DETAILED ACTION
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 .
Claims Status
Claims 1-6 are pending.
Information Disclosure Statement
The information disclosure statements (IDS) submitted on 11/15/2024, 11/19/2025 and 11/25/2025 is acknowledged. The submission is in compliance with the provision of 37 CFR 1.97. Accordingly, the information disclosure statements have been considered.
Claim Objections
Claim 5 objected to because of the following informalities:
Dependent claims 2-4 recite “The microorganism of the genus Corynebacterium of claim 1”. Claim 5 recites “the microorganism of claim 1”. It is suggested that applicants maintain consistency unless there is reason for the different language used by the different dependent claims. 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.
Claims 1-6 are 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.
With regards to claim 1 (and claims 2-5 dependent thereon) and claim 6, claim 1 claim recites “wherein the activity of a gluconate repressor protein is weakened” and claim 6 recites “the gluconate repressor protein activity is weakened”. The term “activity” is unclear in the absence of the specific activity associated with the protein. As known in the art, a protein can have more than one activity such as enzymatic activity, binding activity, regulatory activity, kinetic activity, etc. Furthermore, it is also unclear what the scope is and what is encompassed by the term “weakened” as it relates to the activity of the protein. The term “weakened” can refer to reducing the binding strength, kinetics, substrate turnover, enzymatic activity, etc.. Therefore, the claims are rendered indefinite. In the interest of compact prosecution, the Examiner is interpreting “activity” as any activity of the protein and “weakened” as any reduction of any activity of the protein.
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.
Claims 1-6 are 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 applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention. As stated in MPEP 211.01, during examination, the claims must be interpreted as broadly as their terms reasonably allow. Claims 1-6 require a genus of unknown modifications to weaken the activity of a gluconate repressor protein.
In University of California v. Eli Lilly & Co., 43 USPQ2d 1938, the Court of Appeals for the Federal circuit has held that “A written description of an invention involving a chemical genus, like a description of a chemical species, requires a precise definition such as by structure, formula, [or] chemical name, of the claimed subject matter sufficient to distinguish it from other materials. As indicated in MPEP § 2163, 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, 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 that Applicant was in possession of the claimed genus. In addition, MPEP § 2163 states that a representative number of species means that the species which are adequately described are representative of the entire genus. Thus, where there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
Claim 1 (and claims 2-5 dependent thereon) is directed to all possible microorganisms of the genus Corynebacterium, wherein the activity of a gluconate repressor protein is weakened by any means. There is no disclosure of any particular structure to function/activity relationship of the disclosed species.
Claim 6 is directed to all possible methods for producing L-arginine in which the gluconate repressor protein activity is weakened by any means. There is no disclosure of any particular structure to function/activity relationship of the disclosed species.
The prior art has identified two paralogous GntR-type regulators in C. glutamicum, designated GntR1 and GntR2 which repress the expression of genes involved in gluconate metabolism in the absence of gluconate. GntR1 and GntR2 of C. glutamicum consists of an N-terminal GntR-type helix-turn-helix motif responsible for DNA binding and a C-terminal putative ligand binding domain Frunzke et al. Molecular Microbiology, Vol. 67, pg. 305-322, published November 6, 2007 (see pg. 307). The prior art teaches that simultaneous absence of GntR1 and GntR2 is responsible for the reduced growth rate in glucose minimal medium and indicates that GntR1 and GntR2 can replace each other (see pg. 307). The prior art also teaches that GntR1 and GntR2 act as repressors of genes required for gluconate catabolism (see pg. 308). The prior art also teaches that microarray experiments identified gntP, gntK, ptsG, ptsS and the gene cluster tkt-tal-zwf-opcA-devB as putative target genes of GntR1 and GntR2. Analysis of interactions of GntR1 and GntR2 with the promoter regions of these genes incubated with purified GntR1 and GntR2 showed shifts in the native polyacrylamide gels with both GntR1 and GntR2. The formation of multiple GntR/DNA complexes was also observed with all tested promoter regions. This indicates the presence of several GntR1/2 binding motifs (see sp. 311). GntR1 and GntR2 are transcriptional regulators that are important players in a complex regulatory network that controls uptake and metabolism of carbon sources in C. glutamicum in order to allow the most favorable combination of the available substrates (see pg. 317).
The claims encompass a potentially large genus of unknown methods to reduce the activity/expression of a gluconate repressor protein such as (a) mutations of the regulatory region of a gene encoding the protein of interest, (b) mutations in the coding region of a gene encoding the protein of interest such that the activity is weakened, (c) the use of antisense oligonucleotides of unknown structure that would block the expression of the desired genes, and (d) the use of antisense oligonucleotides of unknown structure that would block the expression of unknown genes encoding inducers of the genes encoding the gluconate repressor protein.
Regarding the level of skill and knowledge in the art of amino acid mutation, the reference of Singh et al., (Curr. Protein Pept. Sci. 18:1-11, 2017; cited on the attached PTO0-892) 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 pg. 7, column 1, top). Also, the unpredictability associated with amino acid mutations is exemplified by the reference of Zhang et al. (Structure 26: 1474-1485, 2018, cited on the attached Form PTO-82) which discloses that even a mutation 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 this lack of additional representative species as encompassed by the claims, Applicants have failed to sufficiently describe the claimed invention, in such full, clear, concise, and exact terms that a skilled artisan would recognize Applicants were in possession of the claimed invention.
Claims 1-6 are 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 a microorganism of the genus Corynebacterium wherein the activity of a gluconate repressor protein (claim 1 and claim 6) consisting of SEQ ID NO: 1 (claim 3), is weakened does not reasonably provide enablement for all possible microorganisms of the genus Corynebacterium, wherein the activity of a gluconate repressor protein is weakened.
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/or 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 USPQ 2nd 1400 (Fed. Cir. 1988)) as follows: (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 claim(s).
Claims 1 (and claims 2-5 dependent on) and 6 are so broad as to encompass all possible microorganisms of the genus Corynebacterium, wherein the activity of a gluconate repressor protein is weakened. The scope of the claim is not commensurate with the enablement provided by the disclosure with regard to the extremely large number of all possible microorganisms of the genus Corynebacterium wherein the activity of a gluconate repressor protein is weakened.
The claims rejected under this section of U.S.C. 112, first paragraph, place minimal structural limits on the required variant polypeptides of the gluconate repressor protein or modifications to genes affecting the gluconate repressor protein or chemical structures of small molecule compounds that inhibit the activity of the gluconate repressor protein in the microorganism encompassed by the claims. Since the amino acid sequence of a protein 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. However, in this case the disclosure is limited to:
Claim 1 (and claims 2-5 dependent on and claim 6) a microorganism of the genus Corynebacterium wherein the activity of a gluconate repressor protein (having an amino acid sequence of SEQ ID NO. 1) is weakened. The specification refers to weakening to include a case in which the activity of the polypeptide is reduced or eliminated compared with the activity of the polypeptide originally possessed by the microorganism due to mutation in the polynucleotide encoding the microorganism (see specification, pg. 8). The specification only provides such examples deleting all or a portion of the gene encoding the polypeptide, modifying an expression region so as to reduce the expression of the gene encoding the polypeptide, or modifications to SEQ ID NO:1 at positions 36, 59, 60, 63, 79, 92 (see specification pg. 16-17).
While recombinant and mutagenesis techniques are known, it is not routine in the art to screen for multiple substitutions or multiple modifications, as encompassed by the instant claims, and the positions within a 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. Additionally, it is not routine to screen for multiple gene modifications, deletions, or alterations. In addition, one skilled in the art would expect any tolerance to modification for a given protein or gene to diminish with each further and additional modification, e.g. multiple substitutions.
The specification does not support the broad scope of the claims which encompass any possible:
(Claim 1 (and claims 2-5 dependent thereon and claim 6) microorganisms of the genus Corynebacterium, wherein the activity of a gluconate repressor protein is weakened. The scope of the claim is not commensurate with the enablement provided by the disclosure with regard to the extremely large number of all possible microorganisms of the genus Corynebacterium wherein the activity of a gluconate repressor protein is weakened because the specification does not disclose (A) regions of the polypeptide which may be modified to weaken the activity of the gluconate repressor protein, gene deletions that may affect the encoding of the polypeptide, modifications of promoters affecting the expression of the gluconate repressor protein, or chemical structures of compounds that can be used to inhibit expression of the protein of interest or activity of the protein of interest (B) the general tolerance of enzymes or genes of the gluconate repressor protein to modification and extent of such tolerance to achieve weakened activity; (C) a rational and predictable scheme for modifying any amino acid residue of the gluconate repressor protein with an expectation of obtaining a gluconate repressor protein with weakened activity, deletions or modifications of the nucleic acid encoding the gluconate repressor protein that can weaken the activity or affection expression the gluconate repressor protein, or promoters affecting the expression of the gluconate repressor gene; or determination of structures of small molecule compounds that inhibit the activity of the gluconate repressor protein and (D) the specification provides insufficient guidance as to which of the essentially infinite possible choices is likely to be successful. Because of this lack of guidance, the extended experimentation that would be required to determine which substitutions, gene alterations, that would be acceptable to retain the required functions of the gluconate repressor protein and the fact that the relationship between the sequence of a peptide and its tertiary structure (i.e. its activity) are not well understood and are not predictable (e.g., see Ngo et al. in The Protein Folding Problem and Tertiary Structure Prediction, 1994, Merz et al. (ed.), Birkhauser, Boston, MA, pp. 433 and 492-495; Franceus et al., J. Ind. Microbiol. Biotechnol. Vol 44, pp 687-695, 2017) and that the relationship between transcription factors and genes may be much more complex than we know (see Zhou et al. (Cell Mol. Life Sci. Vol 63, pg. 2260-2290, published 2006), it would require undue experimentation for one skilled in the art to arrive at the majority of polypeptides having the function of the gluconate repressor protein, determination of small molecule chemical compounds or nucleic acids which can serve as transcription repressors of genes or inhibitors of activity, or all possible mutations to the regulatory or coding regions of a gene to determine which ones would result in the decrease of expression/activity of the desired protein of the claimed genus.
Thus, applicants have not provided sufficient guidance to enable one of ordinary skill in the art to make and use the claimed invention in a manner reasonably correlated with the scope of the claims broadly including any:
(Claim 1 (and claims 2-5 dependent thereon and claim 6) possible microorganisms of the genus Corynebacterium, wherein the activity of a gluconate repressor protein is weakened. The scope of the claim is not commensurate with the enablement provided by the disclosure with regard to the extremely large number of all possible microorganisms of the genus Corynebacterium wherein the activity of a gluconate repressor protein is weakened
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:
(Claim 1 (and claims 2-5 dependent thereon and claim 6) all possible microorganisms of the genus Corynebacterium, wherein the activity of a gluconate repressor protein is weakened. The scope of the claim is not commensurate with the enablement provided by the disclosure with regard to the extremely large number of all possible microorganisms of the genus Corynebacterium wherein the activity of a gluconate repressor protein is weakened, is 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 (i.e., changing from AIA to pre-AIA ) 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.
Claims 1, 2, 4, and 6 are rejected under 35 U.S.C. 102(a)1() and 102(a)(2) as being anticipated by Hara et al. (US Patent Application Publication No. US 2016/0130618 A1; published May 12, 2016), hereinafter referred to as Hara.
With regards to claims 1, 2, 4, and 6, Hara discloses a Corynebacterium glutamicum that is modified to have a reduced activity of GntR (gluconate repressor protein). Hara discloses that GntR refers to a transcription factor which negatively regulates the expression of an operon encoding gluconate metabolic genes (see paragraphs, 0044, 0045, and 0229). Hara further discloses culturing the microorganism in a medium (see paragraph 0532 and 0532).
Claims 2 and 6 are further included in the rejection based on the inherent ability of Corynebacterium glutamicum to produce L-arginine through the L-arginine biosynthesis pathway as evidenced by Zhan et al. (Journal of Industrial Microbiology & Biotechnology, Vol. 46: pg. 45-54, published 2019), (see pg. 45-46).
Therefore, claims 1, 2, 4 and 6 are rejected under 35 U.S.C. 102(a)1() and 102(a)(2) as being anticipated by Hara et al. (US Patent Application Publication No. US 2016/0130618 A1; published May 12, 2016).
Claim Rejections - 35 USC § 103
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 (i.e., changing from AIA to pre-AIA ) 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 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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claim 3 is rejected under 35 U.S.C. 103 as being unpatentable over Hara et al. (US Patent Application Publication No. US 2016/0130618 A1; published May 12, 2016), hereinafter referred to as Hara as applied to claim 1 above, and further in view of UniProt Database Entry A0A0F6WRA7_9CORY; integrated into UniProtKB/TrEMBL July 22, 2015), hereinafter referred to as UniProt.
The teachings of Hara as applied to claim 1 are summarized above.
With respect to claim 3, Hara does not specifically teach that the gluconate repressor protein consists of the amino acid sequence of SEQ ID NO: 1.
However, Uniprot teaches a Corynebacterium GntR transcription regulator (gluconate repressor protein) having an amino acid sequence that is 100% identical to SEQ ID NO. 1 of the current instant application (see sequence alignment below).
RESULT 1
A0A0F6WRA7_9CORY
ID A0A0F6WRA7_9CORY Unreviewed; 250 AA.
AC A0A0F6WRA7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 08-OCT-2025, entry version 35.
DE SubName: Full=Transcriptional regulator {ECO:0000313|EMBL:AKF28326.1};
GN ORFNames=YH66_12685 {ECO:0000313|EMBL:AKF28326.1};
OS [Brevibacterium] flavum.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=92706 {ECO:0000313|EMBL:AKF28326.1, ECO:0000313|Proteomes:UP000034037};
RN [1] {ECO:0000313|EMBL:AKF28326.1, ECO:0000313|Proteomes:UP000034037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15168 {ECO:0000313|EMBL:AKF28326.1,
RC ECO:0000313|Proteomes:UP000034037};
RA Ahn J., Park G., Jeon W., Jang Y., Jang M., Lee H., Lee H.;
RT "Complete Genome Sequence of Brevibacterium flavum ATCC 15168.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP011309; AKF28326.1; -; Genomic_DNA.
DR RefSeq; WP_003860283.1; NZ_CP011309.1.
DR AlphaFoldDB; A0A0F6WRA7; -.
DR PATRIC; fig|92706.3.peg.2659; -.
DR HOGENOM; CLU_017584_9_4_11; -.
DR Proteomes; UP000034037; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR Gene3D; 1.20.120.530; GntR ligand-binding domain-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011711; GntR_C.
DR InterPro; IPR008920; TF_FadR/GntR_C.
DR InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR43537:SF44; GNTR FAMILY REGULATORY PROTEIN; 1.
DR PANTHER; PTHR43537; TRANSCRIPTIONAL REGULATOR, GNTR FAMILY; 1.
DR Pfam; PF07729; FCD; 1.
DR Pfam; PF00392; GntR; 1.
DR SMART; SM00895; FCD; 1.
DR SMART; SM00345; HTH_GNTR; 1.
DR SUPFAM; SSF48008; GntR ligand-binding domain-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50949; HTH_GNTR; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Reference proteome {ECO:0000313|Proteomes:UP000034037};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 21..88
FT /note="HTH gntR-type"
FT /evidence="ECO:0000259|PROSITE:PS50949"
SQ SEQUENCE 250 AA; 27219 MW; 95C7D19D3B152EAD CRC64;
Query Match 100.0%; Score 1243; Length 250;
Best Local Similarity 100.0%;
Matches 250; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MPPANESPMTNPLGSAPTPAKPLLDSVLDELGQDIISGKVAVGDTFKLMDIGERFGISRT 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MPPANESPMTNPLGSAPTPAKPLLDSVLDELGQDIISGKVAVGDTFKLMDIGERFGISRT 60
Qy 61 VAREAMRALEQLGLVASSRRIGITVLPQEEWAVFDKSIIRWRLNDEGQREGQLQSLTELR 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 VAREAMRALEQLGLVASSRRIGITVLPQEEWAVFDKSIIRWRLNDEGQREGQLQSLTELR 120
Qy 121 IAIEPIAARSVALHASTAELEKIRALATEMRQLGESGQGASQRFLEADVTFHELILRYCH 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 IAIEPIAARSVALHASTAELEKIRALATEMRQLGESGQGASQRFLEADVTFHELILRYCH 180
Qy 181 NEMFAALIPSISAVLVGRTELGLQPDLPAHEALDNHDKLADALLNRDADAAETASRNILN 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 NEMFAALIPSISAVLVGRTELGLQPDLPAHEALDNHDKLADALLNRDADAAETASRNILN 240
Qy 241 EVRSALGTLN 250
||||||||||
Db 241 EVRSALGTLN 250
It would have been obvious to one of ordinary skill in the art of protein engineering before the effective filing date of the current instant application to use the Corynebacterium GntR (gluconate repressor protein) taught by Uniprot as the gluconate repressor protein in the Corynebacterium microorganism taught by Hara. One of ordinary skill in the art would be motivated to do so since UniProt teaches that the GntR (gluconate repressor protein) is from Corynebacterium and thus would be compatible in the Corynebacterium microorganism taught by Hara. One of ordinary skill in the art of protein engineering would have expectations of success in doing so from the combined teachings of Hara and UniProt who provide all the teachings needed to do so.
Claim 3 is rejected under 35 U.S.C. 103 as being unpatentable over Hara et al. (US Patent Application Publication No. US 2016/0130618 A1; published May 12, 2016) and further in view of UniProt Database Entry A0A0F6WRA7_9CORY; integrated into UniProtKB/TrEMBL July 22, 2015).
The prior art made of record and not relied upon is considered pertinent to applicant’s disclosure:
Park et al. US Patent No. US 10,253,229 B2; published April 9, 2019.
The patent discloses a Corynebacterium glutamicum microorganism that has a novel variant gluconate repressor 1 (GntR1) that produces L-lysine compared to the microorganism comprising a wild-type gluconate repressor 1 and has enhanced L-lysine productivity. The patent does not disclose or teach Corynebacterium glutamicum with improved L-arginine producing ability.
Conclusion
No claims are allowed.
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/GEORGE THEMISTOCLIS LOUNTOS/ Examiner, Art Unit 1652
/ROBERT B MONDESI/ Supervisory Patent Examiner, Art Unit 1652
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