DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Action Is Final, Necessitated by Amendment
Applicants' response to the Non-Final Office Action mailed on 24 September 2025, has been entered and the Remarks therein, filed on 03 November 2025, are fully considered here.
This action is a Final Office Action, based on new grounds under 35 U.S.C. §103 over Akiyama as evidenced by Burgos et al. in view of Li et al., and Yonehara et al., necessitated by Applicants’ amendment received on 03 November 2025, specifically, amended claim 1 and canceled claim 8. See MPEP 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
Status of Claims
Claims 1-7 and 9-18 are pending.
Claims 2-7, 9-11 and 14-18 are withdrawn from consideration as being drawn to nonelected species. Election was made without traverse in the reply filed on 14 July 2025 to the Restriction/Election Office Action mailed 08 July 2025.
Claims 1 and 12-13 are rejected.
Claim 1 is objected to.
Priority
Applicant’s claim for the benefit of a prior-filed application under 35 U.S.C. §119(e) or under 35 U.S.C. §120, §121, or §365(c) is acknowledged. As noted in the Non-Final Office Action mailed on 24 September 2025, Applicant has complied with all of the conditions for receiving the benefit of an earlier filing date under 35 U.S.C. §120 or §365(c).
Claims 1 and 12-13 have the effective filing date of 29 June 2021.
Application Data Sheet
[This issue was cited in the Non-Final Office Action mailed on 24 September 2025.]
It is noted that the Application Data Sheet (ADS) received 12 April 2023 contains an error. The PCT document (i.e., PCT/CN2022/100139) is listed in the Foreign Priority Information section and not in the Domestic Benefit/National Stage Information section of the ADS.
Applications filed on or after 16 September 2012 must adhere to the rules for correcting or updating incorrect information by submitting a new ADS, as per MPEP 601.05(a), which reads, in part, per 37 CFR 1.76:
(c) Correcting and updating an application data sheet.
(1) Information in a previously submitted application data sheet, inventor's oath or declaration under § 1.63, § 1.64 or § 1.67, or otherwise of record, may be corrected or updated until payment of the issue fee by a new application data sheet providing corrected or updated information, except that inventorship changes must comply with the requirements of § 1.48, foreign priority and domestic benefit information changes must comply with §§ 1.55 and 1.78, and correspondence address changes are governed by § 1.33(a).
(2) An application data sheet providing corrected or updated information may include all of the sections listed in paragraph (b) of this section or only those sections containing changed or updated information. The application data sheet must include the section headings listed in paragraph (b) of this section for each section included in the application data sheet, and must identify the information that is being changed, with underlining for insertions, and strike-through or brackets for text removed, except that identification of information being changed is not required for an application data sheet included with an initial submission under 35 U.S.C. §371.
Claim Objections
The objections to Claims 1 and 12, in the Non-Final Office Action mailed on 24 September 2025, are partly withdrawn in view of Applicants' amendment received on 03 November 2025, in which the cited claims were amended.
Claim 1 is objected to because of the following informalities:
(1) Claim 1 recites: "An adenosine-involved enzymatic synthesis method for NMN...", which should read: "An adenosine-involved enzymatic synthesis method for nicotinamide mononucleotide (NMN)..." or "An adenosine-involved enzymatic synthesis method for β-nicotinamide mononucleotide (NMN)..."
As indicated in the last office action, any abbreviation should be preceded by the full name represented by said abbreviation at the first recitation of each abbreviation.
(2) Claim 1 recites: "...into the sampe pot...", which should read: "...into the same pot...", because the word 'same' is misspelled.
(3) Claim 1 recites: "...and carry out...", which should read, for the purpose of grammatical consistency: "...and to carry out..."
Appropriate correction is required.
Claim Rejections - 35 U.S.C. § 112
35 U.S.C. § 112(b)
The rejection of Claims 1, 8, 12 and 13 under 35 U.S.C. §112(b) or 35 U.S.C. §112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor, or for pre-AIA the applicant regards as the invention, in the Non-Final Office Action mailed on 24 September 2025, is withdrawn in view of Applicants’ amendment received on 03 November 2025, in which the cited claims were amended or canceled.
Claim Rejections - 35 U.S.C. § 103
The rejection of Claims 1, 8, 12 and 13 under 35 U.S.C. §103 as being unpatentable over Akiyama as evidenced by Burgos et al. in view of Li et al., and Yonehara et al. as evidenced by Kadowaki et al., in the Non-Final Office Action mailed on 24 September 2025, is withdrawn in view of Applicants' amendment received on 03 November 2025, in which claim 8 was canceled and a new limitation was added.
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.
Claims 1, 12 and 13 are rejected under 35 U.S.C. §103 as being unpatentable over Akiyama (Pub. No. US 2020/0332332 A1) as evidenced by Burgos et al. (Biochem. 2008, 47: 11086-11096) in view of Li et al. (Bioprocess Biosyst. Eng. 2010, 33: 675-682) and Yonehara et al. (Agric. Biol. Chem. 1986, 50(4): 899-905).
Akiyama as evidenced by Burgos et al. addresses some of the limitations of claim 1.
Regarding claim 1, pertaining to an adenosine-involved enzymatic synthesis method for NMN (nicotinamide mononucleotide) comprising: adding adenosine, phosphate (Pi), carbohydrate, yeast cells, nicotinamide phosphoribosyltransferase (NAMPT), nicotinamide (NAM), ribose, and phosphoribosyl pyrophosphate (PRPP) into the same pot to carry out an energy metabolism step for generating adenosine triphosphate (ATP) from adenosine, Pi, and carbohydrate; to carry out an enzymatic reaction step to produce NMN by reacting NAM, PPRP and ATP via the action of NAMPT; removing Pi via its incorporation into the ATP (re)generation as described,
Akiyama shows a method for producing nicotinamide mononucleotide (NMN). The method comprises bringing a transformant with enhanced expression of the enzymes nicotinamide phosphoribosyltransferase (Nampt), phosphoribosyl pyrophosphate synthetase (Prs) and polyphosphate kinase (Ppk) into contact with a mixture containing ribose-5-phosphate (R5P), nicotinamide (NAM), ATP and polyphosphate (Abstract). Prs is an enzyme which generates PRPP [5-phosphoribose-1-pyrophosphate] (pg. 1, para. [0004]; pg. 2, para. [0027]; and Figure 1). FIG. 1 is a schematic diagram showing reactions that proceed in the method for producing NMN according to the described invention [see below] (pg. 4, para. [0053]; and Fig. 1).
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It is noted that Figure 1 shows an ATP (re)generating step, per instant claim 1. Akiyama shows that the production method of the described invention utilizes an ATP regeneration reaction to produce NMN (pg. 4, para. [0049]). Enzymatic parameters or chemical equilibrium has been reported to shift in favor of NMN generation by the autophosphorylation of Nampt through the hydrolysis of ATP (pg. 5, para. [0086]). Ppk is an enzyme that is utilized to regenerate ATP from ADP (pg. 5, para. [0094] [PpK = polyphosphate kinase]). Ppk2 can be further classified into three subfamilies, class 1, class 2 and class 3. Ppk2 class 1 and Ppk2 class 2 catalyze a reaction to generate ATP by phosphorylating ADP, and a reaction to generate ADP by phosphorylating AMP, respectively (pg. 5, para. [0096]).
As noted above, Nampt mediates the synthesis of NMN from PRPP and NAM (and ATP), per instant claim 1.
The host of the transformant is not particularly limited as long as the cells can express a predetermined enzyme. Examples thereof include yeasts (e.g., the genus Saccharomyces, the genus Candida and the genus Pichia) (pg. 6, para. [0102]).
With regard to the second and third reactions cited in Figure 1 above, both the reactions can be performed by coupling with the ATP regeneration reaction so that the reactions are allowed to proceed efficiently while the consumed ATP is compensated for. Therefore, the second reaction and the third reaction can be performed in the same system so that the third reaction with Nampt is immediately performed after PRPP generation (pg. 10, para. [0144]). The second reaction and the third reaction may be
combined with the first reaction coupled to the ATP regeneration reaction (pg. 10, para. [0145] [i.e., in the same pot]).
Akiyama does not explicitly show that the reaction of NAM, PRPP and ATP results not only in production of NMN but also ADP and phosphate, with regard to claim 1.
Burgos et al. shows that the combination of NAM, PRPP and ATP results in the synthesis of NMN, ADP and phosphate in the presence of the enzyme Nampt.
An experiment to evaluate the effects of ATP, the kinetic parameters for NAM and PRPP were determined without ATP, in the presence of Pi, and with ATP (Scheme 2) (pg. 11091, column 2, para. 1; and column 1, Scheme 2). Scheme 2 shows that NAM + PRPP + ATP produce NMN + PPi and ADP + Pi in the presence of NAMPT (pg. 11091, column 1, Scheme 2 [PPi and Pi = inorganic phosphate]).
Akiyama does not explicitly show: 1) generate adenosine triphosphate (ATP) from adenosine, phosphate and carbohydrate metabolizable by the yeast cells (i.e., an adenosine-involved enzymatic synthesis method) [Claim 1].
Li et al. and Yonehara et al. provide information from which one of ordinary skill in the art of generating ATP in yeast cells would have understood that yeast can produce ATP from adenosine, phosphate and a carbohydrate, by way of addressing the limitations of claim 1.
Regarding claim 1, Li et al. shows the use of permeated yeast cells to synthesize glutathione (pg. 675, column 1, Abstract). The biosynthesis of glutathione (GSH) in cells involves two consecutive, ATP-dependent reactions catalyzed by γ-glutamylcysteine synthetase and GSH synthetase (pg. 675, column 2, para. 1 [nexus to Akiyama- requirement of ATP in an enzymatic reaction to produce a desired compound]). Permeated yeast cells were used as the catalyst to synthesize GSH from the precursor amino acids, and glucose was used to provide ATP by the cellular activities in the glycolytic pathway (pg. 676, column 1, para. 1). That is, the described results indicated that the cellular activities in the glycolysis and GSH synthesis pathways functioned well and GSH could be synthesized even without addition of ATP (pg. 677, column 2, para. 1).
That is, Li et al. shows an ATP-coupled reaction system in order to produce GSH in which the ATP was supplied by yeast cells which fermented glucose in the metabolic glycolytic pathway.
Regarding claim 1, Yonehara et al. shows an ATP production system involving the oxidation of methanol, oxidative phosphorylation of ADP and phosphorylation of adenosine with sorbitol-treated cells of Candida boidinii No. 2201 (pg. 899, Abstract). Described here is an ATP production system from AMP, adenosine or adenine using cells of the methanol yeast Candida boidinii No. 2201 (pg. 899, column 1, para. 1). Figure 2 shows a typical time course of ATP production by C. boidinii No. 2201 cells under the standard reaction conditions. ATP increased rather gradually as compared with adenosine consumption until 10-hr incubation (pg. 900, column 2, para. 1; and pg. 901, column 1, Fig. 2). The standard reaction mixture contained, minimally, K2HPO4, Na4P2O7, adenosine, methanol, sorbitol and MgSO4 (pg. 899, column 2, last para. thru pg. 900, lines 1-5).
That is, Yonehara et al. shows that yeast cells can produce ATP from adenosine, phosphate and a metabolizable carbohydrate source (here, sorbitol to drive the oxidation of methanol).
Accordingly, 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 enzymatic synthesis method for nicotinamide mononucleotide (NMN), as shown by Akiyama, by including a step in which ATP is generated in yeast cells by combining adenosine, phosphate and a carbohydrate [Claim 1], with a reasonable expectation of success.
Akiyama teaches that the method for producing NMN can be performed by using yeast cells as hosts for the transformant carrying the specified genes coding for specific enzymes involved in the method (i.e., Rbk, Prs and Nampt). Therefore, in addition to the contribution of the Ppk enzymes which are involved in the generation of ATP from ADP and/or AMP, it would have been obvious to have also expected that the yeast host cells would have also generated ATP from adenosine, phosphate and carbohydrate, as shown by Li et al. and Yonehara et al., which show that ATP generation is an inherent property of yeast (in fact, of all living) cells (MPEP 2143 (I)(G) and MPEP 2144 (I)).
One of ordinary skill in the art would have been motivated to have made that modification, because Akiyama teaches that NMN synthesis is favored in the presence of ATP due to the ability of the Nampt enzyme to autophosphorylate by hydrolyzing ATP. Therefore, one of ordinary skill in the art of producing NMN would have been motivated to have included an ATP generation step, in addition to a(n) NMN synthesis step, in the production method. In addition, Li et al. shows that ATP generation is coupled to the increased production of a desired product (i.e., glutathione), which is the type of ATP-coupled enzymatic reaction shown by Akiyama (MPEP 2143 (I)(G).
Therefore, the invention as a whole would have been prima facie obvious to a person of ordinary skill before the effective filing date of the claimed invention.
Akiyama et al. further addresses the limitations of claims 12 and 13.
Regarding claim 12, and
regarding claim 13, pertaining to magnesium ion,
Akiyama shows that a compound other than the starting materials may be brought into contact with the transformant with enhanced expression of each predetermined enzyme. For example, metal ions such as magnesium ions are appropriately contained as a component for allowing each enzyme to exert its functions (pg. 10, para. [0150]).
Response to Arguments
Applicant’s arguments, pp. 6-12, filed on 03 November 2025, with respect to the prior art references cited in the 35 U.S.C. §103 rejection, have been fully considered but they are either not persuasive or are moot because the arguments do not apply to the references as they are applied in the context of the current rejection, or as new grounds necessitated by Applicant’s amendment, in which claim 1 was amended and claim 8 was canceled.
1. Applicant remarks (pg. 6, para. 5-6 thru pg. 7), with regard to the nature of a 103 rejection, that it is apparent that to be qualified as a prior art under 35USC103, the prior art must be cited under 35USC102, but the disclosure of the prior art and the claimed invention are not identical and there are one or more differences between the subject matter sought to be patented and the prior art. The differences between the subject matter sought to be patented as a whole of the instant invention and Akiyama which is qualified as prior art of the instant invention under 35USC 102 are obvious in view of the supplemental arts at the time the claimed invention was made to a person having ordinary skill in the art to which the subject matter pertains.
However, in response to Applicant, Applicant has misquoted the proper definition of a 103 rejection under AIA First-to-file (FITF) guidance, which is how the instant application has been categorized. Applicant has quoted the pre-AIA 35 USC 103(a) paragraph in his/her paragraph 5. On the other hand, the rubric for determining obviousness is essentially the same (MPEP 2141). The determination of obviousness under 103 does not require an applied prior art reference to qualify as 102 art (MPEP 2142). Indeed, the primary reference of Akiyama has not been cited in a 102 anticipation or novelty rejection. The reference to section 102 in the 103 conditions for patentability paragraph (cited above) is in the following context: "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,..."
2. Applicant remarks (pg. 7, para. 7-9), with regard to the primary reference of Akiyama, that Akiyama merely discloses a method for producing NMN by enzymatically NR in the presence of ATP, typically using NRK or related kinases; the process relies on supplying ATP externally as an energy donor in a conventional enzyme-catalyzed reaction system, and does not involve in situ ATP regeneration, yeast cell metabolism, or integration with additional energy-producing pathways. Akiyama does not teach placing adenosine plus phosphate, carbohydrate, NAMPT, PRPP, ribose, nicotinamide and yeast cells together in a single same pot to perform a coupled energy-metabolism/enzymatic synthesis and to enable automatic recycling of ADP + phosphate back to ATP by yeast oxidative phosphorylation. The ADP and phosphate produced by NAMPT are automatically recycled by the same yeast cells to regenerate ATP.
However, in response to Applicant, Akiyama does show an inclusive 'same pot' system which encompasses three (enzymatic) reactions, as shown in Figure 1 of Akiyama (see above). Although ATP regeneration does not take place by the specific method of yeast cells metabolizing adenosine, Pi and carbohydrate (as conceded above in the 'does not explicitly show' statement), it would have been obvious to have utilized the yeast cells, taught by Akiyama, to (re)generate ATP, because, as taught by Li et al. and Yonehara et al., yeast can (inherently) generate ATP from adenosine, Pi and carbohydrate. Li et al. shows a typical, yeast-associated ATP-coupled regeneration system, such as the system shown by Akiyama, and Yonehara et al. teaches the specific utilization of adenosine, phosphate compounds and the carbohydrate sorbitol to generate ATP in Candida yeast.
3. Applicant remarks (pg. 7, para. 10 thru pg. 8) that Burgos et al. investigates the enzymatic properties of human nicotinamide phosphoribosyltransferase (NAMPT). However, Burgos et al. do not disclose or suggest any system in which ATP is generated in situ as claimed. In Burgo et al., ATP is added externally as a reagent and is consumed during the in-vitro kinetic assay. The reference does not describe any ATP-regeneration mechanism. Burgos et al. cannot anticipate or render obvious the claimed adenosine-involved, yeast-driven, single pot enzymatic synthesis of NMN.
However, in response to Applicant, Burgos et al. is cited as an evidentiary reference to show that the chemical reaction of NAM, PRPP and ATP, as shown by Akiyama, not only results in the production of NMN, but also ADP and phosphate. It is not necessary for Burgos et al. to show the adenosine-involved enzymatic synthesis method for NMN, as instantly-claimed, in order to support the 103 rejection over Akiyama as a secondary reference (whether as an "in view of" reference or an "as evidenced by" reference) (see MPEP 2141 and the KSR decision).
4. Applicant remarks (pg. 8, para. 11) that Li et al. merely disclosures commonly require externally supplied ATP or enzyme-based ATP regeneration (polyphosphate kinase, acetate kinase, etc.). They do not generally disclose a one-pot system where adenosine is provided and yeast perform oxidative phosphorylation to regenerate ATP from adenosine/phosphate/carbohydrate while NAMPT uses that ATP in the same pot.
However, in response to Applicant, Li et al. was cited to show that naturally-occurring yeast cells (e.g., those taught by Akiyama) harbor ATP regeneration systems as an inherent property of the cell, without the need for external addition of ATP. As applied here as a secondary reference, Li et al. is not required to show the instantly-claimed invention.
5. Applicant remarks (pg. 8, para. 12-15 thru pg. 9) that Yonehara et al. supports that yeast cells can generate ATP from adenosine via energy metabolism. However, Yonehara et al. are limited to describing an isolated ATP production system, not an integrated ATP regeneration system coupled to any enzymatic biosynthesis process. The reference does not identify or confirm the specific intracellular enzymes responsible for converting adenosine to ATP, nor does it describe maintaining all such enzymes in an active, coupled system within a single reaction pot. The reference remains silent as to coupled NAD/NMN biosynthesis, NAMPT catalysis, or self-regenerative phosphate utilization within a single reaction system.
However, in response to Applicant, the claimed subject matter also does not identify particular intracellular enzymes responsible for converting adenosine to ATP. Yonehara et al. was cited to show that yeast (in particular a Candida sp.) can produce ATP via the oxidative phosphorylation of ADP and phosphorylation of adenosine. Yonehara et al. also shows that the reaction involving ATP production involves adenosine, phosphate "donated" by a phosphate compound, and the carbohydrate sorbitol. The reference was used to address the limitation that Akiyama does not show. As applied here as a secondary reference, Yonehara et al. is not required to show the instantly-claimed invention.
6. Applicant remarks (pg. 9, para. 16-18 thru pg. 10) against the reference of Kadowaki et al..
However, Kadowaki et al. is not cited in this Office Action.
7. Applicant remarks (pg. 10, para. 19) that even if one is to combine the references as proposed by the Examiner, the combination would require substantial conceptual reconstruction. None of the cited references provide any motivation or reasonable expectation of success for integrating (i) yeast-based ATP production from adenosine and carbohydrate (as in Yonehara et al. or Kadowaki et al.) with (ii) the NAMPT-catalyzed NMN formation (as in Akiyama or Burgos et al.). These processes operate under distinct biochemical conditions, metabolically active yeast cell environments versus purified enzyme reaction buffers, which are not compatible without extensive optimization.
However, in response to Applicant, it is not clear that the ability of yeast cells to (inherently) produce ATP from adenosine, Pi, and carbohydrate requires mechanical integration into the method shown by Akiyama, because Akiyama teaches that yeast cells can be used to perform the described method- and yeast cells inherently produce and regenerate ATP, as shown by Li et al., and Yonehara et al. Applicant's statement that the two processes would not be compatible without extensive optimization appears to be opinion evidence unsupported by factual information (MPEP 716.01 (c)(I)(II)).
8. Applicant remarks (pg. 10, para. 20-23 thru pg. 11) that the instant invention provides an improvement to the ATP regeneration process in the enzymatic synthesis of NMN. Specifically, the adenosine-involved enzymatic NMN synthesis method of the instant invention uses nicotinamide, ribose, adenosine, phosphate, and a carbohydrate metabolizable by yeast cells as raw materials, and ribokinase, RPPK, NAMPT and yeast cells as catalysts. More specifically, in this reaction system in the same pot, yeast cells perform oxidative phosphorylation metabolism. Compared with conventional synthesis methods, the instant invention can utilize the formed phosphate as a reactant, eliminating the need for a phosphate removal process, and realizing ATP recycling without requiring a separate ATP recovery step, thus reducing ATP consumption and simplifying the purification process of the NMN product through adenosine involvement. After completion of the phosphorylation reaction for NMN synthesis, the reaction system of the instant invention still continues the yeast oxidative phosphorylation process. The yeast cells, in effect, participate in a third stage of the reaction, namely, the product purification stage, in which impurities-especially phosphate-are metabolized and removed. As a result, the subsequent separation and purification of NMN become simpler and more efficient.
However, in response to Applicant, Akiyama also shows the incorporation of several enzymes (inherently) produced by yeast, such as ribokinase, polyphosphate kinase (Ppk) and Nampt (as already cited), in the described method for producing NMN. In addition, the Akiyama system describes a phosphate removal process with regard to the phosphate being used to produce or regenerate ATP. That is, phosphate is used as a reactant to form ATP. Akiyama teaches that ATP is regenerated from ADP and/or AMP (pg. 10, para. [0144]). Yonehara et al. also shows that ADP and AMP are reservoirs of phosphate to be used to generate ATP in the presence of adenosine in a sequential manner (pg. 904, Table I). Therefore, it would have been obvious to have cultivated yeast cells, as shown by Akiyama, according to Yonehara et al. in order to regenerate ATP, rather than the method shown by Akiyama.
9. Applicant remarks (pg. 11, para. 24-26 thru pg. 12) that in summary, the technical solution recited in new Claim 1 of the instant invention addresses the specific technical problems in the prior art, namely: (1) the excessive accumulation of phosphate and the difficulty in its removal; (2) the complexity of the reaction system caused by side reactions producing by-products such as nicotinamide, ribose, ADP, AMP, NR (nicotinamide riboside), adenosine, adenine, and phosphate; and (3) the difficulty and high cost of purifying the NMN product, as well as the instability of product quality. The instant invention solves these problems. Accordingly, the applicant believes that neither Akiyama, nor the supplemental arts, separately or in combination, suggests or makes any mention whatsoever of the difference subject features as claimed in the amended claims 1 and 12-13 of the instant invention.
However, in response to Applicant, the reference combination of Akiyama, Li et al., and Yonehara et al. show that there are several pathways by which ATP can be regenerated, one of them by utilizing yeast cells which can metabolize adenosine, phosphate (Pi) and carbohydrate to produce ATP, which is shown by Yonehara et al., and the other by supplying different enzymes (e.g., Rbk (ribokinase) and PPk (polyphosphate kinase)) in a reaction cocktail, as shown by Akiyama (see Fig. 1 above). Because Akiyama shows using yeast cells to produce NMN, it would have been obvious to have used yeast cells to have produced the ATP (required, in part, for the production of NMN) with a reasonably predictable expectation that nicotinamide mononucleotide (NMN) would have been produced.
Conclusion
No claims are allowed.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP 706.07(a). Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any extension fee 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 date of this final action.
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/SMP/Examiner, Art Unit 1651
/Michelle F. Paguio Frising/Primary Examiner, Art Unit 1651