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 CIP of 14/911,102, issued as US Patent No. 11,753,656, which is a 371 of PCT/US2014/051355.
The amendment filed on December 29, 2025 has been entered.
Election/Restrictions
Applicant elected without traverse of Group I with a species election of
Saccharomyces cerevisiae as the microorganism, and
the following native and/or heterologous enzymes that are activated, upregulated, or overexpressed in the microorganism by their sequence identifiers and whether they are activated, upregulated, or overexpressed:
SEQ ID NO: 231 as the phosphoketolase and overexpressed;
SEQ ID NO: 233 as the acetate kinase and overexpressed;
SEQ ID NO: 232 as the phosphotransacetylase and overexpressed;
SEQ ID NO: 230 as the thiolase and overexpressed;
SEQ ID NO: 234 as the XoA transferase and overexpressed;
SEQ ID NO: 236 as the acetoacetate decarboxylase and overexpressed;
SEQ ID NO: 219 as the bifunctional acetaldehyde/alcohol dehydrogenase and overexpressed;
SEQID NO: 221 as the pyruvate formate lyase and overexpressed;
SEQ ID NO: 237 as the acetyl-CoA synthetase and overexpressed; and
SEQ ID NO: 10 as the STLI and overexpressed
in the reply filed on April 15, 2025.
Claims 15 and 20 are withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species/invention, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on April 15, 2025.
The elected species was disclosed in the prior art, see the 102 and 103 rejections in the Office Action mailed on June 30, 2025. In the amendment filed on December 29, 2025, SEQ ID NO:231, 233, 232, 230, 234, 236, 219, 221, and 237 were deleted from the claims. Therefore, examination has been extended to subsequent species, recombinant S. cerevisiae overexpressing Bifidobacterium adolescentis phosphoketolase, Bifidobacterium adolescentis acetate kinase, Clostridium acetobutylicum acetyl-CoA acetyltransferase, Clostridium acetobutylicum CoA transferase (ctfA and ctfB), Clostridium acetobutylicum acetoacetate decarboxylase, Leuconostoc mesenteroides phosphotransacetylase, S. cerevisiae derived acetyl-CoA synthetase, Bifidobacterium adolescentis pyruvate formate lyase, Bifidobacterium adolescentis acetaldehyde/alcohol dehydrogenase or Clostridum beijerinckii alcohol dehydrogenase, and Pichia sorbitophila STL1 of SEQ ID NO:10, which is disclosed in the prior art. See the rejections under 103 rejections below. Therefore, search and examination has not been extended to any subsequent species.
Status of Claims
Claims 1-5 and 9-20 are pending.
Claims 15 and 20 are withdrawn.
Claims 1-5, 9-14, and 16-19 are under examination.
Information Disclosure Statement
The information disclosure statement (IDS) submitted on December 29, 2025 in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Response to Arguments
Specification
Applicant’s arguments, see page 10 of the Remarks, filed December 29, 2025, with respect to the specification have been fully considered and are persuasive. The specification has been amended to delete the embedded hyperlink and/or other form of browser-executable code. Therefore, the objection of the specification has been withdrawn.
Claim Objections
Applicant’s arguments, see page 11 of the Remarks, filed December 29, 2025, with respect to claim 2 have been fully considered and are persuasive. Claim 2 has been amended to recite “172, or 174”. Therefore, the objection of claim 2 has been withdrawn.
Applicant’s arguments, see page 11 of the Remarks, filed December 29, 2025, with respect to claim 6 have been fully considered and are persuasive. Claim 6 has been cancelled. Therefore, the objection of claim 6 has been withdrawn.
Applicant’s arguments, see page 11 of the Remarks, filed December 29, 2025, with respect to claims 17-18 have been fully considered and are persuasive. Claims 17-18 have been amended to recite the entire phrase of “STL1”. Therefore, the objection of claims 17-18 has been withdrawn.
Claim Rejections - 35 USC § 102
Applicant’s arguments, see pages 1-13 of the Remarks, filed December 29, 2025, with respect to claims 1-2, 4-10, 13-14, and 16-19 have been fully considered and are persuasive. Claim 1 has been amended to recite that the recombinant microorganism comprises a heterologous acetate kinase, which is not disclosed Muramatsu (WO 2012/098662 – form PTO-892 and US Patent No. 9,340,793 – form PTO-892). Therefore, the rejection of claims 1-2, 4-10, 13-14, and 16-19 under 35 U.S.C. 102(a)(1) or 102(a)(2) has been withdrawn.
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 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 of this title, 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.
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.
Withdrawn Rejections
Applicant’s arguments, see page 15 of the Remarks, filed December 29, 2025, with respect to claims 1-11, 13-14, and 16-19 have been fully considered and are persuasive. Applicant has provided a statement that Zelle does not qualify as prior under the 102(b)(2)(C) exception. Therefore, the rejection of claims 1-11, 13-14, and 16-19 under 35 U.S.C. 103 as being unpatentable over Muramatsu (WO 2012/098662 – form PTO-892 or US Patent No. 9,340,793 – form PTO-892), Zelle (US 2014/0256011 – form PTO-1449), and Wang (Biotechnol Lett (2013) 35:1859–1864 – form PTO-1449) has been withdrawn.
Applicant’s arguments, see pages 15-16 of the Remarks, filed December 29, 2025, with respect to claims 1-14 and 16-19 have been fully considered and are persuasive. Applicant has provided a statement that Shaw does not qualify as prior under the 102(b)(2)(C) exception. Therefore, the rejection of claims 1-14 and 16-19 under 35 U.S.C. 103 as being unpatentable over Shaw (US Patent No. 9,988,650 – form PTO-892, US Patent No. 10,465,208, and US patent No. 11,655,484 – form PTO-892) and Muramatsu (WO 2012/098662 – form PTO-892 or US Patent No. 9,340,793 – form PTO-892) and evidenced by Zhao (Gene. 1994 Sep 2;146(2):215-9 — form PTO-1449) has been withdrawn.
Modified Rejections
Claim(s) 1-5, 9-10, 13-14, and 16-19 is/are rejected under 35 U.S.C. 102(a)(1) or 102(a)(2) as being anticipated by Muramatsu (102(a)(1): WO 2012/098662 – cited previously on form PTO-892 and 102(a)(2): US Patent No. 9,340,793 – cited previously on form PTO-892. US Patent No. 9,340,793 is the US national stage of WO 2012/098662. Therefore, US Patent No. 9,340,793 is the English equivalent of WO 2012/098662 and is used for specific passages of Muramatsu) and A1A187_BIFAA (UniProtKB/TrEMBL Database. July 11, 2012 – cited previously on form PTO-892) and evidenced by Zhao (Gene. 1994 Sep 2;146(2):215-9 — form PTO-1449) discloses a S. cerevisiae STL1 (Figure 2 on page 217).
Regarding claims 1-2 and 19, Muramatsu discloses a recombinant S. cerevisiae (A) overexpressing enzymes that convert fructose-6-phosphate to acetyl-phosphate and acetyl-CoA and acetate comprising (1) a heterologous Bifidobacterium adolescentis phosphoketolase (SEQ ID NO:3) and (2) a native acetate kinase and (B) overexpressing enzymes that convert acetyl-CoA and acetate to acetone and/or isopropanol comprising (b)(1) a heterologous Clostridium acetobutylicum acetyl-CoA acetyltransferase or known as thiolase, (2) a heterologous Clostridium acetobutylicum CoA transferase (ctfA and ctfB), and (3) a heterologous Clostridium acetobutylicum acetoacetate decarboxylase (Figures 2 and 4, Column 3, lines 37-54, Column 2 lines 8-22 and lines 34-48, Column 4, lines 31-42, Column 6, lines 9-15, Column 9, lines 1-20, Column 18, line 56 through Column 19 line 10, and Column 20, lines 7-18, and claims 1-3). The phosphoketolase of Muramatsu has 100% sequence identity to the phosphoketolase of SEQ ID NO:231 of the instant application and therefore inherently has the ability to convert D-xylulose 5-phosphate into D-glyceraldehyde 3-phosphate (Column 2, lines 14-17 and see the sequence alignment below) and convert D-fructose 6-phosphate into D-erythrose 4-phosphate, as evidenced by A1A185_BIFAA and paragraph [0118] and [0288] of the instant specification.
Regarding claims 4-5, the recombinant S. cerevisiae of Muramatsu also overexpresses a heterologous Leuconostoc mesenteroides phosphotransacetylase of SEQ ID NO: 31 (Column 2, lines 27-29 and Column 7, lines 11-49). The phosphotransacetylase of SEQ ID NO:31 of Muramatsu has 100% sequence identity to the phosphotransacetylase of SEQ ID NO:122 of the instant application (see the sequence alignment below).
Regarding claims 9-10, the recombinant S. cerevisiae of Muramatsu also overexpresses a heterologous alcohol dehydrogenase and is derived from Clostridum beijerinckii (Column 2, lines 38-39 and Column 22, lines 51-61).
Regarding claims 13-14, the recombinant S. cerevisiae of Muramatsu also overexpresses a heterologous acetyl-CoA synthetase derived from S. cerevisiae (Column 2, lines 27-29 and Column 8, lines 55-67).
Regarding claims 16-18, S. cerevisiae comprises a native STL1 that importers glycerol, as evidenced by Zhao (Figure 2 on page 217).
The recombinant S. cerevisiae of Muramatsu does not comprise a heterologous acetate kinase. Muramatsu discloses a recombinant yeast/S. cerevisiae prepared through modification to suppress and/or enhance expression of heterologous enzymes (Column 1, lines 13-17).
Regarding claims 1 and 3, A1A187_BIFAA discloses a Bifidobacterium adolescentis acetate kinase (see pages 1-2).
Therefore, in combing the above references, it would have been obvious to one having ordinary skill in the art before the time the claimed invention was effectively filed to modify the S. cerevisiae of Muramatsu by overexpressing a heterologous acetate kinase because one of ordinary skill in the art would have been able to carry out such a substitution, and the results were reasonably predictable. The rationale to support a conclusion that the claims would have been obvious is that the substitution of one known element for another yields predictable results to one of ordinary skill in the art. See MPEP 2143. One having ordinary skill in the art would have been motivated to overexpress a heterologous acetate kinase to increase production of acetyl-CoA and thereby isopropanol. One having ordinary skill in the art would have had a reasonable expectation of success since Muramatsu discloses a recombinant S. cerevisiae comprising enzymes, including acetate kinase, and having increased production of acetyl-CoA and compounds made from acetyl-CoA and A1A187_BIFAA discloses a Bifidobacterium adolescentis acetate kinase.
Therefore, the above references render claims 1-5, 9-10, 13-14, and 16-19 prima facie obvious.
Applicant's arguments filed December 29, 2025 have been fully considered but they are not persuasive.
Applicant argues that the claims are obvious over the cited reference because Muramatsu does not disclose, teach or suggest the expression of heterologous acetate kinase and A1A187_BIFAA does not overcome this defect.
This is not found persuasive. A1A187_BIFAA discloses a Bifidobacterium adolescentis acetate kinase, which is heterologous to S. cerevisiae. Muramatsu discloses a recombaint S. cerevisiae overexpressing a heterologous phophoketolase and a native acetate kinase, wherein the S. cerevisiae produces acetyl-CoA, which are subsequently converted to isopropanol. Therefore, it would have been obvious to one having ordinary skill in the art before the time the claimed invention was effectively filed to modify the S. cerevisiae of Muramatsu by overexpressing the heterologous acetate kinase A1A187_BIFAA because one of ordinary skill in the art would have been able to carry out such a substitution, and the results were reasonably predictable. One having ordinary skill in the art would have been motivated to overexpress a heterologous acetate kinase to increase production of acetyl-CoA and thereby isopropanol.
Therefore, the rejection has been maintained.
Claim(s) 9-12 is/are rejected under 35 U.S.C. 103 as being unpatentable over Muramatsu (102(a)(1): WO 2012/098662 – cited previously on form PTO-892 and 102(a)(2): US Patent No. 9,340,793 – cited previously on form PTO-892) and A1A187_BIFAA (UniProtKB/TrEMBL Database. July 11, 2012 – cited previously on form PTO-892), and evidenced by Zhao (Gene. 1994 Sep 2;146(2):215-9 — form PTO-1449) as applied to claims 1-5, 9-10, 13-14, and 16-19 above, and further in view of Sillers (WO 2012/019175 – form PTO-892).
Muramatsu and A1A187_BIFAA do not disclose a recombinant S. cerevisiae overexpressing a bifunctional acetaldehyde/alcohol dehydrogenase, pyruvate formate lyase, and STL1 of SEQ ID NO:10. However, the recombinant S. cerevisiae Muramatsu has increased production of acetyl-CoA and compounds made from acetyl-CoA, such as isopropanol (Column 2, lines 8-17 and lines 44-49).
Sillers discloses producing ethanol by converting pyruvate → acetyl-CoA → acetaldehyde → ethanol by using a pyruvate formate lyase and a bifunctional acetaldehyde/alcohol dehydrogenase (Figure 34B and [0302]).
Regarding claim 11-12, Sillers discloses a recombinant S. cerevisiae overexpressing a Bifidobacterium adolescentis pyruvate formate lyase ((Figure 34B and [0302]-[0305]).
Regarding claim 9-10, Sillers discloses a recombinant S. cerevisiae overexpressing a Bifidobacterium adolescentis acetaldehyde/alcohol dehydrogenase of ((Figure 34B and [0302]-[0304]).
Therefore, in combing the above references, it would have been obvious to one having ordinary skill in the art before the time the claimed invention was effectively filed to further modify the S. cerevisiae of Muramatsu by overexpressing a pyruvate formate lyase and a bifunction alcohol/aldehyde dehydrogenase in addition to the heterologous acetate kinase to increase production of acetyl-CoA derived products, such as ethanol in addition to isopropanol. One having ordinary skill in the art would have been motivated to overexpress a pyruvate formate lyase to increase production of acetyl-CoA and overexpress a bifunction alcohol/aldehyde dehydrogenase to convert said acetyl-CoA to ethanol. One having ordinary skill in the art would have had a reasonable expectation of success since Muramatsu discloses a recombinant S. cerevisiae having increased production of acetyl-CoA and compounds made from acetyl-CoA due to expression of heterologous enzymes, A1A187_BIFAA discloses a Bifidobacterium adolescentis acetate kinase, and Sillers discloses a recombinant S. cerevisiae overexpressing pyruvate formate lyase that converts pyruvate to acetyl-CoA and overexpressing bifunctional alcohol/aldehyde dehydrogenase that converts acetyl-CoA to ethanol.
Therefore, the above references render claims 1-5, 9-14, and 16-19 prima facie obvious.
Applicant's arguments filed December 29, 2025 have been fully considered but they are not persuasive.
Applicant argues that the claims are obvious over the cited reference because Muramatsu does not disclose, teach or suggest the expression of heterologous acetate kinase and Sillers does not remedy this deficiency.
This is not found persuasive. A1A187_BIFAA discloses a Bifidobacterium adolescentis acetate kinase, which is heterologous to S. cerevisiae. Muramatsu discloses a recombaint S. cerevisiae overexpressing a heterologous phophoketolase and a native acetate kinase, wherein the S. cerevisiae produces acetyl-CoA, which are subsequently converted to isopropanol. Therefore, it would have been obvious to one having ordinary skill in the art before the time the claimed invention was effectively filed to modify the S. cerevisiae of Muramatsu by overexpressing the heterologous acetate kinase A1A187_BIFAA because one of ordinary skill in the art would have been able to carry out such a substitution, and the results were reasonably predictable. One having ordinary skill in the art would have been motivated to overexpress a heterologous acetate kinase to increase production of acetyl-CoA and thereby isopropanol.
Applicant argues that Sillers teaches away from expressing heterologous acetate kinase and instead discloses attenuation or deletion of native acetate kinase, [0022], [0216], and [0232]).
This is not found persuasive.
MPEP 2145. X.D.1. states that “the prior art’s mere disclosure of more than one alternative does not constitute a teaching away from any of these alternatives because such disclosure does not criticize, discredit, or otherwise discourage the solution claimed….”. MPEP 2123 states that “[d]isclosed examples and preferred embodiments do not constitute a teaching away from a broader disclosure or nonpreferred embodiments.” In the instant case, paragraphs [0022], [0216], and [0232] do not criticize, discredit, or otherwise discourage overexpression of acetate kinase. Paragraphs [0022], [0216], and [0232] are some of the embodiments of Sillers. Sillers also discloses a recombinant microorganism comprising one or more native and/or heterologous enzymes that function in one or more engineered metabolic pathways to convert a carbohydrate source to a hydrocarbon, wherein the one or more native and/or heterologous enzymes is activated, upregulated, downregulated, or deleted ([0013]). In order to increase the production of an acetate and acetyl-CoA derived products, one having ordinary skill in the art would have been motivated to upregulate a heterologous acetate kinase by overexpressing the acetate kinase in the recombinant S. cerevisiae of Maramatsu to increase production of acetate and acetyl-CoA derived products instead of deleting acetate kinase.
Therefore, the rejection has been maintained.
Claim(s) 18 is/are rejected under 35 U.S.C. 103 as being unpatentable over Muramatsu (102(a)(1): WO 2012/098662 – cited previously on form PTO-892 and 102(a)(2): US Patent No. 9,340,793 – cited previously on form PTO-892) and A1A187_BIFAA (UniProtKB/TrEMBL Database. July 11, 2012 – cited previously on form PTO-892), and evidenced by Zhao (Gene. 1994 Sep 2;146(2):215-9 — form PTO-1449) discloses a S. cerevisiae STL1 (Figure 2 on page 217), and Sillers (WO 2012/019175 – form PTO-892) as applied to claims 1-5, 9-14, and 16-19 above, and further in view of Wang (Biotechnol Lett (2013) 35:1859–1864 – form PTO-1449) and CCE72448.1 (GenBank Database. February 12, 2012 – form PTO-892).
Muramatsu, A1A187_BIFAA, and Sillers do not disclose overexpressing STL1 of SEQ ID NO:10.
Regarding calims 16-18, Wang discloses a recombinant S. cerevisiae overexpressing a H+/glycerol symporter (STL1), wherein ethanol production is increased in said recombinant S. cerevisiae (abstract, pages 1860-1861 and 1863).
Regarding claim 18, CCE72448.1 discloses a STL1 having 100% sequence identity to SEQ ID NO:10 of the instant application (see pages 1-2 and see the sequence alignment below).
Therefore, in combing the teachings of the above references, it would have been obvious to one having ordinary skill in the art before the time the claimed invention was effectively filed to further modify the recombinant S. cerevisiae of Maramatsu by substituting the STL1 with the STL1 of CCE72448.1 because one of ordinary skill in the art would have been able to carry out such a substitution, and the results were reasonably predictable. The rationale to support a conclusion that the claims would have been obvious is that the substitution of one known element for another yields predictable results to one of ordinary skill in the art. See MPEP 2143. One of ordinary skill in the art would have had a reasonable expectation of success since Muramatsu discloses a recombinant S. cerevisiae having increased production of acetyl-CoA and compounds made from acetyl-CoA due to expression of heterologous enzymes, A1A187_BIFAA discloses a Bifidobacterium adolescentis acetate kinase, Sillers discloses a recombinant S. cerevisiae overexpressing pyruvate formate lyase that converts pyruvate to acetyl-CoA and overexpressing bifunctional alcohol/aldehyde dehydrogenase that converts acetyl-CoA to ethanol, Wang discloses a recombinant S. cerevisiae overexpressing a H+/glycerol symporter (STL1), wherein ethanol production is increased, and CCE72448.1 discloses a STL1 having 100% sequence identity to SEQ ID NO:10 of the instant application
Therefore, the above references render claims 1-5, 9-14, and 16-18 prima facie obvious.
Applicant's arguments filed December 29, 2025 have been fully considered but they are not persuasive.
Applicant argues that the claims are obvious over the cited reference because Muramatsu does not disclose, teach or suggest the expression of heterologous acetate kinase and Wang and CCE72448.1 do not overcome this defect.
This is not found persuasive.
A1A187_BIFAA discloses a Bifidobacterium adolescentis acetate kinase, which is heterologous to S. cerevisiae. Muramatsu discloses a recombaint S. cerevisiae overexpressing a heterologous phophoketolase and a native acetate kinase, wherein the S. cerevisiae produces acetyl-CoA, which are subsequently converted to isopropanol. Therefore, it would have been obvious to one having ordinary skill in the art before the time the claimed invention was effectively filed to modify the S. cerevisiae of Muramatsu by overexpressing the heterologous acetate kinase A1A187_BIFAA because one of ordinary skill in the art would have been able to carry out such a substitution, and the results were reasonably predictable. One having ordinary skill in the art would have been motivated to overexpress a heterologous acetate kinase to increase production of acetyl-CoA and thereby isopropanol.
Therefore, the rejection has been maintained.
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.
Claims 1-5, 9-14, and 16-19 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-38 of US Patent No. 9,988,650 (reference patent) in view of Muramatsu (WO 2012/098662 – form PTO-892 or US Patent No. 9,340,793 – form PTO-892) and evidenced by Zhao (Gene. 1994 Sep 2;146(2):215-9 — form PTO-1449). US Patent No. 9,340,793 is the US national stage of WO 2012/098662. Therefore, US Patent No. 9,340,793 is the English equivalent of WO 2012/098662 and is used for specific passages of Muramatsu. 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:
Regarding claims 1-3 and 19 of the instant application, claims 1-5, 9, and 34 of the reference patent recites recombinant yeast comprising (A) enzymes that convert fructose-6-phosphate to acetyl-phosphate and acetyl-CoA comprising (1) a heterologous Bifidobacterium adolescentis phosphoketolase of SEQ ID NO:12 and (2) a heterologous Bifidobacterium adolescentis acetate kinase of SEQ ID NO:16 and (B) enzymes of the acetyl-CoA production pathway. The phosphoketolase of the reference patent has 100% sequence identity to the phosphoketolase of SEQ ID NO:231 of the instant application and therefore inherently has the ability to convert D-xylulose 5-phosphate into D-glyceraldehyde 3-phosphate and convert D-fructose 6-phosphate into D-erythrose 4-phosphate, as evidenced by paragraph [0118] and [0288] of the instant specification and see the sequence alignment below. The enzymes recited in the reference patent are overexpressed because Column 10, lines 19-29 of the reference patent defines that the term “recombinant” refers to overexpression of enzymes.
Regarding claims 4-5 of the instant application, claims 6-8 of the reference patent recites that the recombinant yeast overexpresses a heterologous Leuconostoc mesenteroides phosphotransacetylase of SEQ ID NO: 10.
Regarding claims 9-10 of the instant application, claims 1 and 10-11 of the reference patent recites that the recombinant yeast overexpresses a heterologous bifunctional aldehyde-alcohol alcohol dehydrogenase of SEQ ID NO:44.
Regarding claims 11-12 of the instant application, claims 32-33 of the reference patent recites that the recombinant yeast overexpresses a heterologous pyruvate formate lyase of SEQ ID NO:46.
The claims of the reference patent do not disclose a recombinant yeast/S. cerevisiae overexpressing thiolase, CoA transferase, acetoacetate decarboxylase, or acetyl-CoA synthetase, or STL1.
Regarding claims 1-2 and 19, Muramatsu discloses a recombinant S. cerevisiae (A) overexpressing enzymes that convert fructose-6-phosphate to acetyl-phosphate and acetyl-CoA comprising (1) a heterologous Bifidobacterium adolescentis phosphoketolase (SEQ ID NO:3) and (2) a native acetate kinase and (B) overexpressing enzymes that convert acetyl-CoA and acetate to acetone and/or isopropanol comprising (b)(1) a heterologous Clostridium acetobutylicum acetyl-CoA acetyltransferase or known as thiolase, (2) a heterologous Clostridium acetobutylicum CoA transferase (ctfA and ctfB), and (3) a heterologous Clostridium acetobutylicum acetoacetate decarboxylase (Figures 2 and 4, Column 3, lines 37-54, Column 2 lines 8-22 and lines 34-48, Column 4, lines 31-42, Column 6, lines 9-15, Column 9, lines 1-20, Column 18, line 56 through Column 19 line 10, and Column 20, lines 7-18, and claims 1-3). The recombinant S. cerevisiae of Muramatsu has increased production of acetyl-CoA and products made from acetyl-CoA, such as isopropanol (Column 2, lines 8-14 and lines 44-49).
Regarding claims 13-14, the recombinant S. cerevisiae of Muramatsu also overexpresses a heterologous acetyl-CoA synthetase derived from S. cerevisiae (Column 2, lines 27-29 and Column 8, lines 55-67).
Regarding claims 16-18 of the instant application, S. cerevisiae comprises a native STL1 that importers glycerol, as evidenced by Zhao. Zhao discloses a S. cerevisiae STL1 (Figure 2 on page 217).
Therefore, it would have been obvious to one having ordinary skill in the art to modify the yeast of the reference patent by overexpressing a thiolase, CoA transferase, acetoacetate decarboxylase, and acetyl-CoA synthetase in yeast or S. cerevisiae to increase production of isopropanol. One having ordinary skill in the art would have been motivated to overexpress a thiolase to increase production of acetoacetyl-CoA, overexpress a CoA transferase to convert said acetoacetyl-CoA to acetoacetate, overexpress acetoacetate decarboxylase to convert said acetoacetate to acetone, wherein the bifunction alcohol/aldehyde dehydrogenase converts said acetone to isopropanol, and overexpress acetyl-CoA synthetase to increase production of acetyl-CoA. One having ordinary skill in the art would have had a reasonable expectation of success since the claims of the reference patent recites a recombinant yeast having increased production of acetyl-CoA and Muramatsu discloses a recombinant S. cerevisiae having increased production of acetyl-CoA and compounds made from acetyl-CoA, such as isopropanol.
Therefore, the conflicting claims are not patentably distinct from each other.
Applicant's arguments filed December 29, 2025 have been fully considered but they are not persuasive.
In response to applicant's argument that the examiner's conclusion of obviousness is based upon improper hindsight reasoning, it must be recognized that any judgment on obviousness is in a sense necessarily a reconstruction based upon hindsight reasoning. But so long as it takes into account only knowledge which was within the level of ordinary skill at the time the claimed invention was made, and does not include knowledge gleaned only from the applicant's disclosure, such a reconstruction is proper. See In re McLaughlin, 443 F.2d 1392, 170 USPQ 209 (CCPA 1971).
Applicant argues that the ‘650 family reference patents relate to an engineered pathway to produce ethanol, while claim 1 of the instant application relates to a recombinant microorganism comprising a different engineered pathway to produce acetone and/or isopropanol. Applicant argues that the ‘650 family reference patents do not disclose, teach or suggest acetone and/or isopropanol.
This is not found persuasive. The above rejection has a secondary reference, Muramatsu. Claims 1 and 34 of the reference patent recites a recombaint yeast comprising at least one heterologous enzymes of the acetyl-CoA production pathway. Muramatsu discloses a recombinant S. cerevisiae overexpressing enzymes that convert acetyl-CoA and acetate to acetone and/or isopropanol comprising (b)(1) a heterologous Clostridium acetobutylicum acetyl-CoA acetyltransferase or known as thiolase, (2) a heterologous Clostridium acetobutylicum CoA transferase (ctfA and ctfB), and (3) a heterologous Clostridium acetobutylicum acetoacetate decarboxylase (Figures 2 and 4, Column 3, lines 37-54, Column 2 lines 8-22 and lines 34-48, Column 4, lines 31-42, Column 6, lines 9-15, Column 9, lines 1-20, Column 18, line 56 through Column 19 line 10, and Column 20, lines 7-18, and claims 1-3). Therefore, the modified yeast of the reference patent produces acetone and/or isopropanol.
Therefore, the rejection is maintained.
Claims 1-14 and 16-19 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-80 of US Patent No. 10,465,208 (reference patent) in view of Muramatsu (WO 2012/098662 – form PTO-892 or US Patent No. 9,340,793 – form PTO-892) and evidenced by Zhao (Gene. 1994 Sep 2;146(2):215-9 — form PTO-1449). US Patent No. 9,340,793 is the US national stage of WO 2012/098662. Therefore, US Patent No. 9,340,793 is the English equivalent of WO 2012/098662 and is used for specific passages of Muramatsu. 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:
Regarding claims 1-3 and 19 of the instant application, claims 1-7 and 10 of the reference patent recites recombinant yeast comprising (A) enzymes that convert fructose-6-phosphate to acetyl-phosphate and acetyl-CoA comprising (1) a heterologous Bifidobacterium adolescentis phosphoketolase of SEQ ID NO:12 and (2) a heterologous heterologous acetate kinase of SEQ ID NO:16 and (B) enzymes of the acetyl-CoA production pathway. The phosphoketolase of the reference patent has 100% sequence identity to the phosphoketolase of SEQ ID NO:231 of the instant application and therefore inherently has the ability to convert D-xylulose 5-phosphate into D-glyceraldehyde 3-phosphate and convert D-fructose 6-phosphate into D-erythrose 4-phosphate, as evidenced by paragraph [0118] and [0288] of the instant specification and see the sequence alignment below. The enzymes recited in the reference patent are overexpressed because Column 10, lines 25-35 of the reference patent defines that the term “recombinant” refers to overexpression of enzymes.
Regarding claims 4-5 of the instant application, claims 7-9 of the reference patent recites that the recombinant yeast overexpresses a heterologous Leuconostoc mesenteroides phosphotransacetylase of SEQ ID NO: 10.
Regarding claims 9-10 of the instant application, claims 1 and 11-12 of the reference patent recites that the recombinant yeast overexpresses a heterologous bifunctional aldehyde-alcohol alcohol dehydrogenase of SEQ ID NO:44.
Regarding claims 11-12 of the instant application, claims 29-30 of the reference patent recites that the recombinant yeast overexpresses a heterologous pyruvate formate lyase of SEQ ID NO:46.
The claims of the reference patent do not disclose a recombinant yeast/S. cerevisiae overexpressing thiolase, CoA transferase, acetoacetate decarboxylase, or acetyl-CoA synthetase, or STL1.
Regarding claims 1-2 and 19, Muramatsu discloses a recombinant S. cerevisiae (A) overexpressing enzymes that convert fructose-6-phosphate to acetyl-phosphate and acetyl-CoA comprising (1) a heterologous Bifidobacterium adolescentis phosphoketolase (SEQ ID NO:3) and (2) a native acetate kinase and (B) overexpressing enzymes that convert acetyl-CoA and acetate to acetone and/or isopropanol comprising (b)(1) a heterologous Clostridium acetobutylicum acetyl-CoA acetyltransferase or known as thiolase, (2) a heterologous Clostridium acetobutylicum CoA transferase (ctfA and ctfB), and (3) a heterologous Clostridium acetobutylicum acetoacetate decarboxylase (Figures 2 and 4, Column 3, lines 37-54, Column 2 lines 8-22 and lines 34-48, Column 4, lines 31-42, Column 6, lines 9-15, Column 9, lines 1-20, Column 18, line 56 through Column 19 line 10, and Column 20, lines 7-18, and claims 1-3). The recombinant S. cerevisiae of Muramatsu has increased production of acetyl-CoA and products made from acetyl-CoA, such as isopropanol (Column 2, lines 8-14 and lines 44-49).
Regarding claims 13-14, the recombinant S. cerevisiae of Muramatsu also overexpresses a heterologous acetyl-CoA synthetase derived from S. cerevisiae (Column 2, lines 27-29 and Column 8, lines 55-67).
Regarding claims 16-18 of the instant application, S. cerevisiae comprises a native STL1 that importers glycerol, as evidenced by Zhao. Zhao discloses a S. cerevisiae STL1 (Figure 2 on page 217).
Therefore, it would have been obvious to one having ordinary skill in the art to modify the yeast of the reference patent by overexpressing a thiolase, CoA transferase, acetoacetate decarboxylase, and acetyl-CoA synthetase in yeast or S. cerevisiae to increase production of isopropanol. One having ordinary skill in the art would have been motivated to overexpress a thiolase to increase production of acetoacetyl-CoA, overexpress a CoA transferase to convert said acetoacetyl-CoA to acetoacetate, overexpress acetoacetate decarboxylase to convert said acetoacetate to acetone, wherein the bifunction alcohol/aldehyde dehydrogenase converts said acetone to isopropanol, and overexpress acetyl-CoA synthetase to increase production of acetyl-CoA. One having ordinary skill in the art would have had a reasonable expectation of success since the claims of the reference patent recites a recombinant yeast having increased production of acetyl-CoA and Muramatsu discloses a recombinant S. cerevisiae having increased production of acetyl-CoA and compounds made from acetyl-CoA, such as isopropanol.
Therefore, the conflicting claims are not patentably distinct from each other.
Applicant's arguments filed December 29, 2025 have been fully considered but they are not persuasive. See above for Applicant’s arguments and rebuttal.
Therefore, the rejection is maintained.
Claims 1-14 and 16-19 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-52 of US Patent No. 11,655,484 (reference patent) in view of Muramatsu (WO 2012/098662 – form PTO-892 or US Patent No. 9,340,793 – form PTO-892) and evidenced by Zhao (Gene. 1994 Sep 2;146(2):215-9 — form PTO-1449). US Patent No. 9,340,793 is the US national stage of WO 2012/098662. Therefore, US Patent No. 9,340,793 is the English equivalent of WO 2012/098662 and is used for specific passages of Muramatsu. 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:
Regarding claims 1, 3 and 19 of the instant application, claims 1, 5-7, and 40-42 of the reference patent recites recombinant S. cerevisiae comprising (A) a heterologous Bifidobacterium adolescentis acetate kinase of SEQ ID NO:16 and (B) enzymes of the acetyl-CoA production pathway. The enzymes recited in the reference patent are overexpressed because Column 10, lines 19-29 of the reference patent defines that the term “recombinant” refers to overexpression of enzymes.
Regarding claims 4-5 of the instant application, claims 2-4 of the reference patent recites that the recombinant yeast overexpresses a heterologous Leuconostoc mesenteroides phosphotransacetylase of SEQ ID NO: 10. The phosphotransacetylase of SEQ ID NO:10 of the reference patent has 100% sequence identity to the phosphotransacetylase of SEQ ID NO:232 of the instant application (see the sequence alignment below).
Regarding claims 9-10 of the instant application, claims 1 and 8-9 of the reference patent recites that the recombinant yeast overexpresses a heterologous bifunctional aldehyde-alcohol alcohol dehydrogenase of SEQ ID NO:44. The bifunctional aldehyde-alcohol alcohol dehydrogenase of SEQ ID NO:44 of the reference patent has 100% sequence identity to the bifunctional aldehyde-alcohol alcohol dehydrogenase of SEQ ID NO:219 (see the sequence alignment below).
Regarding claims 11-12 of the instant application, claims 38-39 of the reference patent recites that the recombinant yeast overexpresses a heterologous pyruvate formate lyase of SEQ ID NO:46. The pyruvate formate lyase of SEQ ID NO:46 of the reference patent has 100% sequence identity to the bifunctional aldehyde-alcohol alcohol dehydrogenase of SEQ ID NO:221 (see the sequence alignment below).
Regarding claims 16-18 of the instant application, S. cerevisiae comprises a native STL1 that importers glycerol, as evidenced by Zhao. Zhao discloses a S. cerevisiae STL1 (Figure 2 on page 217).
The claims of the reference patent do not disclose a recombinant S. cerevisiae overexpressing a phosphoketolase, thiolase, CoA transferase, acetoacetate decarboxylase, or acetyl-CoA synthetase, or STL1.
Regarding claims 1-2 and 19, Muramatsu discloses a recombinant S. cerevisiae (A) overexpressing enzymes that convert fructose-6-phosphate to acetyl-phosphate and acetyl-CoA comprising (1) a heterologous Bifidobacterium adolescentis phosphoketolase (SEQ ID NO:3) and (2) a native acetate kinase and (B) overexpressing enzymes that convert acetyl-CoA and acetate to acetone and/or isopropanol comprising (b)(1) a heterologous Clostridium acetobutylicum acetyl-CoA acetyltransferase or known as thiolase, (2) a heterologous Clostridium acetobutylicum CoA transferase (ctfA and ctfB), and (3) a heterologous Clostridium acetobutylicum acetoacetate decarboxylase (Figures 2 and 4, Column 3, lines 37-54, Column 2 lines 8-22 and lines 34-48, Column 4, lines 31-42, Column 6, lines 9-15, Column 9, lines 1-20, Column 18, line 56 through Column 19 line 10, and Column 20, lines 7-18, and claims 1-3). The recombinant S. cerevisiae of Muramatsu has increased production of acetyl-CoA and products made from acetyl-CoA, such as isopropanol (Column 2, lines 8-14 and lines 44-49).
Regarding claims 13-14, the recombinant S. cerevisiae of Muramatsu also overexpresses a heterologous acetyl-CoA synthetase derived from S. cerevisiae (Column 2, lines 27-29 and Column 8, lines 55-67).
Regarding claims 16-18 of the instant application, S. cerevisiae comprises a native STL1 that importers glycerol, as evidenced by Zhao. Zhao discloses a S. cerevisiae STL1 (Figure 2 on page 217).
Therefore, it would have been obvious to one having ordinary skill in the art to modify the S. cerevisiae of the reference patent by overexpressing a phosphoketolase, thiolase, CoA transferase, acetoacetate decarboxylase, and acetyl-CoA synthetase in yeast or S. cerevisiae to increase production of isopropanol. One having ordinary skill in the art would have been motivated to overexpress a phosphoketolase to increase production of acetylphosphosphate thereby increasing production of acetyl-CoA, overexpress thiolase to increase production of acetoacetyl-CoA, overexpress a CoA transferase to convert said acetoacetyl-CoA to acetoacetate, overexpress acetoacetate decarboxylase to convert said acetoacetate to acetone, wherein the bifunction alcohol/aldehyde dehydrogenase converts said acetone to isopropanol, and overexpress acetyl-CoA synthetase to increase production of acetyl-CoA. One having ordinary skill in the art would have had a reasonable expectation of success since the claims of the reference patent recites a recombinant yeast having increased production of acetyl-CoA and Muramatsu discloses a recombinant S. cerevisiae having increased production of acetyl-CoA and compounds made from acetyl-CoA, such as isopropanol.
Therefore, the conflicting claims are not patentably distinct from each other.
Applicant's arguments filed December 29, 2025 have been fully considered but they are not persuasive. See above for Applicant’s arguments and rebuttal.
Therefore, the rejection is maintained.
Claims 1-5, 9-14 and 16-19 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-25 of US Patent No. 11,753,656 (reference patent) in view of Muramatsu (WO 2012/098662 – form PTO-892 or US Patent No. 9,340,793 – form PTO-892) and Sillers (WO 2012/019175 – form PTO-892). US Patent No. 9,340,793 is the US national stage of WO 2012/098662. Therefore, US Patent No. 9,340,793 is the English equivalent of WO 2012/098662 and is used for specific passages of Muramatsu. The instant application is a CIP of the 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:
Regarding claims 1, 9-10, and 16-19 of the instant application, claims 1, 17, and 21 of the reference patent recite a recombinant yeast/Saccharomyces comprising (A) a heterologous STL1 of SEQ ID NO:10 and (B) a heterologous bifunctional acetaldehyde/alcohol dehydrogenase. The STL1 of SEQ ID NO:10 of the reference patent has 100% sequence identity to the STL1 of SEQ ID NO:10 of the instant application.
Regarding claim 11 of the instant application, claim 4 of the reference patent recites that the recombinant yeast/Saccharomyces comprises an engineered pathway that converts pyruvate to acetyl-CoA and formate. Pyrvuate formate lyase converts pyruvate to acetyl-CoA and formate.
Regarding 13 of the instant application, claim 6 of the reference patent recites that the recombinant yeast/Saccharomyces comprises an engineered pathway that converts acetate to acetyl-CoA. Acetyl-CoA synthetase converts acetate to acetyl-CoA.
The claims of the reference patent do not recite a recombinant yeast/Saccharomyces comprising phosphoketolase, acetate kinase, thiolase, CoA transferase, acetoacetate carboxylase, and phosphotransacetylase.
Regarding claims 1-2 and 19, Muramatsu discloses a recombinant S. cerevisiae (A) overexpressing enzymes that convert fructose-6-phosphate to acetyl-phosphate and acetyl-CoA comprising (1) a heterologous Bifidobacterium adolescentis phosphoketolase (SEQ ID NO:3) and (2) a native acetate kinase and (B) overexpressing enzymes that convert acetyl-CoA and acetate to acetone and/or isopropanol comprising (b)(1) a heterologous Clostridium acetobutylicum acetyl-CoA acetyltransferase or known as thiolase, (2) a heterologous Clostridium acetobutylicum CoA transferase (ctfA and ctfB), and (3) a heterologous Clostridium acetobutylicum acetoacetate decarboxylase (Figures 2 and 4, Column 3, lines 37-54, Column 2 lines 8-22 and lines 34-48, Column 4, lines 31-42, Column 6, lines 9-15, Column 9, lines 1-20, Column 18, line 56 through Column 19 line 10, and Column 20, lines 7-18, and claims 1-3). The phosphoketolase of Muramatsu has 100% sequence identity to the phosphoketolase of SEQ ID NO:231 of the instant application and therefore inherently has the ability to convert D-xylulose 5-phosphate into D-glyceraldehyde 3-phosphate and convert D-fructose 6-phosphate into D-erythrose 4-phosphate, as evidenced by paragraph [0118] and [0288] and see the sequence alignment below. Muramasu discloses that phosphoketolase converts xylulose 5-phosphate to acetylphosphate, which is converted to acetyl-CoA by phosphotransacetylase (Column 2, lines 17 and Column 8, lies 49-54). The recombinant S. cerevisiae of Muramatsu has increased production of acetyl-CoA and products made from acetyl-CoA, such as isopropanol (Column 2, lines 8-14 and lines 44-49).
Regarding claims 4-5, the recombinant S. cerevisiae of Muramatsu also overexpresses a heterologous Leuconostoc mesenteroides phosphotransacetylase of SEQ ID NO: 31 (Column 2, lines 27-29 and Column 7, lines 11-49). The phosphotransacetylase of SEQ ID NO:31 of Muramatsu has 100% sequence identity to the phosphotransacetylase of SEQ ID NO:122 of the instant application (see the sequence alignment below).
Regarding claims 13-14, the recombinant S. cerevisiae of Muramatsu also overexpresses a heterologous acetyl-CoA synthetase derived from S. cerevisiae (Column 2, lines 27-29 and Column 8, lines 55-67).
Regarding claim 11-12, Sillers discloses a recombinant S. cerevisiae overexpressing a heterologous Bifidobacterium adolescentis pyruvate formate lyase of SEQ ID NO:210 (Figure 34B and [0302]-[0305]).
Regarding claim 9-10, Sillers discloses a recombinant S. cerevisiae overexpressing a Bifidobacterium adolescentis acetaldehyde/alcohol dehydrogenase of SEQ ID NO: 209 (Figure 34B and [0302]-[0304]).
Therefore, it would have been obvious to one having ordinary skill in the art to modify the it would have been obvious to one having ordinary skill in the art before the time the claimed invention was effectively filed to modify the yeast/Saccharomyces of the reference patent by overexpressing the STL1, phosphoketolase, acetate kinase, thiolase, CoA transferase, acetoacetate carboxylase, and phosphotransacetylase to increase production of acetyl-CoA derived products, such as ethanol in addition to isopropanol. One having ordinary skill in the art would have been motivated to overexpress the above enzymes to increase production of ethanol and isopropanol via acetyl-CoA. One having ordinary skill in the art would have had a reasonable expectation of success since the claims of the reference patent recites a recombinant yeast having increased production of acetyl-CoA, Muramatsu discloses a recombinant S. cerevisiae overexpressing phosphokeltoase, acetate kinase, thiolase, CoA transferase, acetoacetate carboxylase, and phosphotransacetylase having increased production of acetyl-CoA and compounds made from acetyl-CoA, and Sillers discloses a recombinant S. cerevisiae overexpressing pyruvate formate lyase that converts pyruvate to acetyl-CoA and overexpressing bifunctional alcohol/aldehyde dehydrogenase that converts acetyl-CoA to ethanol.
Therefore, the conflicting claims are not patentably distinct from each other.
Applicant's arguments filed December 29, 2025 have been fully considered but they are not persuasive.
Applicant argues that the claims of the instant application are patentably distinct from the claims of the reference patent because Sillers teaches away from expressing heterologous acetate kinase and instead discloses attenuation or deletion of native acetate kinase, [0022], [0216], and [0232]).
This is not found persuasive.
MPEP 2145. X.D.1. states that “the prior art’s mere disclosure of more than one alternative does not constitute a teaching away from any of these alternatives because such disclosure does not criticize, discredit, or otherwise discourage the solution claimed….”. MPEP 2123 states that “[d]isclosed examples and preferred embodiments do not constitute a teaching away from a broader disclosure or nonpreferred embodiments.” In the instant case, paragraphs [0022], [0216], and [0232] do not criticize, discredit, or otherwise discourage overexpression of acetate kinase. Paragraphs [0022], [0216], and [0232] are some of the embodiments of Sillers. Sillers also discloses a recombinant microorganism comprising one or more native and/or heterologous enzymes that function in one or more engineered metabolic pathways to convert a carbohydrate source to a hydrocarbon, wherein the one or more native and/or heterologous enzymes is activated, upregulated, downregulated, or deleted ([0013]). In order to increase the production of an acetate and acetyl-CoA derived products, one having ordinary skill in the art would have been motivated to upregulate a heterologous acetate kinase by overexpressing the acetate kinase in the recombinant S. cerevisiae of Maramatsu to increase production of acetate and acetyl-CoA derived products instead of deleting acetate kinase.
Applicant argues that the claims of the instant application are patentably distinct from the claims of the reference patent because the claims of the ‘656 patent require that the recombinant yeast produces increased ethanol relative to a control recombinant yeast without said heterologous STL1 protein while the present claims are directed to recombinant yeast used for converting biomass into acetone and/or isopropanol.
This is not found persuasive. The claims of the instant application do not recite a limitation excluding ethanol production.
Therefore, the rejection has been maintained.
Conclusion
Claims 1-5 and 9-20 are pending.
Claims 15 and 20 are withdrawn.
Claims 1-5, 9-14, and 16-19 are rejected.
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 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 phosphotransacetylase of SEQ ID NO:122 of the instant application (“Qy”) and phosphotransacetylase of Muramatsu (“Db”)
Sequence 31, US/13979537
Patent No. 9340793
GENERAL INFORMATION
APPLICANT: TOYOTA JIDOSHA KABUSHIKI KAISHA
TITLE OF INVENTION: A recombinant yeast and a method for producing
TITLE OF INVENTION: a substance using thereof
FILE REFERENCE: PH-4477-PCT
CURRENT APPLICATION NUMBER: US/13/979,537
CURRENT FILING DATE: 2013-07-12
NUMBER OF SEQ ID NOS: 100
SEQ ID NO 31
LENGTH: 326
TYPE: PRT
ORGANISM: Leuconostoc mesenteroides
Query Match 100.0%; Score 1616; Length 326;
Best Local Similarity 100.0%;
Matches 326; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MELFEQLKNKITGQNKTIVFPEGEDPRIQGAAIRLAADNLIEPILLGDAQEISKTAQAHN 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MELFEQLKNKITGQNKTIVFPEGEDPRIQGAAIRLAADNLIEPILLGDAQEISKTAQAHN 60
Qy 61 FDLSNIETIDPASYDENELAKLNATLVERRKGKTDAETAAKWLQNVNYFGTMLVYTGKAD 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 FDLSNIETIDPASYDENELAKLNATLVERRKGKTDAETAAKWLQNVNYFGTMLVYTGKAD 120
Qy 121 GMVSGAVHPTGDTVRPALQIIKTAPGSSRISGAFIMQKGEERYVFADAAINIDIDSDTMA 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 GMVSGAVHPTGDTVRPALQIIKTAPGSSRISGAFIMQKGEERYVFADAAINIDIDSDTMA 180
Qy 181 EIAIQSAHTAQVFDIEPKVAMLSFSTKGSAKSPLVDKVATATALAKKLAPELADSIDGEL 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 EIAIQSAHTAQVFDIEPKVAMLSFSTKGSAKSPLVDKVATATALAKKLAPELADSIDGEL 240
Qy 241 QFDAAFVESVAAAKAPDSKVAGKANTFIFPSLEAGNIGYKIAQRLGGFEAIGPILQGLAK 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 QFDAAFVESVAAAKAPDSKVAGKANTFIFPSLEAGNIGYKIAQRLGGFEAIGPILQGLAK 300
Qy 301 PVSDLSRGANEEDVYKVAIITAAQAL 326
||||||||||||||||||||||||||
Db 301 PVSDLSRGANEEDVYKVAIITAAQAL 326
Sequence alignment between the STL1 of SEQ ID NO:10 of the instant application (“Qy”) and the STL1 of CCE72448.1 (“Db”)
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