Notice of Pre-AIA or AIA Status
The present application is being examined under the pre-AIA first to invent provisions.
Continued Examination Under 37 CFR 1.114
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on November 25, 2025 has been entered.
DETAILED ACTION
Claims 1-95, 97 and 109 are cancelled. Claim 118 is new. Claims 96, 98-108 and 110-118 are pending. Claims 96, 98-108, 110-114 and 118 are under examination.
The rejection of claim 97 under pre-AIA 35 U.S.C. 112, fourth paragraph and pre-AIA 35 U.S.C. 103(a) are withdrawn in light of the cancellation of the claim.
Claim Rejections - 35 USC § 103
The following is a quotation of pre-AIA 35 U.S.C. 103(a) which forms the basis for all obviousness rejections set forth in this Office action:
(a) A patent may not be obtained though the invention is not identically disclosed or described as set forth in section 102, if the differences between the subject matter sought to be patented and the prior art are such that the subject matter as a whole would have been obvious at the time the invention was made to a person having ordinary skill in the art to which said subject matter 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 pre-AIA 35 U.S.C. 103(a) 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 under pre-AIA 35 U.S.C. 103(a), the examiner presumes that the subject matter of the various claims was commonly owned at the time any inventions covered therein were made absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and invention dates of each claim that was not commonly owned at the time a later invention was made in order for the examiner to consider the applicability of pre-AIA 35 U.S.C. 103(c) and potential pre-AIA 35 U.S.C. 102(e), (f) or (g) prior art under pre-AIA 35 U.S.C. 103(a).
Claims 96, 98, 107-108 and 118 are rejected under pre-AIA 35 U.S.C. 103(a) as being unpatentable over Gunawardena et al. (WO 2008/080124 A2, published July 3, 2008) in view of Nestlé (EP 1 227 152 A1, published on July 31, 2002) and Shalel-Levanon et al. (Biotechnology and Bioengineering, 2005, Vol. 92, Issue 2, pp.147-159). The rejection of claim 96 is further evidenced by Schomburg, D., Schomburg, I., Chang, A. (eds) (Springer Handbook of Enzymes. 2006. vol 29. Springer, Berlin, Heidelberg) and Expasy (EC 2.3.1.54 formate C-acetyltransferase pyruvate formate-lyase; ENZYME - 2.3.1.54 formate C-acetyltransferase).
Regarding claim 96, Gunawardena teaches pyruvate formate lyase and formate dehydrogenase expression in Saccharomyces cerevisiae (p.46, Example 14 starting at [00230]). Gunawardena teaches the pyruvate formate lyase is cloned from E. coli pflB and pflA (relevant to a first heterologous pyruvate formate lyase) (p.46, [00230]).
Gunawardena does not teach a pyruvate formate lyase having the amino acid sequence of SEQ ID NO:60, or a second pyruvate formate lyase corresponding to EC 2.3.1.54.
However, Nestlé teaches a formate C-acetyltransferase with SEQ ID NO: 555 which has 100% homology to instant SEQ ID NO:60. As evidenced by Schomburg, formate c-acetyltransferase is a synonym for pyruvate formate lyase.
Shalel-Levanon teaches that E. coli have two pyruvate formate lyase enzymes encoded by the genes pflB, and pflD (p.150 Table II). As evidenced by Expasy, pyruvate formate lyase enzymes are classified as E.C. 2.3.1.54.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the recombinant yeast of Gunawardena by further including a second heterologous pyruvate formate lyase corresponding to E.C. 2.3.1.54 taught by Shalel-Levanon having the amino acid sequence taught by Nestlé to arrive at the claimed invention. One of ordinary skill would reasonably expect that combining two known pyruvate formate lyases together would predictably result in a recombinant yeast comprising a first heterologous pyruvate formate lyase having the amino acid sequence of SEQ ID NO:60 and a second heterologous pyruvate formate lyase corresponding to E.C. 2.3.1.54, because Gunawardena teaches a recombinant yeast comprising a heterologous pyruvate formate lyase, Shalel-Levanon teaches E. coli comprise two pyruvate formate lyases, and inserting a second heterologous pyruvate formate lyase into the yeast of Gunawardena would amount to a combination of known elements together in a predictable way. One of ordinary skill in the art would reasonably expect that introducing two heterologous pyruvate formate lyase from E. coli into a yeast would predictably result in a recombinant yeast comprising a first heterologous pyruvate formate lyase and a second heterologous pyruvate formate lyase, because Shalel-Levanon teaches that E. coli comprise two pyruvate formate lyases, and it was known in the art at the time of invention that heterologous pyruvate formate lyase genes could be inserted and expressed in yeast at the time of invention.
Regarding claim 98, Gunawardena teaches that acetyl-CoA may be produced in the cytosol by overexpressing two bacterial enzymes, a pyruvate formate lyase and a formate dehydrogenase; and using this pathway, pyruvate is converted to acetyl-CoA and formate (description p.26, [00154]). Gunawardena teaches that increased acetyl-CoA may be generated by the overexpression of an acetaldehyde dehydrogenase gene (relevant to further comprising a heterologous polypeptide having acetaldehyde dehydrogenase activity) (description p.24, [00143]). Gunawardena further teaches that acetaldehyde generated from pyruvate has two main fates: it can be further metabolized by a reductive process to alcohol by the action of an alcohol dehydrogenase (ADH) enzyme (description p.51, [00261]).
Regarding claims 107 and 108, Gunawardena teaches a yeast cell is the preferred host such as Saccharomyces cerevisiae or Kluyveromyces lactis (relevant to wherein the recombinant yeast is selected from Saccharomyces cerevisiae or Kluyveromyces lactis) (description p.10, [0053]).
Regarding claim 118, Gunawardena further teaches that acetaldehyde generated from pyruvate can be further metabolized by a reductive process to alcohol by the action of an alcohol dehydrogenase (ADH) enzyme (description p.51, [00261]).
Gunawardena is silent as to whether the recombinant yeast exhibits increased ethanol yield in an ethanol-producing fermentation process compared to a corresponding wild-type yeast.
However, based on Gunawardena’s teaching that acetaldehyde generated from pyruvate can be further metabolized to alcohol by the action of an ADH enzyme, one of ordinary skill in the art would reasonably expect that the recombinant yeast taught by Gunawardena would predictably result in increased ethanol yield compared to a corresponding wild-type yeast.
Claims 99, 102, 104, 106 and 110-111 are rejected under pre-AIA 35 U.S.C. 103(a) as being unpatentable over Gunawardena et al. (WO 2008/080124 A2, published July 3, 2008; previously cited) in view of Nestlé (EP 1 227 152 A1, published on July 31, 2002; previously cited) and Shalel-Levanon et al. (“Effect of ArcA and FNR on the Expression of Genes Related to the Oxygen Regulation and the Glycolysis Pathway in Escherichia coli Under Microaerobic Growth Conditions”, Biotechnology and Bioengineering, 2005, Vol. 92, Issue 2, pp.147-159) as applied to claims 96, 98 and 109 above, and further in view of Waks et al. (“Engineering a Synthetic Dual-Organism System for Hydrogen Production”, Applied and Environmental Microbiology, 2009, Vol. 75, No.7, pp.1867-1875; previously cited).
The teachings of Gunawardena et al., Nestlé and Shalel-Levanon et al. are discussed above.
Regarding claim 99, Gunawardena teaches that increased acetyl-CoA may be generated by the overexpression of an acetaldehyde dehydrogenase gene (description p.24, [00143]). Gunawardena teaches the use of metabolically engineering yeast cells for the production of biofuels at high yield (description p.2, [0002]).
Gunawardena, Nestlé and Shalel-Levanon do not teach a bifunctional acetaldehyde/alcohol dehydrogenase.
However, Waks teaches a strain of yeast expressing the anaerobic enzyme pyruvate formate lyase from E. coli that overproduced formate relative to undetectable levels in the wild type (relevant to a recombinant yeast comprising a first heterologous pyruvate formate lyase) (abstract). Waks further teaches that the addition of a downstream enzyme AdhE of E. coli resulted in an additional 4.5-fold formate production increase (relevant to acetaldehyde dehydrogenase) (abstract). Waks further teaches that AdhE represents acetaldehyde/alcohol dehydrogenase E from E. coli (relevant to a bifunctional acetaldehyde/alcohol dehydrogenase) (p.1869, FIG. 1). Waks teaches that conversion of biomass into formate, which can subsequently be processed into biologically produced hydrogen from renewable biomass is an attractive replacement for fossil fuels (abstract).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the recombinant yeast of Gunawardena in view of Nestlé and Shalel-Levanon to further add a heterologous polypeptide having bifunctional acetaldehyde/alcohol dehydrogenase activity taught by Waks. Both Gunawardena and Waks teach the production of biofuels from biomass. One of ordinary skill in the art would have been motivated to do so because Waks teaches that yeast were able to further increase formate production 4.5-fold higher with the addition of the enzyme, and formate can be subsequently processed into hydrogen. One of ordinary skill in the art would have found it beneficial to further increase formate production by adding a bifunctional acetaldehyde/alcohol dehydrogenase enzyme to the yeast, because increasing formate production would result in increased production of yeast-based biohydrogen.
Regarding claims 102, 104 and 106, Gunawardena, Nestlé and Shalel-Levanon do not teach wherein said recombinant yeast comprises a down regulation in the expression of one or more native enzymes that function to reduce glycerol synthesis and wherein said recombinant yeast produces less glycerol than a control recombinant yeast with native enzymes that function to produce glycerol (claim 102); wherein said recombinant yeast further comprises a deletion in one or more native enzymes that function to produce glycerol (claim 104); or the recombinant yeast further comprising a deletion of one or more native enzymes encoded by an fdh1 polynucleotide, an fdh2 polynucleotide, or both (claim 106).
However, Waks teaches engineering yeast to secrete formate through the deletion of the endogenous formate dehydrogenases (FDHs) (p.1868, 1st column 1st paragraph). Waks teaches FDH1 and FDH2 deletions were performed in series (relevant to further comprising a deletion of one or more native enzymes encoded by an fdh1 polynucleotide, an fdh2 polynucleotide, or both an fdh1 polynucleotide and an fdh2 polynucleotide) (p.1868, 2nd column – Construction of S. cerevisiae strains). Waks teaches that since the goal was to engineer yeast to secrete formate, they created a ΔFDH1 ΔFDH2 double-deletion mutant and integrated pflA, pflB and adhE to create formate-overproducing strains (p.1869, 2nd column – Results Construction of a formate-producing pathway in S. cerevisiae). Waks teaches formate concentration in the medium was increased by 18-fold in the FDH deletion background (p.1868, 1st column 1st paragraph).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the recombinant yeast of Gunawardena in view of Nestlé and Shalel-Levanon to delete the fdh1 and fdh2 genes encoding native enzymes that function to produce glycerol taught by Waks. One of ordinary skill in the art would have been motivated to delete the native enzymes encoded by an fdh1 polynucleotide and fdh2 polynucleotide, because Waks teaches FDH deletion increased formate concentration by 18-fold.
Regarding claims 110-111, Gunawardena, Nestlé and Shalel-Levanon are silent as to whether said recombinant yeast produces an amount of formate of at least 0.012 g/L in 24 hours (claim 110) or at least 1.0-fold, 5.0-fold, or 10.0-fold more formate than is produced by a recombinant yeast lacking the first and/or second pyruvate formate lyase (claim 111).
However, Waks teaches that at 24 hours, maximum formate production was about 2200 µM for strain PSY3649 (relevant to claim 110) (p.1871, FIG. 3). Using a molecular weight of 46.03 g/mol for formate, 2200 µM is equal to 0.1 g/L, which overlaps with the claimed range of at least 0.012 g/L in 24 hours.
Waks teaches that an 18-fold formate increase was achieved in a strain background whose formate degradation pathway had been deleted (relevant to claim 111: wherein said recombinant yeast produces a formate yield of at least 1.0-fold, 5.0-fold, or 10.0-fold more formate) (abstract).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to produce an amount of formate of at least 0.012 g/L and a formate yield of at least 1.0-fold, 5.0-fold or 10.0-fold more formate, because having the pyruvate formate lyase enzyme will necessarily cause an increase in formate. Gunawardena in view of Nestlé and Shalel-Levanon teach a recombinant yeast comprising the same pyruvate formate lyase as the claimed invention. Thus, the recombinant yeast of Gunawardena in view of Nestlé and Shalel-Levanon would necessarily produce the desired amount of formate and an increased formate yield.
Claims 103 and 105 are rejected under pre-AIA 35 U.S.C. 103(a) as being unpatentable over Gunawardena et al. (WO 2008/080124 A2, published July 3, 2008; previously cited) in view of Nestlé (EP 1 227 152 A1, published on July 31, 2002; previously cited), Shalel-Levanon et al. (“Effect of ArcA and FNR on the Expression of Genes Related to the Oxygen Regulation and the Glycolysis Pathway in Escherichia coli Under Microaerobic Growth Conditions”, Biotechnology and Bioengineering, 2005, Vol. 92, Issue 2, pp.147-159) and Waks et al. (“Engineering a Synthetic Dual-Organism System for Hydrogen Production”, Applied and Environmental Microbiology, 2009, Vol. 75, No.7, pp.1867-1875; previously cited) as applied to claims 102 and 104 above, and further in view of Medina et al. (“Elimination of Glycerol Production in Anaerobic Cultures of a Saccharomyces cerevisiae Strain Engineered To Use Acetic Acid as an Electron Acceptor”, Applied and Environmental Microbiology, 2010, Vol. 76, No.1, pp.190-195; previously cited).
The teachings of Gunawardena, Nestlé, Shalel-Levanon and Waks are discussed above.
Regarding claims 103 and 105, Gunawardena, Nestlé, Shalel-Levanon and Waks do not teach wherein one or more native enzymes are encoded by a gpd1 polynucleotide or a gpd2 polynucleotide.
However, Medina teaches that a major challenge to yeast-based ethanol production is that substantial amounts of glycerol are invariably produced as a by-product (p.190, 1st column, 1st paragraph). Medina teaches deletion of two genes encoding NAD-dependent glycerol-3-phosphate dehydrogenase (GPD1 and GPD2) led to elimination of glycerol production (abstract). Medina teaches that in Saccharomyces cerevisiae, glycerol production is essential to reoxidize NADH produced in a biosynthetic processes (abstract). Medina teaches that eliminating glycerol production led to an alternate pathway of acetate reduction into ethanol as the mechanism for NADH reoxidation, thereby increasing ethanol yields (abstract).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified the recombinant yeast taught by Gunawardena, Nestlé, Shalel-Levanon and Waks to further delete native enzymes encoded by GPD1 and GPD2 taught by Medina, because Medina teaches deleting these two genes eliminated glycerol production in Saccharomyces cerevisiae. One of ordinary skill in the art would have been motivated to delete the native genes responsible for glycerol synthesis in yeast, because Medina teaches that glycerol production is a major challenge to yeast-based ethanol production. One of ordinary skill in the art would have found it beneficial to eliminate glycerol synthesis in yeast because Medina teaches that eliminating glycerol production led to acetate reduction into ethanol, thereby increasing ethanol yields and increasing bioethanol formation in yeast.
Claims 100-101 are rejected under pre-AIA 35 U.S.C. 103(a) as being unpatentable over Gunawardena et al. (WO 2008/080124 A2, published July 3, 2008; previously cited) in view of Nestlé (EP 1 227 152 A1, published on July 31, 2002; previously cited) and Shalel-Levanon et al. (“Effect of ArcA and FNR on the Expression of Genes Related to the Oxygen Regulation and the Glycolysis Pathway in Escherichia coli Under Microaerobic Growth Conditions”, Biotechnology and Bioengineering, 2005, Vol. 92, Issue 2, pp.147-159) as applied to claims 96 and 98 above, and Waks et al. (“Engineering a Synthetic Dual-Organism System for Hydrogen Production”, Applied and Environmental Microbiology, 2009, Vol. 75, No.7, pp.1867-1875; previously cited) as applied to claim 99 above, and further in view of Tokuhiro et al. (JP 2010-239925A, published on October 28, 2010; previously cited). As the original Tokuhiro reference is in Japanese, an English translation is relied upon for support.
The teachings of Gunawardena, Nestlé, Shalel-Levanon and Waks are discussed above.
Regarding claims 100-101, Gunawardena, Nestlé, Shalel-Levanon and Waks do not teach wherein the bifunctional acetaldehyde/alcohol dehydrogenase is from Bifidobacterium adolescentis.
However, Tokuhiro teaches a recombinant yeast that has improved xylose utilization and expression of the gene which codes acetaldehyde dehydrogenase (English translation p.2, paragraph 6). Tokuhiro teaches that the acetaldehyde dehydrogenase that converts acetyl CoA to acetaldehyde can suppress glycerol as a by-product at the same time as the improvement of ethanol yield and the ability to use xylose (English translation p.2, paragraph 6). Tokuhiro teaches that the gene encoding the acetaldehyde dehydrogenase is preferably derived from Bifidobacterium adolescentis (English translation p.2, paragraph 8). SEQ ID NO: 4 taught by Tokuhiro has 100% sequence homology to instant SEQ ID NO:100. Thus, Tokuhiro teaches a bifunctional acetaldehyde/alcohol dehydrogenase comprising the amino acid sequence of SEQ ID NO:100.
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to modify the recombinant yeast taught by Gunawardena in view of Nestlé, Shalel-Levanon and Waks to replace the bifunctional acetaldehyde/alcohol dehydrogenase taught by Waks with the acetaldehyde/alcohol dehydrogenase taught by Tokuhiro to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to select the bifunctional acetaldehyde/alcohol dehydrogenase taught by Tokuhiro because Tokuhiro teaches that the bifunctional enzyme from B. adolescentis can suppress glycerol as a by-product while also improving ethanol yield and the ability to use xylose. One of ordinary skill in the art would have found it beneficial to further suppress glycerol and improve ethanol yield from the yeast.
Claims 112-114 are rejected under pre-AIA 35 U.S.C. 103(a) as being unpatentable over Gunawardena et al. (WO 2008/080124 A2, published July 3, 2008; previously cited) in view of Nestlé (EP 1 227 152 A1, published on July 31, 2002; previously cited) and Shalel-Levanon et al. (“Effect of ArcA and FNR on the Expression of Genes Related to the Oxygen Regulation and the Glycolysis Pathway in Escherichia coli Under Microaerobic Growth Conditions”, Biotechnology and Bioengineering, 2005, Vol. 92, Issue 2, pp.147-159) as applied to claim 96 above, and further in view of Tokuhiro et al. (JP 2010-239925A, published on October 28, 2010; previously cited). As the original Tokuhiro reference is in Japanese, an English translation is relied upon for support.
The teachings of Gunawardena, Nestlé and Shalel-Levanon are discussed above.
Regarding claims 112-114, Gunawardena, Nestlé and Shalel-Levanon do not teach wherein said recombinant yeast further comprises a heterologous saccharolytic enzyme (claim 112), wherein said saccharolytic enzyme is selected from pentose sugar utilizing enzymes (claim 113), or wherein said amylases comprises a glucoamylase (claim 114).
Claim 114 is being interpreted to require the amylase to comprise a glucoamylase if the saccharolytic enzyme is selected to be an amylase. However, claim 114 does not require that the saccharolytic enzyme is an amylase, and therefore is considered obvious over Gunawardena in view of Nestlé and Tokuhiro.
However, Tokuhiro teaches the transformed yeast may secrete and express cellulase and hemicellulase, and other biomass degrading enzymes such as xylanase (relevant to claim 112: wherein said recombinant yeast further comprises a heterologous saccharolytic enzyme) (English translation p.5, paragraph 7). Tokuhiro further teaches preparation of yeast Saccharomyces cerevisiae having xylose metabolizing enzyme gene (relevant to wherein said saccharolytic enzyme is selected from pentose sugar utilizing enzymes) (English translation p.6, paragraph 6). Tokuhiro teaches xylose isomerase gene derived from Piromyces sp. E2 (relevant to a heterologous saccharolytic enzyme) (English translation p.6, paragraph 7). Tokuhiro teaches converting renewable biomass into useful substances such as ethanol using biomass as a raw material (English translation p.1, Description). Tokuhiro teaches that yeasts cannot generally use xylose, but in order to ferment lignocellulose efficiently as a raw material, it is required that yeast be modified so that xylose can be used (English translation p.1, last 2 paragraphs).
It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to further include cellulase, hemicellulase or xylose isomerase taught by Tokuhiro in the recombinant yeast of Gunawardena in view of Nestlé and Shalel-Levanon to arrive at the claimed invention. One of ordinary skill in the art would have been motivated to do so because Tokuhiro teaches being able to utilize xylose can increase ethanol yield and allow yeast to utilize lignocellulose as a raw material. One of ordinary skill in the art would have found it beneficial to create a yeast that can convert renewable biomass into ethanol.
Response to Arguments
Applicant argues that Gunawardena merely suggests that a recombinant yeast can be engineered to express the E. coli pyruvate formate lyases in prophetic examples, but fails to teach that E. coli pyruvate formate lyases can actually be functional, and no data is provided in the prophetic examples 14-16 and 31-32 (See Remarks dated 11/25/2025, p.9 1st paragraph). Applicant further argues that one of ordinary skill in the art would appreciate that PFL enzymes that are functional in their native host does not predict that the PFL enzymes will be functional in a non-native host such as a recombinant yeast (See Remarks dated 11/25/2025, p.9 1st paragraph). Applicant argues that the specification discloses a recombinant yeast strain M3625 in Example 8 which comprises both a “pflA” and “pflB” from B. adolescentis which is able to produce formate and exhibit glucoamylase activity, and in example 9 strains M3515 and M3624 were engineered to express the PFL enzymes from B. adolescentis as well as include deletions in native gpd1, fdh1 and fdh2 genes which produced more formate, less glycerol and more ethanol than the control yeast strain (See Remarks dated 11/25/2025, p.10). Applicant further refers to Example 11 to demonstrate that two heterologous B. adolescentis PFL enzymes were able to be functional in yeast and were able to be expressed at the same time and maintain functionality in yeast (See remarks dated 11/25/2025, p.10 – p.11 top 2 lines).
Applicant's arguments filed November 25, 2025 have been fully considered but they are not persuasive. In response to applicant's arguments against the references individually, one cannot show nonobviousness by attacking references individually where the rejections are based on combinations of references. See In re Keller, 642 F.2d 413, 208 USPQ 871 (CCPA 1981); In re Merck & Co., 800 F.2d 1091, 231 USPQ 375 (Fed. Cir. 1986).
As Applicant states, Gunawardena teaches that methods of gene cloning using vectors for expression in Saccharomyces cerevisiae yeast were well-known and established in the art (Gunawardena p.36, [00176]). Nestlé teaches a host that contains a recombinant vector containing a polynucleotide encoding a fusion protein comprising SEQ ID NO:555, which has 100% homology to instant SEQ ID NO:60 (Nestle p.67, claims 5, 6, and 9). Thus, it would have been obvious to one of ordinary skill that replacing the pyruvate formate lyase taught by Gunawardena with the pyruvate formate lyase taught by Nestlé in the yeast host taught by Gunawardena would predictably result in a yeast host comprising a heterologous pyruvate formate lyase as required by instant claim 96. The instantly required structure of a recombinant yeast comprising a first and second pyruvate formate lyase is taught by Gunawardena. The function of the host in producing butanol, ethanol or any other product does not materially change the required structure of a recombinant yeast comprising a first and second heterologous pyruvate formate lyase.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to DEEPA MISHRA whose telephone number is (571) 272-6464. The examiner can normally be reached Monday - Friday 9:30am - 3:30pm EST.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Louise W. Humphrey can be reached at (571) 272-5543. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/LOUISE W HUMPHREY/Supervisory Patent Examiner, Art Unit 1657
/DEEPA MISHRA/Examiner, Art Unit 1657