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 .
Priority
This application is a 371 of PCT/KR2020/003317 filed 03/10/2020. 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.
Acknowledgment is made of applicant’s claim for foreign priority under 35 U.S.C. 119 (a)-(d) to KR10-2019-0046934 filed 04/22/2019. Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55.
Status of the Claims
Applicant’s amendment filed on 09/25/2025 is acknowledged.
Claims 1, 5-8, 10, 11, 13-19 and 21-24 are pending. Claims 1, 6, 8 and 13-18 are amended. Claims 4 and 20 are cancelled. Claim 11 is withdrawn.
Claims 1, 5-8, 10, 13-19 and 21-24 (claim set filed 09/25/2025) and are examined on the merits herein.
Terminal Disclaimer
The terminal disclaimer filed on 09/25/2025 disclaiming the terminal portion of any patent granted on this application which would extend beyond the expiration date of any patent granted on Application number 17/600,594 has been reviewed and is accepted. The terminal disclaimer has been recorded.
Withdrawal of Rejections
The response and amendment filed on 09/25/2025 are acknowledged. All of the amendment and arguments have been thoroughly reviewed and considered.
For the purposes of clarity of the record, the reasons for the Examiner's withdrawal and/or maintaining if applicable, of the substantive or essential claim rejections are detailed directly below and/or in the Examiner's response to arguments section.
The previous claims 1, 4-8, 10 and 13-24 rejection under 35 U.S.C. 112(a) (pages 4-6 of the previous Office Action) has been withdrawn necessitated by amendment of claim 1 and cancellation of claims 4 and 20.
The previous claims 4, 8 and 13-17 rejection under 35 U.S.C. 112(a) (pages 6-8 of the previous Office Action) has been withdrawn necessitated by amendment of claim 1 and cancellation of claim 4.
The previous claims 18-20 rejection under 35 U.S.C. 112(a) (pages 8-10 of the previous Office Action) has been withdrawn necessitated by amendment of claim 18 and cancellation of claim 20.
The previous Double Patenting rejection of claims 1, 4-8, 8- 10 and 13-24 has been withdrawn necessitated by Applicant ’s submission of Terminal Disclaimer.
Maintained/Modified Rejections
The following rejections are maintained and/or modified taking into consideration amendment
to claims filed on 09/25/2025.
Claim Rejections - 35 USC § 112
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 5-7 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.
Claims 5-7, are directed to the microorganism with enhanced activity of glycine cleavage protein wherein glycine cleavage protein comprises one or more proteins from the recited group and is derived from Corynebacterium ammoniagenes. Thus, claims broadly encompass genus of glycine cleavage proteins from C. ammoniagenes and their variants that have function of enhanced glycine cleavage activity. The structure function relationship for the glycine cleavage proteins is not provided in the specification and it is not described what core structure of glycine cleavage protein is needed to exhibit the enhanced activity. The specification does not provide examples of the representative number of species for functionally active glycine cleavage proteins except single species for each glycine cleavage protein and specific sequences are not presented in claims 5-7.
Thus, one of ordinary skill in the art would conclude based on the lack of representative number
of species and the lack of describing the structure function correlation for glycine cleavage proteins that the Applicant was not is possession of the claimed genus and that the specification fails to satisfy the requirements of written description under 35 U.S.C. 112 (a).
Response to Arguments
The 35 U.S.C. 112(a) rejections set forth on pages 6-8 and 8-10 of the previous office action are withdrawn as described above.
Regarding the 35 U.S.C. 112(a) rejection set forth on pages 4-6 of previous office action: amendment of claim 1 satisfies the written description for CycA glycine transporter protein for claim 1 and dependent claims, however, that amendment does not resolve the issue of written description for glycine cleavage proteins in claims 5-7. The 35 U.S.C. 112(a) rejection for claims 5-7 is maintained as described above.
Claim Rejections - 35 USC § 103
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claims 1, 10, 17 and 21-24 are rejected under 35 U.S.C. 103 as being unpatentable over Kirchner (Kirchner and Tauch J. Biotechnol., 2003, 287-299 on record in IDS) in view of Stauffer (Stauffer ASMScience/EcoSalPlus, 2013, doi:10.1128/ecosalplus.3.6.1.2) and Liu (Liu et al. J. Biotechnol., 2016, 225, 57-58) as evidenced by Yang_1 (Yang_1 and Yang Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences (SIBS) of Chinese Academy of Sciences (CAS), 2016, pp. 1-2, [retrieved on 11/04/2024]. Retrieved from the Internet: <Corynebacterium stationis strain ATCC 6872 chromosome, complete genome - Nucleotide – NCBI (nih.gov)>).
Regarding claim 1 and 17, Kirchner teaches Corynebacterium glutamicum to be used as a producer of L-amino acids: “During the last decades, the gram-positive soil bacterium Corynebacterium glutamicum has been shown to be a very versatile microorganism for the large-scale fermentative production of L-amino acids.” (Abstract). The production properties of C. glutamicum strains are improved by genetic engineering. Kirchner describes techniques and tools for genetic engineering of C. glutamicum (Abstract).
Kirchner does not teach enhancement of glycine transporter activity in the microorganism and the glycine transporter to comprise CycA protein derived from C. ammoniagenes and comprising the amino acid sequence of SEQ ID NO: 1.
Stauffer teaches one-carbon units (C1) derived from glycine to be involved in synthesis of different metabolites including histidine: “…C1 units derived from serine and glycine are used in the synthesis of purines, histidine, thymine, pantothenate, and methionine…” (Abstract). Stauffer discusses the major route for glycine transport in E. coli, glycine transport system (Cyc): “The E. coli glycine transport system (Cyc) has been shown to transport glycine, D-alanine, D-serine, and the antibiotic D-cycloserine (240, 241, 242). This is the major route of glycine transport…” (p. 15, right column, 3rd paragraph).
Liu teaches complete annotated genome sequence of C. stationis ATCC 6872 (Abstract). Liu mentions that C. ammoniagenes was reassigned as C. stationis (p. 57, left column, 1st paragraph). Additionally, the specification teaches that C. ammoniagenes and C. stationis are the same species and can be used interchangeably: “Accordingly, as used herein, the terms Corynebacterium ammoniagenes, Brevibacterium ammoniagenes, Corynebacterium stationis, and Brevibacterium stationis may be used interchangeably.” (p. 3, last two paragraphs). Liu discloses that: “The genome sequence of ATCC 6872 has been deposited in the GenBank database under accession number CP014279” (p. 57, right column, last paragraph). C. stationis ATCC 6872 has CycA gene as evidenced by Yang_1 (p. 2, line 15). Yang_1 shows that the CycA gene from C. stationis ATCC 6872 encodes D-serine/D-alanine/glycine transporter (p. 2, line 33). The amino acid sequence of CycA protein encoded by the C. stationis ATCC 6872 of Liu teaching has 100% identity to instant SEQ ID NO:1 as evidenced by Yang_1.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to combine teachings of Kirchner and Stauffer and introduce glycine transporter system from Stauffer teaching into C. glutamicum by genetic engineering methods described by Kirchner. One would have been motivated to make this combination since Stauffer discloses necessity of glycine for synthesis of different metabolites including amino acids and L-histidine and Kirchner teaches C. glutamicum to be used as amino acid producer. A skilled artisan would have reasonably expected success in this combination since Kirchner provides methods of C. glutamicum genetic modification and Stauffer pointed to the participation of glycine in histidine biosynthesis and to glycine transporter providing glycine supply in bacterial cell.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to combine teachings of Kirchner and Stauffer on genetic modification of C. glutamicum and introduction of glycine transporter and use glycine transporter from C. ammoniagenes (stationis) from Liu teaching with sequence 100% identical to instant SEQ ID NO:1. One would have been motivated to make this combination since Liu teaches annotated genome of bacterium from the same Corynebacterium genus and which has annotated CycA gene for glycine transporter and sequence for CycA protein as evidenced by Yang_1. A skilled artisan would have reasonably expected success in this combination since Kirchner provides methods of C. glutamicum genetic modification, Stauffer pointed to the role of glycine transporter and Liu provided gene and sequence for the C. ammoniagenes glycine transporter. Thus, combination of Kirchner, Stauffer and Liu teachings as evidenced by Yang_1 renders claims 1 and 17 obvious.
Regarding claim 10, Kirchner teaches expression of modified genes and production of metabolites: “These genetic tools allowed the cloning, expression, disruption, and replacement of C. glutamicum genes and the investigation of those metabolic pathways, which are relevant for improved amino acid production” (p. 288, left column, last paragraph) which is performed with modified microorganism being cultured in media and hence being present in a composition. Note the recitation “for producing histidine” is interpreted as a recitation of intended use. The recitation of intended use is given weight to the extent that it imparts a structural limitation and the prior art needs to be capable of performing the intended use. (MPEP 2111.02). Since there is no indication that the recitation can impart the structural difference between the claimed invention and the prior art, the prior is capable of performing the intended use. In instant case, the prior art renders the instantly claimed microorganism obvious and therefore, claim 10 is obvious. Thus, Kirchner, Stauffer and Liu teachings as evidenced by Yang_1 render claim 10 obvious.
Regarding claims 21 and 22, the histidine producing ability of the microorganism is interpreted as intended use that does not impart the structure as described above. The recited in claims 21 and 22 increase in the histidine producing ability of the microorganism is a further limitation of the intended use. Therefore, the microorganism taught by prior art of Kirchner, Stauffer and Liu is capable to have 4.3% and from 4.3 to 20.9% increase in an L-histidine producing ability compared to endogenous activity. Thus, Kirchner, Stauffer and Liu teachings as evidenced by Yang_1 render claims 21 and 22 obvious.
Regarding claims 23 and 24, decrease in a L-glycine producing ability of the microorganism is interpreted as intended use. The recitation of intended use is given weight to the extent that it imparts a structural limitation and the prior art needs to be capable of performing the intended use. (MPEP 2111.02). Since there is no indication that the recitation can impart the structural difference between the claimed invention and the prior art, the prior it is capable of performing the intended use. In instant case, the art renders the instantly claimed microorganism obvious and therefore, the microorganism taught by prior art of Kirchner, Stauffer and Liu is capable to have 10.6% and from 10.6 to 14% decrease in an L-glycine producing ability compared to endogenous activity. Thus, Kirchner, Stauffer and Liu teachings as evidenced by Yang_1 render claims 23 and 24 obvious.
Claims 18 and 19 are rejected under 35 U.S.C. 103 as being unpatentable over Kirchner (Kirchner and Tauch J. Biotechnol., 2003, 287-299 on record in IDS) in view of Stauffer (Stauffer ASMScience/EcoSalPlus, 2013, doi:10.1128/ecosalplus.3.6.1.2) and Liu (Liu et al. J. Biotechnol., 2016, 225, 57-58 as evidenced by Yang_1 (Yang_1 and Yang Institute of Plant Physiology and Ecology, Shanghai Institute for Biological Sciences (SIBS) of Chinese Academy of Sciences (CAS), 2016, pp. 1-2 [retrieved on 11/04/2024]. Retrieved from the Internet: <Corynebacterium stationis strain ATCC 6872 chromosome, complete genome - Nucleotide - NCBI (nih.gov)>) as applied to claim 1 above, and further in view of Zhao (Zhao et al. Appl. Microbiol. Biotechnol., 2011, 90, 2005-2013).
Teachings of Kirchner, Stauffer, Liu and Yang_1 have been set forth above.
Kirchner, Stauffer, Liu and Yang_1 do not teach inactivation of enzymatic activity of gamma-aminobutyrate permease, formyl tetrahydrofolate deformylase and/or transposase.
Regarding claims 18 and 19, Zhao teaches gene ncgl1108 to encode L-phenylalanine transporter in C. glutamicum (Abstract). Gene NCgl1108 encodes gamma-aminobutyrate permease according to claim 19 and specification (p. 12, 2nd paragraph). Zhao describes genetic disruption of NCgl1108 that resulted in decreased growth only on L-Phe and significant reduction of L-Phe uptake. At the same time the modified C. glutamicum growth on L-Trp and L-Tyr was not affected (Abstract).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to follow guidance of Zhao on the function of gamma-aminobutyrate permease encoded by Ncgl1108 gene and use these gene as the site for genetic manipulation, i.e. insertion of the glycine transporter gene from C. ammoniagenes for modification C. glutamicum to enhance production of amino acid based on teachings of Kirchner, Stauffer and Liu. It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention that insertion of the glycine transporter gene will result in the inactivation of enzymatic activity of gamma-aminobutyrate permease. One would have been motivated to make this combination since Zhao described function of Ncgl1108 gene as L-Phe transporter which is not involved in L-histidine biosynthesis, used the same bacterial species, C. glutamicum, and showed that C. glutamicum having disrupted Ncgl1108 gene can grow on L-Trp or L-Tyr. A skilled artisan would have reasonably expected success in this combination since Kirchner provides methods of C. glutamicum genetic modification, Zhao described site for modification, Stauffer pointed to the role of glycine transporter and Liu provided gene and sequence for the C. ammoniagenes glycine transporter. Thus, combination of Kirchner, Stauffer, Liu and Zhao teachings as evidenced by Yang_1 renders claims 18 and 19 obvious.
Claims 5-8 and 13-16 are rejected under 35 U.S.C. 103 as being unpatentable over Kirchner (Kirchner and Tauch J. Biotechnol., 2003, 287-299 on record in IDS) in view of Stauffer (Stauffer ASMScience/EcoSalPlus, 2013, doi:10.1128/ecosalplus.3.6.1.2) and Liu (Liu et al. J. Biotechnol., 2016, 225, 57-58 as evidenced by Yang_1 (Yang_1 and Yang Institute of Plant Physiology and Ecology, Shanghai Institute for Biological Sciences (SIBS) of Chinese Academy of Sciences (CAS), 2016, pp. 1-2 [retrieved on 11/04/2024]. Retrieved from the Internet: <Corynebacterium stationis strain ATCC 6872 chromosome, complete genome - Nucleotide - NCBI (nih.gov)>) as applied to claim 1 above, and further in view of Ochrombel (US 20170051324 A1) as evidenced by Yang_2 (Yang_2 and Yang Institute of Plant Physiology and Ecology, Shanghai Institute for Biological Sciences (SIBS) of Chinese Academy of Sciences (CAS), 2016, pp. 1-2 [retrieved on 11/04/2024]. Retrieved from the Internet: <Corynebacterium stationis strain ATCC 6872 chromosome, complete genome - Nucleotide - NCBI (nih.gov)>), Yang_3 (Yang_3 and Yang Institute of Plant Physiology and Ecology, Shanghai Institute for Biological Sciences (SIBS) of Chinese Academy of Sciences (CAS), 2016, pp. 1-2 [retrieved on 11/04/2024]. Retrieved from the Internet: <Corynebacterium stationis strain ATCC 6872 chromosome, complete genome - Nucleotide – NCBI (nih.gov)>), Yang_4 (Yang_4 and Yang Institute of Plant Physiology and Ecology, Shanghai Institute for Biological Sciences (SIBS) of Chinese Academy of Sciences (CAS), 2016, pp. 1-2 [retrieved on 11/04/2024]. Retrieved from the Internet: <Corynebacterium stationis strain ATCC 6872 chromosome, complete genome - Nucleotide - NCBI (nih.gov)>), Yang_5 (Yang_5 and Yang Institute of Plant Physiology and Ecology, Shanghai Institute for Biological Sciences (SIBS) of Chinese Academy of Sciences (CAS), 2016, pp. 1-2 [retrieved on 11/04/2024]. Retrieved from the Internet: <Corynebacterium stationis strain ATCC 6872 chromosome, complete genome - Nucleotide - NCBI (nih.gov)>) and Yang_6 (Yang_6 and Yang Institute of Plant Physiology and Ecology, Shanghai Institute for Biological Sciences (SIBS) of Chinese Academy of Sciences (CAS), 2016, pp. 1-2 [retrieved on 11/04/2024]. Retrieved from the Internet: <Corynebacterium stationis strain ATCC 6872 chromosome, complete genome - Nucleotide - NCBI (nih.gov)>).
Teachings of Kirchner, Stauffer, Liu and Yang_1 have been set forth above.
Kirchner, Stauffer, Liu and Yang_1 do not teach activity of glycine cleavage protein enhanced.
Regarding claims 5 and 6, Ochrombel teaches method for producing L-amino acids in Corynebacterium using glycine cleavage system (Title). Ochrombel discloses that the yield of produced -L-amino acids is increased by glycine cleavage system: “It has also been found that the yield of L-amino acid may be further increased by using a glycine cleavage system (GCV), since the formation of the undesired L-glycine by-product can be largely prevented by the glycine cleavage system” (paragraph 0004). Ochrombel describes that the glycine cleavage system is a multi-enzyme complex composed of two or more subunits, such as GcvP, GcvT and GcvH (paragraph 0005) that corresponds to claim 6 limitation. Ochrombel discloses other enzyme belonging to glycine cleavage system: “… the enzymes LpdA, LplA, LipA, LipB and GcvH also belong to the glycine cleavage system.” (paragraph 0030). Ochrombel mentions that the glycine cleavage system is not present in C. glutamicum and can be incorporated from another Corynebacterium: “…the production strain C. glutamicum particularly preferred for amino acid production, for example, has no inherent glycine cleavage system. In order to utilize the advantages of a glycine cleavage system for C. glutamicum , such a system had to be incorporated into C. glutamicum from another Corynebacterium and be expressed heterologously.” (paragraph 0009).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to combine teachings of Kirchner, Stauffer and Liu on C. glutamicum with introduced glycine transporter system and modify microorganism further to incorporate glycine cleavage system, including GcvP, GcvT, GcvH LipA or LipB proteins following Ochrombel guidance. One would have been motivated to make this combination since Ochrombel teaches increase in the yield of produced L-amino acids by using glycine cleavage system. A skilled artisan would have reasonably expected success in this combination since Kirchner and Ochrombel provide methods of C. glutamicum genetic modification and Stauffer and Ochrombel pointed to the role of glycine transporter and glycine cleavage proteins in the increase in the efficiency of amino acids production and Liu provided gene and sequence for the C. ammoniagenes glycine transporter. Thus, teachings of Kirchner, Stauffer, Liu and Ochrombel as evidenced by Yang_1 render claims 5 and 6 obvious.
Regarding claims 7 and 8, Liu teaches complete annotated genome sequence of C. stationis (C. ammoniagenes) ATCC 6872 (Abstract). Liu discloses that: “The genome sequence of ATCC 6872 has been deposited in the GenBank database under accession number CP014279” (p. 57, right column, last paragraph). C. stationis ATCC 6872 has GcvP gene as evidenced by Yang_2 (p. 2, line 28). Yang_2 shows that the GcvP gene (p. 2, line 28) from C. stationis ATCC 6872 encodes aminomethyl-transferring glycine dehydrogenase (p. 2, line 42) and provides the corresponding amino acid sequence which has 100% identity to SEQ ID NO:26.
Regarding claim 13, C. stationis ATCC 6872 has GcvT gene as evidenced by Yang_3 (p. 2, line 32). Yang_3 shows that the GcvT gene (p. 2, line 32) from C. stationis ATCC 6872 encodes glycine cleavage system aminomethyltransferase (p. 2, line 47) and provides the corresponding amino acid sequence which has 100% identity to SEQ ID NO:27.
Regarding claim 14, C. stationis ATCC 6872 has GcvH gene as evidenced by Yang_4 (p. 2, line 28). Yang_4 shows that the GcvH gene (p. 2, line 28) from C. stationis ATCC 6872 encodes glycine cleavage system protein GcvH (p. 2, line 41) and provides the corresponding amino acid sequence which has 100% identity to SEQ ID NO:28.
Regarding claim 15, C. stationis ATCC 6872 has LipA gene as evidenced by Yang_5 (p. 2, line 28). Yang_5 shows that the LipA gene (p. 2, line 28) from C. stationis ATCC 6872 encodes lipoyl synthase (p. 2, line 44) and provides the corresponding amino acid sequence which has 100% identity to SEQ ID NO:29.
Regarding claim 16, C. stationis ATCC 6872 has LipB gene as evidenced by Yang_6 (p. 2, line 28). Yang_6 shows that the LipB gene (p. 2, line 28) from C. stationis ATCC 6872 encodes lipoyl (octanoyl) transferase LipB (p. 2, line 42) and provides the corresponding amino acid sequence which has 100% identity to SEQ ID NO:26.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to use the sequences for glycine cleavage proteins, GcvP, GcvT, GcvH LipA or LipB from C. stationis ATCC 6872 of Liu teaching to incorporate glycine cleavage system into modified microorganism based on Kirchner, Stauffer, Liu and Ochrombel teachings. One would have been motivated to make this combination since Liu teaches annotated genome of bacterium from the same Corynebacterium genus and which has annotated GcvP, GcvT, GcvH LipA or LipB genes for glycine cleavage proteins and corresponding sequences as evidenced by Yang_2, Yang_3, Yang_4, Yang_5 and Yang_6. A skilled artisan would have reasonably expected success in this combination since Kirchner and Ochrombel provide methods of C. glutamicum genetic modification and Stauffer and Ochrombel pointed to the role of glycine transporter and glycine cleavage proteins in the increase in the efficiency of amino acids production and Liu provided gene and sequences for the C. ammoniagenes glycine transporter and glycine cleavage proteins. Thus, teachings of Kirchner, Stauffer, Liu and Ochrombel as evidenced by Yang_1, Yang_2, Yang_3, Yang_4, Yang_5 and Yang_6 render claims 7, 8 and 13-16 obvious.
Response to Arguments
Applicant's arguments filed 09/25/2025 have been fully considered but they are not persuasive.
Applicant argues (addressing p. 6 of the Remarks) that: “the unexpectedly superior results shown in Table 3 commensurate with the scope of the present claim that recites “the glycine transporter comprises the amino acid sequence of SEQ ID NO:1”. Applicant refers to the previous office action where it was pointed that the increase in histidine production was shown for C. glutamicum comprising a glycine transporter comprising SEQ ID NO:1 and not for the entire scope of C. glutamicum structure and hence the unexpected results are not commensurate in scope with the claimed invention. These arguments are not persuasive because:
First, the advantage of the introduction of CycA glycine transporter from C. ammoniagenes with SEQ ID NO: 1 recognized by the Applicant does not make the combination of prior art non-obvious because the prior art does not need to point out all advantages if there is a motivation to combine the prior art. MPEP 2145: “The fact that appellant has recognized another advantage which would flow naturally from following the suggestion of the prior art cannot be the basis for patentability when the differences would otherwise be obvious." Ex parte Obiaya, 227 USPQ 58, 60 (Bd. Pat. App. & Inter. 1985) (The prior art taught combustion fluid analyzers which used labyrinth heaters to maintain the samples at a uniform temperature. Although appellant showed that an unexpectedly shorter response time was obtained when a labyrinth heater was employed, the Board held this advantage would flow naturally from following the suggestion of the prior art.). See also Lantech Inc. v. Kaufman Co. of Ohio Inc., 878 F.2d 1446, 12 USPQ2d 1076, 1077 (Fed. Cir. 1989), cert. denied, 493 U.S. 1058 (1990) (unpublished — not citable as precedent) ("The recitation of an additional advantage associated with doing what the prior art suggests does not lend patentability to an otherwise unpatentable invention.")”. In instant case, Stauffer teaches necessity of glycine for synthesis of amino acids, including histidine (Abstract) providing motivation to add glycine transporter to C. glutamicum of Kirchner teaching used for production of L-amino acids (Abstract) and Liu provides CycA gene encoding glycine transporter and sequence for CycA protein from the same Corynebacterium genus wherein the CycA amino acid sequence has 100% identity to instant SEQ ID NO: 1. Pursuant to MPEP 2112.01(II), “[p]roducts of identical chemical composition cannot have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable. Therefore, if the prior art teaches the identical chemical structure, the properties applicant discloses are necessarily present. Therefore, since the combination of prior art teaches microorganism of claim 1 including all limitation of claim 1 this microorganism will necessarily produce histidine to the level shown in Table 3 and hence these results are not unexpected.
Second, assuming arguendo applicant has shown unexpected data, claims are not commensurate in scope with the unexpected results. MPEP 716.02: “Whether the unexpected results are the result of unexpectedly improved results or a property not taught by the prior art, the "objective evidence of nonobviousness must be commensurate in scope with the claims which the evidence is offered to support." In instant case, results presented in Table 3 are based on very specific C. glutamicum microorganisms, CA 14-0682∆purU::pcj7_cycA(Cam) and CA 14-0682∆purU ::PglyA_cycA(Cam). Although these microorganisms comprise cycA gene of C. ammoniagenes encoding protein with amino acid sequence of SEQ ID NO:1, these microorganisms have additional specific characteristics, i.e.: (i) they are mutant strains of C. glutamicum, CA14-0682, obtained in Example 1; (ii) they have cycA gene introduced by deletion of purU gene and (iii) have introduced promoters, pcj7 or PglyA. Thus, microorganisms of Table 3 have very specific characteristics not present in the claim 1 and hence the claims are not commensurate in scope with the unexpected results.
Conclusion
No claims are allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to LIOUBOV G KOROTCHKINA whose telephone number is (571)270-0911. The examiner can normally be reached Monday-Friday: 8:00-5:30.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Sharmila G Landau can be reached at (571)272-0614. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/L.G.K./Examiner, Art Unit 1653
/SHARMILA G LANDAU/Supervisory Patent Examiner, Art Unit 1653