DETAILED ACTION
Objections and rejections raised in prior Office Actions are withdrawn unless restated below.
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 .
withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 07/08/2025 has been entered.
Claim Objections
Claims 1 and 9 are objected to because of the following informalities:
Claims 1 and 9 in the preamble recite “bioproduction of flavonoids and anthocyanins.” In view of the specification, the same is understood as only requiring production of one compound falling within the genus of flavonoids and anthocyanins. See specification, page 3, lines 10-11. That is, it is not considered to be a reasonable interpretation of the claims that production of plural different species of flavonoids and anthocyanins be produced for infringement. As such, the claims should be amended to indicate that production of only one compound is required.
Appropriate correction is required.
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 1-18 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.
“New or amended claims which introduce elements or limitations that are not supported by the as-filed disclosure violate the written description requirement. See, e.g., In re Lukach, 442 F.2d 967, 169 USPQ 795 (CCPA 1971) (subgenus range was not supported by generic disclosure and specific example within the subgenus range); In re Smith, 458 F.2d 1389, 1395, 173 USPQ 679, 683 (CCPA 1972) (an adequate description of a genus may not support claims to a subgenus or species within the genus)”; MPEP 2163(I)(B). “While there is no in haec verba requirement, newly added claims or claim limitations must be supported in the specification through express, implicit, or inherent disclosure.” MPEP 2163(I)(B).
“With respect to newly added or amended claims, applicant should show support in the original disclosure for the new or amended claims. See, e.g., Hyatt v. Dudas, 492 F.3d 1365, 1370, n.4 (Fed. Cir. 2007) (citing MPEP § 2163.04 which provides that a "simple statement such as ‘applicant has not pointed out where the new (or amended) claim is supported, nor does there appear to be a written description of the claim limitation ‘___’ in the application as filed’ may be sufficient where the claim is a new or amended claim, the support for the limitation is not apparent, and applicant has not pointed out where the limitation is supported."); see also MPEP §§ 714.02 and 2163.06 ("Applicant should ... specifically point out the support for any amendments made to the disclosure."); and MPEP § 2163.04.” MPEP 2163(II)(A).
Claims 1 and 9 have been amended to recite a tyrosine ammonia lyase having a sequence at least 95% identical to SEQ ID NO: 1, SEQ ID NO: 23, SEQ ID NO: 24, SEQ ID NO: 25 or SEQ ID NO: 26.
In the beginning of remarks dated 01/29/2026, applicant references several paragraphs of U.S. 2022/0333118 including paras. [0053], which is as follows:
“Tyrosine ammonia-lyase (TAL) can be, for example, a member of the aromatic amino acid deaminase family that catalyzes the elimination of ammonia from L-tyrosine to yield p-coumaric acid. An exemplary tyrosine ammonia lyase is the Saccharothrix espanaensis tyrosine ammonia lyase (TAL; SEQ ID NO: 1). Also considered for use in the engineered cells provided herein are TALs with SEQ ID NOS. 23-26, TALs listed in Table 1, TAL homologs and variants having at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identity to SEQ ID:1 that have the activity of a tyrosine ammonia lyase that produces p-coumaric acid from tyrosine.”
The as-filed specification only discusses TAL homologs having at least 95% identity to a base sequence of SEQ ID NO: 1. There is no disclosure in the as-filed specification of a genus of TAL enzymes having at least 95% identity to any of SEQ ID NOS: 23, 24, 25 and/or 26 as recited in claims 1 and 9 as amended. “While there is no in haec verba requirement, newly added claims or claim limitations must be supported in the specification through express, implicit, or inherent disclosure.” However, here, a disclosure of at least 95% identity to SEQ ID NO: 1 cannot be extended as an implicit disclosure of a genus of other TAL proteins with at least 95% identity to other base sequences being SEQ ID NOS: 23, 24, 25 and/or 26. As such, applicant has not pointed out where the amended claims 1 and 9 are supported, nor does there appear to be a written description of the claim limitation at least 95% identity to SEQ ID NOS: 23, 24, 25 or 26 in the application as-filed, where the support for the limitation is not apparent, and applicant has not sufficiently pointed out where the limitation is supported. The rejected claims do not conform to the written description requirement for these reasons.
Claim Rejections - 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claim(s) 1-20 (all pending claims) is/are rejected under 35 U.S.C. 103 as being unpatentable over Koma et al. (Chromosome Engineering To Generate Plasmid-Free Phenylalanine- and Tyrosine-Overproducing Escherichia coli Strains, Appl. Environ. Microbiol. 86, 2020, e00525-20) (previously cited) further in view of Liu et al. (Construction of a switchable synthetic Escherichia coli for aromatic amino acids by a tunable switch, J. Indust. Microbiol. 47, 2020, 233-242) (previously cited) and Li et al. (U.S. 2019/0367930 A1).
Koma et al., abstract, states:
Many phenylalanine- and tyrosine-producing strains have used plasmid-based overexpression of pathway genes. The resulting strains achieved high titers and yields of phenylalanine and tyrosine. Chromosomally engineered, plasmid-free producers have shown lower titers and yields than plasmid-based strains, but the former are advantageous in terms of cultivation cost and public health/environmental risk. Therefore, we engineered here the Escherichia coli chromosome to create superior phenylalanine- and tyrosine-overproducing strains that did not depend on plasmid-based expression. Integration into the E. coli chromosome of two central metabolic pathway genes (ppsA and tktA) and eight shikimate pathway genes (aroA, aroB, aroC, aroD, aroE, aroGfbr, aroL, and pheAfbr), controlled by the T7lac promoter, resulted in excellent titers and yields of phenylalanine; the superscript “fbr” indicates that the enzyme encoded by the gene was feedback resistant. The generated strain could be changed to be a superior tyrosine-producing strain by replacing pheAfbr with tyrAfbr. A rational approach revealed that integration of seven genes (ppsA, tktA, aroA, aroB, aroC, aroGfbr, and pheAfbr) was necessary as the minimum gene set for high-yield phenylalanine production in E. coli MG1655 (tyrR, adhE, ldhA, pykF, pflDC, and ascF deletant). The phenylalanine- and tyrosine-producing strains were further applied to generate phenyllactic acid-, 4-hydroxyphenyllactic acid-, tyramine-, and tyrosol-producing strains; yield of these aromatic compounds increased proportionally to the increase in phenylalanine and tyrosine yields.
The genes ppsA and tktA and aroA, aroB, aroC, aroD, aroE, aroGfbr, aroL, and pheAfbr under control of a heterologous T7 lac promoter are understood to be overexpressed or upregulated.
Gene aroE encodes shikimate dehydrogenase and tyrA encodes chorismate mutase. “In Tyr synthesis, CA is converted to 4-hydroxyphenylpyruvate (4HPP) by CA [chorismate] mutase/prephenate dehydrogenase, encoded by tyrA.” Koma, page 2. “Similarly, although shikimate dehydrogenase is encoded by both aroE and ydiB, aroE was selected since YdiB catalyzes an undesirable reaction (the reversible conversion of dehydroquinate to quinate).” Koma, page 7. As such, Kona teaches an engineered E. coli host cell comprising plural genetic modifications being upregulation/overexpression of chorismate mutase TyrA, and upregulation/overexpression of shikimate dehydrogenase AroE. However, Koma does not teach deletion of pyruvate oxidase.
Further, Koma teaches that the same tyrosine-overproducing engineered E. coli has “gene encoding a feedback-resistant form of DAHP synthase, aroGfbr,” which meets the features directly recited in claims 2 and 10 for upregulation of 2-deoxy-D-arabino-hepulosonate 7-phosphate (DHAP) synthase.
For claims 3 and 11, the same tyrosine-overproducing engineered E. coli strain has integrated overexpressed aroL gene encoding shikimate kinase (see Table 1 of Koma) as to mee the features of these claims.
For claims 4 and 12, Table 1 of Koma describes a tyrosine-producing E. coli strain having the following genotype (strain M-PAR-242 further includes the features/genotype of strain (last strain in table):
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The above strain in addition to overexpression/upregulation of aroGfbr and aroE has deletion of pheA, which is considered to be a downregulation of L-phenylalanine biosynthetic pathway. “PheA and TyrA determine whether there will be synthesis of Phe and Tyr at the CA node,” such that deletion of pheA downregulates L-phenylalanine biosynthetic pathway. Koma, page 17.
Regarding claims 5 and 13, “Since E. coli imports glucose via a PEP-dependent transfer system (PTS), one molecule of PEP is converted to pyruvate to take up one molecule of glucose into the cell. Therefore, half of the amount of synthesized PEP is consumed without relation to Phe synthesis. Two ways are known to tackle this problem: (i) PEP regeneration from pyruvate by overexpression of a PEP synthase gene (ppsA) and (ii) alteration of the glucose uptake system from PTS to a PTS-independent system such as galactose permease or glucose facilitator.” Koma, page 2. The strains described above including M-PAR-242 overexpress/upregulate ppsA encoding PEP (phosphoenolpyruvate) synthase.
Regarding claims 6 and 14, “Overexpression of tktA was effective to enhance E4P availability.” Koma, page 2. The strains described above including M-PAR-242 overexpress/upregulate tktA encoding transketolase.
Regarding claims 7, 8, 15 and 16, the strains described above including M-PAR-242 have tyrR interrupted by insertion of aroGfbr into the tyrR locus such that tyrR is disrupted. “Deletion of tyrR released these genes from transcriptional repression.” Koma, page 3.
Regarding claims 17 and 18, the strains described above including M-PAR-242 have deletion of ldhA encoding lactate dehydrogenase. “On the other hand, adhE, ldhA, and pflDC deletions were expected to reduce ethanol-, lactic acid-, and formic acid formation, respectively.” Koma, page 4.
However, Koma does not teach deletion of pyruvate oxidase and production of flavonoids or anthocyanin by expression of a tyrosine ammonia lyase having SEQ ID NO: 1.
Li relates to microorganisms engineered to produce tyrosine and tyrosine derivatives. “A biochemical compound to be produced by any of the methods of the invention, or which production is decoupled from the growth of the producing microorganism in accordance of the present invention, may be any carbon-containing compound which can be produced by a living microorganism.” Li, para. [0431]. “According to certain embodiments, the biochemical compound is L-tyrosine or a derivative thereof. Li, para. [0435]. “According to certain embodiments, the L-tyrosine derivative is a compound selected from the group consisting of: p-coumaric acid, caffeic acid, ferulic acid, vanillin, vanillic acid, cinnamic acid, resveratrol, naringenin, fisetin, curcumin and morphine.” Li, para. [0438]. “In order to convert L-tyrosine into the desired derivative, such as p-coumaric acid, the microorganism suitably comprises (e.g., expresses) one or more enzymes catalyzing the chemical reaction(s) leading to the desired derivative. Table 1 below provides an overview of L-tyrosine derivatives and the enzymes involved in the conversion of L-tyrosine into the respective derivative. The microorganism may inherently express the one or more enzymes or may be modified to express the one or more enzymes by using, e.g., DNA recombination techniques.” Li para. [0439].
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“According to certain embodiments, the polypeptide having tyrosine ammonia lyase activity is a polypeptide comprising an amino acid sequence set forth in SEQ ID NO: 7, 8, 9, 10, 11, 12, 13, 14, 15, 16 or 17 (preferably, SEQ ID NO: 7).” Li, para. [0442]. SEQ ID NO: 11 of Li is identical to recited SEQ ID NO: 1.
Further, Li teaches that an embodiment having ability to produce L-tyrosine and its derivatives to further express enzymes of a tyrosine biosynthesis pathway that substantially overlaps those of Koma including: “A microorganism may be considered as having the ability to produce L-tyrosine if it expresses all enzymes involved in the biosynthetic pathway resulting in L-tyrosine. For example, a microorganism may be considered as having the ability to produce L-tyrosine if it expresses the following enzymes: transketolase I (EC 2.2.1.1; encoded by the gene tktA or ortholog thereof); 2-dehydro-3-deoxyphosphoheptonate aldolase (EC 2.5.1.54; encoded by the gene aroG or ortholog thereof); 3-dehydroquinate synthase (EC 4.2.3.4; encoded by the gene aroB or ortholog thereof); 3-dehydroquinate dehydratase (EC 4.2.1.10; encoded by the gene aroD or ortholog thereof); shikimate dehydrogenase (EC 1.1.1.25; encoded by the gene aroE or ortholog thereof); shikimate kinase I (EC 2.7.1.71; encoded by the gene aroK or ortholog thereof); shikimate kinase II (EC 2.7.1.71; encoded by the gene aroL or ortholog thereof); 3-phosphoshikimate-1-carboxyvinyltransferase (EC 2.5.1.19; encoded by the gene aroA or ortholog thereof); chorismate synthase (EC4.2.3.5; encoded by the gene aroC or ortholog thereof); chorismate mutase/prephenate dehydrogenase (EC 5.4.99.5/EC 1.3.1.12; encoded by the gene tyrA or ortholog thereof); and tyrosine aminotransferase (EC 2.6.1.5; encoded by the gene tyrB or ortholog thereof). The microorganism may inherently have the ability to produce L-tyrosine or a derivative thereof or may be modified to have the ability to produce L-tyrosine or a derivative thereof by using, e.g., DNA recombination techniques.” Li et al., para. [0580]. Working examples of Li are implemented in E. coli.
As such, Li teaches that a microorganism that is modified for production of L-tyrosine, including E. coli, can be further modified to produce further valuable derivatives of L-tyrosine, including naringenin that is a flavonoid, by further expression of at least a tyrosine ammonia lyase, including a tyrosine ammonia lyase having recited SEQ ID NO: 1 (SEQ ID NO: 11 of Li). As such, at the time of filing an ordinarily skilled artisan would have been motivated to modify any E. coli modified for L-tyrosine production including the same taught by Koma as discussed above to further express heterologous genes/enzymes for producing a L-tyrosine derivative being the flavonoid naringenin including heterologous expression of a gene (nucleic acid sequence)/enzyme encoding a tyrosine ammonia lyase having recited SEQ ID NO: 1.
Regarding further deletion or downregulation of pyruvate oxidase, Liu, abstract, states:
Escherichia coli, a model microorganism for which convenient metabolic engineering tools are available and that grows quickly in cheap media, has been widely used in the production of valuable chemicals, including aromatic amino acids. As the three aromatic amino acids, L-tryptophan, L-tyrosine, and L-phenylalanine, share the same precursors, to increase the titer of a specific aromatic amino acid, the branch pathways to the others are usually permanently inactivated, which leads to the generation of auxotrophic strains. In this study, a tunable switch that can toggle between different states was constructed. Then, a switchable and non-auxotrophic E. coli strain for synthesis of aromatic amino acids was constructed using this tunable switch. By adding different inducers to cultures, three different production patterns of aromatic amino acids by the engineered strain could be observed. This tunable switch can also be applied in regulating other branch pathways and in other bacteria.
In addition to the tunable switch taught by Liu, Liu teaches modifications to E. coli that are beneficial towards the production of all of L-tryptophan, L-tyrosine, and L-phenylalanine, share the same precursors beginning with a strain GPT100. Table 1 of Liu shows a GPT100 strain having deletion of ackA, poxB, tyrA and aroP genes. The poxB gene is a gene encoding pyruvate oxidase wherein deletion of the same is indicated to reduce acetate production as shown in Fig. 1 of Liu. That is, an ordinarily skilled artisan at the time of filing would understand from Fig. 1 of Liu that deletion of poxB as reducing the conversion of glucose carbon source to acetate as to increase the amount of carbon flow directed towards aromatic amino acid production including any further derivative of L-tyrosine including naringenin as discussed above.
As shown in Fig. 1 of Liu, the engineered E. coli of Liu have many commonalities with Koma including overexpression of tktA, aroG, and aroL. Both Kona and Liu teach that certain endogenous genes of E. coli can be deleted in order to increase carbon flow for tyrosine production by reducing production of other fermentation byproducts. For example, “On the other hand, adhE, ldhA, and pflDC deletions were expected to reduce ethanol-, lactic acid-, and formic acid formation, respectively.” Koma, page 4. Liu teaches that another product for which production can be reduced to benefit increased tyrosine production is acetate wherein: In E. coli, two pathways are mainly responsible for the generation of acetate (Fig. 1). The main and constitutive pathway in E. coli involves phosphate acetyl transferase, encoded by pta, and acetate kinase, encoded by ackA. Another route is through oxidative decarboxylation of pyruvate by pyruvate oxidase PoxB.” Liu, pages 236-37. “[W]e found that this strain with relatively high l-tryptophan [an amino acid made from same shikimate pathway precursors as tyrosine, see Liu, Fig. 1] titer also exhibited high acetate secretion, thus leading to a waste of the carbon source.” Liu, page 236, right col. Fig. 1 of Liu illustrates deletion of poxB. As such, just as Koma teaches that “adhE, ldhA, and pflDC deletions were expected to reduce ethanol-, lactic acid-, and formic acid formation,” an ordinarily skilled artisan at the time of filing would have been further motivated to additionally delete poxB encoding pyruvate oxidase in the tyrosine producing strains otherwise taught by Koma in order to achieve the benefit of reduced acetate production that Koma teaches is beneficial for tyrosine production (i.e. production of acetate is a waste of carbon source).
Regarding claim 9 and claims depending therefrom, all of the above modifications whether deletion or overexpressing/upregulating certain genes/enzymes (i.e. genetic modifications) is done by “preparing” an engineered E. coli host cell to have such genetic modifications, as discussed in the “Materials and Methods” section of Liu (page 235) and “Generation of strains by chromosome engineering” of Koma (page 21).
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 1-20 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-10, 13-38 and 41-62 of copending Application No. 17/720,006 in view of Koma et al. (Chromosome Engineering To Generate Plasmid-Free Phenylalanine- and Tyrosine-Overproducing Escherichia coli Strains, Appl. Environ. Microbiol. 86, 2020, e00525-20), Liu et al. (Construction of a switchable synthetic Escherichia coli for aromatic amino acids by a tunable switch, J. Indust. Microbiol. 47, 2020, 233-242) (previously cited), and Li et al. (U.S. 2019/0367930 A1).
The rejections of claims 1-20 under 35 U.S.C. 103 stated above over Koma, Liu and Li are incorporated herein by reference.
The reference claims include:
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The reference claims recite an engineered host cell for producing a flavonoid that includes expression of a nucleic acid encoding tyrosine ammonia lyase. Koma, Liu and Li, as discussed above teach expression of tyrosine ammonia lyase along with other features of claims 1-20 for production of tyrosine to support production of naringenin, a flavonoid. Just as the prior art of Koma, Liu and Li motivates an ordinarily skilled artisan at the time of filing to produce an embodiment of all of claim 1-20, an ordinarily skilled artisan at time of filing would have similarly been motivated to modify embodiments of the copending claims, particularly copending claim 9, to have the features of claims 1-20 for supporting tyrosine production that is the substrate for tyrosine ammonia lyase and naringenin as discussed above. Again, as discussed, Li in particular teaches that it is beneficial to provide an engineered E. coli expressing tyrosine ammonia lyase along with additional genes and features supporting production of tyrosine and a tyrosine derivative being naringenin in the same host cell such that an ordinarily skilled artisan at time of filing would have similarly been motivated to modify embodiments of the copending claims.
This is a provisional nonstatutory double patenting rejection.
Response to arguments
In brief, applicant points to newly added claim limitations, particularly with respect to a tyrosine ammonium lyase, as overcoming prior grounds of rejection. Claim limitations added to the first time in amendments dated 01/29/2026 are addressed above.
Conclusion
The double patenting rejection is above is necessitated by applicant’s amendment. Applicant amended the claims for the first time in the prior amendment to require an engineered host call that produces a flavonoid and expresses a tyrosine ammonia lyase, which created a claim scope overlap with the reference claims of Ser. No. 17/720,006.
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 TODD M EPSTEIN whose telephone number is (571)272-5141. The examiner can normally be reached Mon-Fri 9:00a-5:30p.
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/TODD M EPSTEIN/Primary Examiner, Art Unit 1652
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