial adaptability) are not recited in the rejected claim(s). Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993).
The traversal is on the ground(s) that the parent transaminase of SEQ ID NO:2 of the instant application has an Asp residue at position 416, which corresponds to position the Arg residue at position 416 of Hong and for the technical problem addressed in the present application, the presence of the Asp residue at position 416 is more beneficial for the catalytic conformation required to synthesize a sterically chiral amine. Therefore, Applicant argues that the prior art does not disclose the information of using SEQ ID NO:1 or 2 as transaminase for synthesizing sterically hindered chiral amines and does not fully disclose specific mutation sites (such as F88A) can serve as specific technical features of Group I, II, and II. This is not found persuasive. First, the transaminase mutant of SEQ ID NO:28 of Hong has an Thr residue at position 416 and not a Arg residue. Second, Hong discloses a transaminase mutant having which has an Ala residue at the position corresponding to 417 of SEQ ID NO:2 of the instant application. Therefore, the limitations of the technical feature (or claim 1) has been met. Third, the technical feature linking Groups I-III is a transaminase mutant of SEQ ID NO:1 or 2, wherein the transaminase mutant has one or more amino acid substitutions recited in claim 1. The technical feature does not require the property of synthesizing a sterically chiral amine nor synthesizing sterically hindered chiral amines. Fourth, the technical feature linking Groups I-III does not require a F88A mutation but one or more amino acid substitutions recited in claim 1.
The traversal is on the ground(s) that the applications and results of the transaminase mutants of Hong is different from those of the instant application. This is not found persuasive. The technical feature linking Groups I-III is a transaminase mutant of SEQ ID NO:1 or 2, wherein the transaminase mutant has one or more amino acid substitutions recited in claim 1. This technical feature is disclosed by Hong as discussed above. The technical feature does not require the properties discussed in Applicant’s argument.
The traversal is on the ground(s) that the effects of the present application are different from those of Hong. This is not found persuasive. The technical feature linking Groups I-III is a transaminase mutant of SEQ ID NO:1 or 2, wherein the transaminase mutant has one or more amino acid substitutions recited in claim 1. This technical feature is disclosed by Hong as discussed above. The technical feature does not require the properties discussed in Applicant’s argument.
Since Applicant has elected any of the amino acid mutation(s) recited at pages 13-18 in the reply filed on November 14, 2025, the Examiner has selected T107A or S417 as the amino acid modification made in the parent transaminase of SEQ ID NO:2, which is disclosed in the prior art, see the 102 rejection below. Therefore, search and examination has not been extended to any subsequent species.
The requirement is still deemed proper and is therefore made FINAL.
Claims 2-11 are withdrawn from further consideration pursuant to 37 CFR 1.142(b), as being drawn to a nonelected species (claims 10-11) and non-elected invention (claims 2-9), there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on November 14, 2025.
Status of Claims
Claims 1-11 are pending.
Claims 2-11 are withdrawn.
Claim 1 is under examination.
Claim for Foreign Priority
Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on August 3, 2023, July 22, 2024, October 22, 2024, and January 21, 2025 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statements are being considered by the examiner.
Drawings
The drawings are objected to because the Fig. 1-3 are blurry and illegible. Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance.
Specification
The disclosure is also objected to because of the following informalities: Table 10 at page 39 is blurry and illegible.
Appropriate correction is required.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claim 1 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 1 recites the limitation “/”. The metes and bounds of the limitation in the context of the claim are not clear. It is unclear how the “/” relates to amino acid mutations. Clarification is requested.
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.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
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 of carrying out his invention.
Claim 1 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, 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, or for pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention.
MPEP 2111.01 states that ''[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow.'' Regarding claim 1, the limitation “mutant obtained from a mutation of amino acids of SEQ ID NO:2, the mutation of amino acid is selected from any one…” has been broadly interpreted to encompass any mutant transaminase of SEQ ID NO:2, wherein the transaminase mutant comprises an S417A amino acid substitution and any other amino acid mutations. Therefore, the claim is directed to drawn to a genus of transaminase mutants having unknown structure but having transaminase activity.
MPEP 2163 I. states that to “satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention.
MPEP 2163. II.A.3.(a) sates that “Possession may be shown in many ways. For example, possession may be shown by describing an actual reduction to practice of the claimed invention. Possession may also be shown by a clear depiction of the invention in detailed drawings or in structural chemical formulas which permit a person skilled in the art to clearly recognize that inventor had possession of the claimed invention. An adequate written description of the invention may be shown by any description of sufficient, relevant, identifying characteristics so long as a person skilled in the art would recognize that the inventor had possession of the claimed invention.
According to MPEP 2163.II.A.3.(a).ii), “Satisfactory 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.’"
The recitation of “transaminase” fails to provide a sufficient description of the genus of the polynucleotides and encoded polypeptides as it merely describes the functional features of the genus without providing any definition of the structural features of the species within the genus. The specification does not specifically define any of the species that fall within the genus. The specification does not define any structural features commonly possessed by members of the genus that distinguish them from others. One skilled in the art therefore cannot, as one can do with a fully described genus, visualize or recognize the identity of the members of the genus.
Wild-type Chromobacterium violaceum ω-transaminase was known in the art. Foster (US 2019/0352682 – form PTO-892) discloses wildtype Chromobacterium violaceum ω-transaminase having 100% sequence identity to the transaminase having the amino acid sequence of SEQ ID NO:1 of the instant application ([0010]) and see the sequence alignment below). Foster also discloses a few point mutations ([0015]). However, any transaminase mutant having unknown structure but having transaminase activity were not known in the art.
Fransceus (J Ind Microbiol Biotechnol. 2017 May;44(4-5):687-695. – form PTO-892) reviews protein engineering techniques, such as random mutagenesis and recombination, directed evolution and iterative or combinatory saturation “hotspots”. Fransceus states that “a recurring problem, however, is choosing which amino acid positions should be targeted. Answering this question is not an easy feat and requires substantial insight in the relationship between an enzyme’s sequence or structure and its properties.” Sanavia (Computational and Structural Biotechnology Journal, Volume 18, 2020, Pages 1968-1979. – form PTO-892) discloses challenges in the prediction of protein stability in the occurrence of multiple mutations. “Multiple-point mutations are common variations of the protein sequence that may be needed in protein engineering when a single-point mutation is not enough to yield the desired stability change. Dealing with multiple-site variations adds another level of complexity beyond the prediction of the effect of a single variant on protein stability, since it requires the learning of many types of combinatorial effects”.
The specification is limited to the description of specific transaminase mutants of SEQ ID NO:1 or 2, wherein the transaminase mutants consist of the amino acid substitutions recited in claim 1 and has transaminase activity (such as a transaminase mutant having the amino acid sequence of SEQ ID NO:2 except having an Ala at position 417). While MPEP 2163 acknowledges that in certain situations “one species adequately supports a genus,” it also acknowledges that “[f]or 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.” In view of the widely variant species encompassed by the genus, the examples described above is not enough and does not constitute a representative number of species to describe the whole genus. Therefore, the specification fails to describe a representative species of the claimed genus.
Further, one of skill in the art could identify mutants of SEQ ID NO:1 or 2. However, there is no teaching regarding which amino acids can vary from SEQ ID NO:1 or 2 and result in polypeptide having transaminase activity. An important consideration is that structure is not necessarily a reliable indicator of function. In the instant case, there is no disclosure relating similarity of structure to conservation of function. Conservation of structure is not necessarily a surrogate for conservation of function.
Given this lack of description of the representative species encompassed by the genus of the claims, the specification fails to sufficiently describe the claimed invention in such full, clear, concise, and exact terms that a skilled artisan would recognize that applicants were in possession of the inventions of claim 1.
Claim 1 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, because the specification, while being enabling for specific transaminase mutants of SEQ ID NO:1 or 2, wherein the transaminase mutants consist of the amino acid substitutions recited in claim 1 and has transaminase activity, does not reasonably provide enablement any mutant of SEQ ID NO:1 or 2 having unknown structure but having transaminase activity The specification does not enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the invention commensurate in scope with these claims.
Factors to be considered in determining whether undue experimentation is required are summarized in In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988). They include (1) the quantity of experimentation necessary, (2) the amount of direction or guidance presented, (3) the presence or absence of working examples, (4) the nature of the invention, (5) the state of the prior art, (6) the relative skill of those in the art, (7) the predictability or unpredictability of the art, and (8) the breadth of the claims.
The breadth of the claims.
MPEP 2111.01 states that ''[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow.'' Regarding claim 1, the limitation “mutant obtained from a mutation of amino acids of SEQ ID NO:2, the mutation of amino acid is selected from any one…” has been broadly interpreted to encompass any mutant transaminase of SEQ ID NO:2, wherein the transaminase mutant comprises an S417A amino acid substitution and any other amino acid mutations. Therefore, the claim is directed to drawn to any transaminase mutant having unknown structure but having transaminase activity.
The claims are not commensurate with the enablement provided by the disclosure with regard to the extremely large number of polypeptides. In the instant case, the specification is limited to specific transaminase mutants of SEQ ID NO:1 or 2, wherein the transaminase mutants consist of the amino acid substitutions recited in claim 1 and has transaminase activity (such as a transaminase mutant having the amino acid sequence of SEQ ID NO:2 except having an Ala at position 417).
The quantity of experimentation required to practice the claimed invention based on the teachings of the specification.
While enzyme isolation techniques, recombinant and mutagenesis techniques were known in the art at the time of the invention, e.g. mutagenesis, and it is routine in the art to screen for variants comprising multiple substitutions or multiple modifications as encompassed by the instant claims, the specific amino acid positions within the protein's sequence where amino acid modifications can be made with a reasonable expectation of success in obtaining the desired activity/utility are limited in any protein and the result of such modifications is unpredictable. In addition, one skilled in the art would expect any tolerance to modification for a given protein to diminish with each further and additional modification, e.g. multiple substitutions.
In the absence of: (a) rational and predictable scheme for making any transaminase mutant comprising one of the amino acid substitutions recited in claim 1 and any other amino acid mutations and having transaminase activity, and (b) a correlation between structure and the function of having transaminase activity. the specification provides insufficient guidance as to which of the essentially infinite possible choices is likely to be successful. One of skill in the art would have to test these infinite possible polypeptides to determine which polypeptides have transaminase activity. While enablement is not precluded by the necessity for routine screening, if a large amount of screening is required, as is the case herein, the specification must provide a reasonable amount of guidance which respect to the direction in which the experimentation should proceed so that a reasonable number of species can be selected for testing. In view of the fact that such guidance has not been provided in the instant specification, it would require undue experimentation to enable the full scope of the claims.
The state of prior art, the relative skill of those in the art, and predictability or unpredictability of the art.
Since the amino acid sequence of the transaminase mutant determines its structural and functional properties, predictability of which changes can be tolerated in a protein's amino acid sequence and obtain the desired activity requires a knowledge of and guidance with regard to which amino acids in the protein's sequence, if any, are tolerant of modification and which are conserved (i.e. expectedly intolerant to modification), and detailed knowledge of the ways in which the proteins' structure relates to its function. In the instant case, neither the specification or the art provide a correlation between structure and activity such that one of skill in the art can envision the structure of any mutant having transaminase activity. In addition, the art does not provide any teaching or guidance as to (1) which segments of the polypeptide of SEQ ID NO:1 or 2 that are essential for polypeptides having transaminase activity, and (2) the general tolerance of the transaminase of SEQ ID NO:1 or 2 to structural modifications and the extent of such tolerance. The art clearly teaches that changes in a protein's amino acid sequence to obtain the desired activity without any guidance/knowledge as to which amino acids in a protein are required for that activity is highly unpredictable. At the time of the invention there was a high level of unpredictability associated with altering a polypeptide sequence with an expectation that the polypeptide will maintain the desired activity. For example, Studer (Residue mutations and their impact on protein structure and function: detecting beneficial and pathogenic changes. Biochem. J. (2013) 449, 581–594. – form PTO-892) teach that (1) protein engineers are frequently surprised by the range of effects caused by single mutations that they hoped would change only one specific and simple property in enzymes, (2) the often surprising results obtained by experiments where single mutations are made reveal how little is known about the rules of protein stability, and (3) the difficulties in designing de novo stable proteins with specific functions.
Wild-type Chromobacterium violaceum ω-transaminase was known in the art. Foster (US 2019/0352682 – form PTO-892) discloses wildtype Chromobacterium violaceum ω-transaminase having 100% sequence identity to the transaminase having the amino acid sequence of SEQ ID NO:1 of the instant application ([0010]) and see the sequence alignment below). Foster also discloses a few point mutations ([0015]). However, any transaminase mutant having unknown structure but having transaminase activity were not known in the art.
Fransceus (J Ind Microbiol Biotechnol. 2017 May;44(4-5):687-695. – form PTO-892) reviews protein engineering techniques, such as random mutagenesis and recombination, directed evolution and iterative or combinatory saturation “hotspots”. Fransceus states that “a recurring problem, however, is choosing which amino acid positions should be targeted. Answering this question is not an easy feat and requires substantial insight in the relationship between an enzyme’s sequence or structure and its properties.” Sanavia (Computational and Structural Biotechnology Journal, Volume 18, 2020, Pages 1968-1979. – form PTO-892) discloses challenges in the prediction of protein stability in the occurrence of multiple mutations. “Multiple-point mutations are common variations of the protein sequence that may be needed in protein engineering when a single-point mutation is not enough to yield the desired stability change. Dealing with multiple-site variations adds another level of complexity beyond the prediction of the effect of a single variant on protein stability, since it requires the learning of many types of combinatorial effects”.
The amount of direction or guidance presented and the existence of working examples.
The specification is limited to specific transaminase mutants of SEQ ID NO:1 or 2, wherein the transaminase mutants consist of the amino acid substitutions recited in claim 1 and has transaminase activity. However, the speciation fails to provide any information as to (1) specific substrates associated with any transaminase mutant or (2) structural elements required in polypeptide having transaminase activity.
Thus, in view of the overly broad scope of the claims, the lack of guidance and working examples provided in the specification, the high level of unpredictability of the prior art in regard to structural changes and their effect on function and the lack of knowledge about a correlation between structure and function, an undue experimentation would be necessary one having ordinary skill in the art to make and use the claimed invention in a manner reasonably correlated with the scope of the claims. The scope of the claims must bear a reasonable correlation with the scope of enablement (In re Fisher, 166 USPQ 19 24 (CCPA 1970)). Without sufficient guidance, determination of polypeptides having the desired biological characteristics recited in the claims are unpredictable and the experimentation left to those skilled in the art is unnecessarily, and improperly, extensive and undue. See In re Wands 858 F.2d 731, 8 USPQ2nd 1400 (Fed. Cir, 1988).
Claim Rejections - 35 USC § 102
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
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.
Claim(s) 1 is/are rejected under 35 U.S.C. 102(a)(1) or 102(a)(2) as being anticipated by Hong (102(a)(1): WO 2019148494 – cited previously on form PTO-892 and 102(a)(2) its corresponding US Patent No. 11,359,219 – cited previously on form PTO-892. US Patent No. 11,359,219 is used for specific passages of Hong).
MPEP 2111.01 states that ''[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow.'' Regarding claim 1, the limitation “mutant obtained from a mutation of amino acids of SEQ ID NO:2, the mutation of amino acid is selected from any one…” has been broadly interpreted to encompass any mutant transaminase of SEQ ID NO:2, wherein the transaminase mutant comprises an Ala residue at the position corresponding to T107 or S417 of SEQ ID NO: 2 of the instant application and any other amino acid differences compared to SEQ ID NO:2 of the instant application.
Regarding claim 1, Hong discloses a transaminase mutant of SEQ ID NO:1, wherein the transaminase mutant has a T107A amino acid substitution and other amino acid differences compared to SEQ ID NO:2 of the instant application (Column 2, lines 52-61). T107 of SEQ ID NO:1 of Hong corresponds to T107 of SEQ ID NO:2 of the instant application (see the sequence alignment below).
Regarding claim 1, Hong also discloses a transaminase mutant having the amino acid sequence of SEQ ID NO:28, which has an Ala residue at the position corresponding to 417 of SEQ ID NO:2 of the instant application and other amino acid differences compared to SEQ ID NO:2 of the instant application (Columns 97-100 and see the sequence alignment below).
Therefore, the reference of Hong anticipates claim 1.
The applied reference (US Patent No. 11,359,219) has a common inventor and assignee with the instant application. Based upon the earlier effectively filed date of the reference, it constitutes prior art under 35 U.S.C. 102(a)(2). This rejection under 35 U.S.C. 102(a)(2) might be overcome by: (1) a showing under 37 CFR 1.130(a) that the subject matter disclosed in the reference was obtained directly or indirectly from the inventor or a joint inventor of this application and is thus not prior art in accordance with 35 U.S.C. 102(b)(2)(A); (2) a showing under 37 CFR 1.130(b) of a prior public disclosure under 35 U.S.C. 102(b)(2)(B) if the same invention is not being claimed; or (3) a statement pursuant to 35 U.S.C. 102(b)(2)(C) establishing that, not later than the effective filing date of the claimed invention, the subject matter disclosed in the reference and the claimed invention were either owned by the same person or subject to an obligation of assignment to the same person or subject to a joint research agreement.
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.
Claim 1 is rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-18 of U.S. Patent No. 11,359,219 (reference patent).
Although the claims at issue are not identical, they are not patentably distinct from each other because they are claiming common subject matter, as follows:
MPEP 2111.01 states that ''[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow.'' Regarding claim 1, the limitation “mutant obtained from a mutation of amino acids of SEQ ID NO:2, the mutation of amino acid is selected from any one…” has been broadly interpreted to encompass any mutant transaminase of SEQ ID NO:2, wherein the transaminase mutant comprises an Ala residue at the position corresponding to T107 of SEQ ID NO: 2 of the instant application and any other amino acid differences compared to SEQ ID NO:2 of the instant application.
Regarding claim 1 of the instant application, claim 1 of the reference patent recites a transaminase mutant of SEQ ID NO:1, wherein the transaminase mutant has a T107A amino acid substitution and other amino acid differences compared to SEQ ID NO:2 of the instant application. T107 of SEQ ID NO:1 of the reference patent corresponds to T107 of SEQ ID NO:2 of the instant application (see the sequence alignment below).
Therefore, the conflicting claims are not patentably distinct from each other.
Conclusion
Claims 1-11 are pending.
Claims 2-11 are withdrawn.
Claim 1 is rejected.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to YONG D PAK whose telephone number is (571)272-0935. The examiner can normally be reached M-Th: 5:30 am - 3:30 pm.
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/YONG D PAK/Primary Examiner, Art Unit 1652
Sequence alignment between the transaminase of SEQ ID NO:1 of the instant application (“Qy”) and the transaminase of SEQ ID NO:1 of Foster (“Db”)
US-16-372-083-1
Filing date in PALM: 2019-04-01
Sequence 1, US/16372083
Publication No. US20190352682A1
GENERAL INFORMATION
APPLICANT: INVISTA NORTH AMERICA S.A.R.L.
TITLE OF INVENTION: MATERIALS AND METHODS FOR BIOSYNTHETIC MANUFACTURE OF
TITLE OF INVENTION: CARBON-BASED CHEMICALS
FILE REFERENCE: 061646-1131148 (00701US)
CURRENT APPLICATION NUMBER: US/16/372,083
CURRENT FILING DATE: 2019-04-01
PRIOR APPLICATION NUMBER: 62/650,642
PRIOR FILING DATE: 2018-03-30
NUMBER OF SEQ ID NOS: 9
SEQ ID NO 1
LENGTH: 459
TYPE: PRT
ORGANISM: Chromobacterium violaceum
Best Local Similarity 100.0%;
Matches 459; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MQKQRTTSQWRELDAAHHLHPFTDTASLNQAGARVMTRGEGVYLWDSEGNKIIDGMAGLW 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MQKQRTTSQWRELDAAHHLHPFTDTASLNQAGARVMTRGEGVYLWDSEGNKIIDGMAGLW 60
Qy 61 CVNVGYGRKDFAEAARRQMEELPFYNTFFKTTHPAVVELSSLLAEVTPAGFDRVFYTNSG 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 CVNVGYGRKDFAEAARRQMEELPFYNTFFKTTHPAVVELSSLLAEVTPAGFDRVFYTNSG 120
Qy 121 SESVDTMIRMVRRYWDVQGKPEKKTLIGRWNGYHGSTIGGASLGGMKYMHEQGDLPIPGM 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 SESVDTMIRMVRRYWDVQGKPEKKTLIGRWNGYHGSTIGGASLGGMKYMHEQGDLPIPGM 180
Qy 181 AHIEQPWWYKHGKDMTPDEFGVVAARWLEEKILEIGADKVAAFVGEPIQGAGGVIVPPAT 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 AHIEQPWWYKHGKDMTPDEFGVVAARWLEEKILEIGADKVAAFVGEPIQGAGGVIVPPAT 240
Qy 241 YWPEIERICRKYDVLLVADEVICGFGRTGEWFGHQHFGFQPDLFTAAKGLSSGYLPIGAV 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 YWPEIERICRKYDVLLVADEVICGFGRTGEWFGHQHFGFQPDLFTAAKGLSSGYLPIGAV 300
Qy 301 FVGKRVAEGLIAGGDFNHGFTYSGHPVCAAVAHANVAALRDEGIVQRVKDDIGPYMQKRW 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 FVGKRVAEGLIAGGDFNHGFTYSGHPVCAAVAHANVAALRDEGIVQRVKDDIGPYMQKRW 360
Qy 361 RETFSRFEHVDDVRGVGMVQAFTLVKNKAKRELFPDFGEIGTLCRDIFFRNNLIMRACGD 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 RETFSRFEHVDDVRGVGMVQAFTLVKNKAKRELFPDFGEIGTLCRDIFFRNNLIMRACGD 420
Qy 421 HIVSAPPLVMTRAEVDEMLAVAERCLEEFEQTLKARGLA 459
|||||||||||||||||||||||||||||||||||||||
Db 421 HIVSAPPLVMTRAEVDEMLAVAERCLEEFEQTLKARGLA 459
Sequence alignment between the transaminase of SEQ ID NO:2 of the instant application (“Qy”) and the transaminase of SEQ ID NO:1 of Hong (“Db”)
US-16-966-528-1
Sequence 1, US/16966528
Patent No. 11359219
GENERAL INFORMATION
APPLICANT: ASYMCHEM LIFE SCIENCE (TIANJIN) CO., LTD.
TITLE OF INVENTION: Transaminase Mutant and Application thereof
FILE REFERENCE: KP20148US
CURRENT APPLICATION NUMBER: US/16/966,528
CURRENT FILING DATE: 2020-07-31
PRIOR APPLICATION NUMBER: PCT/CN2018/075272
PRIOR FILING DATE: 2018-02-05
NUMBER OF SEQ ID NOS: 56
SEQ ID NO 1
LENGTH: 459
TYPE: PRT
ORGANISM: Chromobacterium violaceum
Query Match 97.7%; Score 2416; Length 459;
Best Local Similarity 98.0%;
Matches 450; Conservative 2; Mismatches 7; Indels 0; Gaps 0;
Qy 1 MQKQRTCSQWRELDAAHHLHPFTDTASLNQAGARVMTRGEGVYLWDCEGNKIIDGMAGLW 60
|||||| ||||||||||||||||||||||||||||||||||||||| |||||||||||||
Db 1 MQKQRTTSQWRELDAAHHLHPFTDTASLNQAGARVMTRGEGVYLWDSEGNKIIDGMAGLW 60
Qy 61 CVNVGYGRKDFAEAARRQMEELPFYNTFYKTTHPAVVELSSLLAEVTPAGFDRVFYTNSG 120
||||||||||||||||||||||||||||:|||||||||||||||||||||||||||||||
Db 61 CVNVGYGRKDFAEAARRQMEELPFYNTFFKTTHPAVVELSSLLAEVTPAGFDRVFYTNSG 120
Qy 121 SESVDTMIRMVRRYWDVQGKPEKKTLIGRWNGYHGSTIGGASLGGFKAMHEQGDLPIPGM 180
||||||||||||||||||||||||||||||||||||||||||||| | ||||||||||||
Db 121 SESVDTMIRMVRRYWDVQGKPEKKTLIGRWNGYHGSTIGGASLGGMKYMHEQGDLPIPGM 180
Qy 181 AHIEQPWWYKHGKDMTPDEFGVVAARWLEEKILEIGADKVAAFVGEPIQGAGGVIVPPAT 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 AHIEQPWWYKHGKDMTPDEFGVVAARWLEEKILEIGADKVAAFVGEPIQGAGGVIVPPAT 240
Qy 241 YWPEIERICRKYDVLLVADEVICGFGRTGEWFGHQHFGFQPDLFTAAKGLSSGYLPIGAV 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 YWPEIERICRKYDVLLVADEVICGFGRTGEWFGHQHFGFQPDLFTAAKGLSSGYLPIGAV 300
Qy 301 FVGKRVAEGLIAGGDFNHGFTYSGHPVCAAVAHANVAALRDEGIVQRVKDDIGPYMQKRW 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 FVGKRVAEGLIAGGDFNHGFTYSGHPVCAAVAHANVAALRDEGIVQRVKDDIGPYMQKRW 360
Qy 361 RETFSRFEHVDDVRGVGMALAFTLVKNKAKRELFPDFGEIGTLCRDIFFRNNLIMDSCGD 420
|||||||||||||||||| ||||||||||||||||||||||||||||||||||| :|||
Db 361 RETFSRFEHVDDVRGVGMVQAFTLVKNKAKRELFPDFGEIGTLCRDIFFRNNLIMTACGD 420
Qy 421 HIVSAPPLVMTRAEVDEMLAVAERCLEEFEQTLKARGLA 459
|||||||||||||||||||||||||||||||||||||||
Db 421 HIVSAPPLVMTRAEVDEMLAVAERCLEEFEQTLKARGLA 459
Sequence alignment between the transaminase of SEQ ID NO:2 of the instant application (“Qy”) and the transaminase of SEQ ID NO:28 of Hong (“Db”)
US-16-966-528-28
Sequence 28, US/16966528
Patent No. 11359219
GENERAL INFORMATION
APPLICANT: ASYMCHEM LIFE SCIENCE (TIANJIN) CO., LTD.
TITLE OF INVENTION: Transaminase Mutant and Application thereof
FILE REFERENCE: KP20148US
CURRENT APPLICATION NUMBER: US/16/966,528
CURRENT FILING DATE: 2020-07-31
PRIOR APPLICATION NUMBER: PCT/CN2018/075272
PRIOR FILING DATE: 2018-02-05
NUMBER OF SEQ ID NOS: 56
SEQ ID NO 28
LENGTH: 459
TYPE: PRT
ORGANISM: Chromobacterium violaceum
Query Match 98.8%; Score 2442; Length 459;
Best Local Similarity 98.7%;
Matches 453; Conservative 2; Mismatches 4; Indels 0; Gaps 0;
Qy 1 MQKQRTCSQWRELDAAHHLHPFTDTASLNQAGARVMTRGEGVYLWDCEGNKIIDGMAGLW 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MQKQRTCSQWRELDAAHHLHPFTDTASLNQAGARVMTRGEGVYLWDCEGNKIIDGMAGLW 60
Qy 61 CVNVGYGRKDFAEAARRQMEELPFYNTFYKTTHPAVVELSSLLAEVTPAGFDRVFYTNSG 120
||||||||||||||||||||||||||||:|||||||||||||||||||||||||||||||
Db 61 CVNVGYGRKDFAEAARRQMEELPFYNTFFKTTHPAVVELSSLLAEVTPAGFDRVFYTNSG 120
Qy 121 SESVDTMIRMVRRYWDVQGKPEKKTLIGRWNGYHGSTIGGASLGGFKAMHEQGDLPIPGM 180
||||||||||||||||||||||||||||||||||||||||||||| | ||||||||||||
Db 121 SESVDTMIRMVRRYWDVQGKPEKKTLIGRWNGYHGSTIGGASLGGMKYMHEQGDLPIPGM 180
Qy 181 AHIEQPWWYKHGKDMTPDEFGVVAARWLEEKILEIGADKVAAFVGEPIQGAGGVIVPPAT 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 AHIEQPWWYKHGKDMTPDEFGVVAARWLEEKILEIGADKVAAFVGEPIQGAGGVIVPPAT 240
Qy 241 YWPEIERICRKYDVLLVADEVICGFGRTGEWFGHQHFGFQPDLFTAAKGLSSGYLPIGAV 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 YWPEIERICRKYDVLLVADEVICGFGRTGEWFGHQHFGFQPDLFTAAKGLSSGYLPIGAV 300
Qy 301 FVGKRVAEGLIAGGDFNHGFTYSGHPVCAAVAHANVAALRDEGIVQRVKDDIGPYMQKRW 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 FVGKRVAEGLIAGGDFNHGFTYSGHPVCAAVAHANVAALRDEGIVQRVKDDIGPYMQKRW 360
Qy 361 RETFSRFEHVDDVRGVGMALAFTLVKNKAKRELFPDFGEIGTLCRDIFFRNNLIMDSCGD 420
|||||||||||||||||| |||||||||||||||||||||||||||||||||||| :|||
Db 361 RETFSRFEHVDDVRGVGMVLAFTLVKNKAKRELFPDFGEIGTLCRDIFFRNNLIMTACGD 420
Qy 421 HIVSAPPLVMTRAEVDEMLAVAERCLEEFEQTLKARGLA 459
|||||||||||||||||||||||||||||||||||||||
Db 421 HIVSAPPLVMTRAEVDEMLAVAERCLEEFEQTLKARGLA 459