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 .
Claim Rejections - 35 USC § 103
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.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 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.
Claims 1-5, 10 & 12 are rejected under 35 U.S.C. 103 as being unpatentable over Hirano et. al. (US 9,506,094 B2, 29NOV16, hereafter “Hirano).
Regarding claims, 1-5, 10 & 12: A Corynebacterium stationis, (and the culture medium) with purine nucleotide production ability, in which the activity of a phosphate importer system encoded by pit gene wherein the pit gene is PitA (of foreign origin, from E. coli, greater than or equal to 99% or 85% identical to SEQ ID NO: 1).
Hirano teaches two strains of the same species of bacteria as recited in the instant application Corynebacterium stationis (Col. 5, lines 16-17), that can be modified to include the PitA gene from E. coli (Col. 20, lines 14-19 & 45-61) with 100% identity in sequence to Seq ID No: 1 of instant application (Hirano SEQ ID NO: 2).
The teachings of Hirano renders obvious the compositions of claims 1-5, 10 & 12 even though Hirano does not explicitly state that C. stationis has “purine nucleotide production ability”, the specification of the instant application states that this is a wild type trait (instant application specification, page 21). Thus, a C. stationis with the PitA gene from E. coli as taught by Hirano would also have purine nucleotide production ability. Hirano also teaches that the coryneform (explicitly defined as including C. stationis) bacteria is cultured in a medium (Col. 33, line 20-6 of Col. 34).. For details of the sequence alignment please see the file titled SubsetOfTheSequenceAlignmentResults05FEB26.pdf. For the sake of clarity of the record, it is noted that the sequence alignment results refer to Hirano as US 9,476,076 B2 which came from US Patent Application 14/796,326, this document was withdrawn from issue and replaced by US 9,506,094 B2.
Thus, it would have been obvious to one of ordinary skill in the art to combine the optional embodiments of modified coryneform bacteria taught by Hirano with the result of C. stationis with an enhanced phosphate importation activity encoded by PitA from E. coli with the expectation of success. One would have been motivated to do so since Hirano explicitly recites “it is exemplary to increase the activity of the Pit system, and to increase the activity of the PitA protein, which is the pitA gene product” (Col. 20, lines 46-48), with regard to the options for increasing the activity of the phosphate importation system in a coryneform bacteria (to include C. stationis).
Claims 6-9 are rejected under 35 U.S.C. 103 as being unpatentable over Hirano as applied to claims 1-5, 10 & 12 above, and further in view of Lee et. al. (Microorganisms That Produce Purine Nucleotides And Methods Of Producing Purine Nucleotides Using The Same, KR 102185850 B1, 02DEC20, hereafter “Lee”).
Hirano teaches C. stationis with enhanced phosphate importation via modification of the bacteria with the addition of PitA from E. coli and 100% sequence identity to SEQ ID NO: 1 of instant application (Col. 5, lines 16-17, Col. 20, lines 14-19 & 45-61 & SEQ ID NO: 2). Purine production is a wild type trait found in C. stationis as specified in the instant application (instant application specification, page 21).
Hirano does not explicitly recite the production of 5’-inosine monophosphate, 5’-xanthosine monophosphate or 5’-guanosine monophosphate.
However, Lee teaches the production of 5’-inosine monophosphate, 5’-xanthosine monophosphate or 5’-guanosine monophosphate in a C. stationis microorganism with enhanced phosphate importer activity, in a medium wherein the method comprises recovering the purine nucleotides from the cultured medium or the microorganism (Claims section).
Regarding claims 6-9: C. stationis with enhanced phosphate importation encoded by a pit gene wherein the purine nucleotides consist of one or more of the following 5’-inosine monophosphate, 5’-xanthosine monophosphate or 5’-guanosine monophosphate; and the method for producing those purine nucleotides comprising culturing the microorganism and then recovering the nucleotides from the media or the microorganism. Hirano teaches the exact species of microorganism with enhanced phosphate importation encoded by a pit gene, specifically the exact same sequence of PitA gene in SEQ ID NO: 1 of the instant application (Col. 5, lines 16-17, Col. 20, lines 14-19 & 45-61 & SEQ ID NO: 2). Though Hirano does not teach the production of purine nucleotides Lee teaches the production of the purine nucleotides claimed in the instant application by a C. stationis microorganism with its phosphate importation enhanced by the addition of a different foreign phosphate importation system, the pstSCAB operon (Claims section). Lee further teaches the same method of producing the same purine nucleotides (Claims section). This suggests that an artisan of ordinary skill in the art would be able to combine the composition of Hirano with the composition and methods of Lee with the expectation of success. One would have been motivated to combine the production of purine nucleotides by C. stationis with an enhanced importation of phosphate from Lee with the specific C. stationis with the enhancement encoded by the PitA gene from E. coli from Hirano since the addition of a single gene is simpler and has fewer points of failure than the incorporation of an entire operon into a microorganism.
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.
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Claims 1-9 & 12 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1, 4, 10-11 & 13 of U.S. Patent Application No. 17/911,876 in view of Hirano as applied to claims 1-10 &12 above. Although the claims at issue are not identical, they are not patentably distinct from each other because the C. stationis of claims 1-6 & 12 of the instant application are not limited to only having the known modification of its phosphate importer system enhanced by a pit gene (PitA), as taught by Hirano, but could also include other modifications such as the glutamine-hydrolyzing guanosine-5’-monophosphate (GMP) synthase variant of claims 1 and its dependent claims 4 & 13 of ‘876. Claim 10 of ‘876 recites a method for producing a purine nucleotide comprising culturing the microorganism of claim 13. Claim 11 of ‘876, which depends on claim 10, recites recovering the purine nucleotide from a culture medium or the microorganism.
Hirano teaches two strains of the same species of bacteria as recited in the instant application Corynebacterium stationis (Col. 5, lines 16-17), that can be modified to include the PitA gene from E. coli (Col. 20, lines 14-19 & 45-61) with 100% identity in sequence to Seq ID No: 1 of instant application (Hirano SEQ ID NO: 2).
Regarding claims 1-6 & 12: C. stationis with an enhanced phosphate importer activity encoded by a pit gene (PitA, from E. coli, 85% or 99% or higher identity to SEQ ID NO:1), having purine nucleotide production ability consisting of one or more from: 5’-Inosine Monophosphate, 5’-xanthosine monophosphate or 5’-guanosine monophosphate. Claim 13 of ‘876 recites C. stationis comprising the glutamine-hydrolyzing GMP synthase variant. This renders obvious the C. stationis with the ability to produce 5’-guanosine monophosphate that has its phosphate importation system enhanced by the addition of a pit gene (PitA) as recited by claims 1-6 & 12 of the instant application since both the C. stationis of ‘876 and the instant application are not limited only having the modifications recited in the claims and the modification of C. stationis to include the PitA gene from E. coli for the purpose of enhancing phosphate importation is known in the art. Thus, it would have been obvious to one of ordinary skill in the art to combine the known modifications to C. stationis from Hirano with the composition taught by ‘876 with the result of the composition of claims 1-6 & 12 of the instant application. One would have been motivated to do so because Hirano teaches that the inclusion of PitA from E. coli is an exemplary modification for increasing phosphate importation in coryneform bacteria (Col. 20, lines 46-48) and phosphate is explicitly required for purine nucleotide synthesis as claimed in the instant application.
Regarding claim 7-9: A method for producing purine nucleotides, comprising culturing the modified C. stationis in a medium and then recovering those purine nucleotides from the media or from the microorganism wherein, the purine nucleotide is any one or more selected from the group consisting of: 5’-Inosine Monophosphate, 5’-xanthosine monophosphate or 5’-guanosine monophosphate. Claims 10 & 11 of ‘876 recite a method for producing a purine nucleotide comprising culturing C. stationis that has been modified to include a glutamine-hydrolyzing GMP synthase variant and then recovering that purine nucleotide (5’-guanosine monophosphate) from the media or the microorganism. This renders obvious the method of claims 7-9 since both the C. stationis of ‘876 and the instant application are not limited to only having the modifications recited in the claims and the modification of C. stationis to include the PitA gene from E. coli for the purpose of enhancing phosphate importation is known in the art as taught by Hirano.
Thus, it would have been obvious to one of ordinary skill in the art to combine the known modifications to C. stationis from Hirano with the composition taught by ‘876 and further incorporated into the methods of claims 10& 11 of ‘876 with the result of the methods of claims 7-9 of the instant application. One would have been motivated to do so because Hirano teaches that the inclusion of PitA from E. coli is an exemplary modification for increasing phosphate importation in coryneform bacteria (Col. 20, lines 46-48) and phosphate is explicitly required for purine nucleotide synthesis.
Claims 1-5 & 12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claim 15 of U.S. Patent Application No. 19/484,198 in view of Hirano as applied to claims 1-10 &12 above. Although the claims at issue are not identical, they are not patentably distinct from each other because claim 15 of ‘198 recites C. stationis comprising a modified Major Facilitator Superfamily (MFS) transporter variant and in both applications the modifications to C. stationis are not limited to the ones recited in the claims and the modification of C. stationis to include the PitA gene from E. coli for the purpose of enhancing phosphate importation is known in the art.
Hirano teaches two strains of the same species of bacteria as recited in the instant application Corynebacterium stationis (Col. 5, lines 16-17), that can be modified to include the PitA gene from E. coli (Col. 20, lines 14-19 & 45-61) with 100% identity in sequence to Seq ID No: 1 of instant application (Hirano SEQ ID NO: 2).
Regarding claims 1-5 & 12: C. stationis with an enhanced phosphate importer activity encoded by a pit gene (PitA, from E. coli, 85% or 99% or higher identity to SEQ ID NO:1), having purine nucleotide production ability. Claim 15 of ‘198 renders obvious claims 1-5 &12 of the instant application because the purine production ability is a wild type feature of C. stationis and neither the C. stationis of claim 15 of ‘198 nor claims 1-5 & 12 of the instant application are limited to only having the modifications claimed, and could reasonably have both the known modification of PitA as taught by Hirano and an MFS variant. It is also noted that it is clear from the rest of the claims in ‘198 that this is for the purpose of purine nucleotide production, though none of the other claims depend on claim 15.
Thus, it would have been obvious to one of ordinary skill in the art to combine the known modification to C. stationis from Hirano with the C. stationis taught by ‘198 with the result of the composition of claims 1-5 & 12 of the instant application. One would have been motivated to do so because Hirano teaches that the inclusion of PitA from E. coli is an exemplary modification for increasing phosphate importation in coryneform bacteria (Col. 20, lines 46-48) and phosphate is explicitly required for purine nucleotide synthesis.
Claims 1-5 & 12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 & 5-7 of U.S. Patent Application No. 19/135,750 in view of Hirano as applied to claims 1-10 &12 above. Although the claims at issue are not identical, they are not patentably distinct from each other because claims 1-5 & 12 of the instant application are rendered obvious by claim 6 of ‘750 which depends on claims 5 & 1. Claim 6 of ‘750 recites a C. stationis with purine nucleotide producing ability and an enzyme with enhanced glycine degradation activity.
Hirano teaches two strains of the same species of bacteria as recited in the instant application Corynebacterium stationis (Col. 5, lines 16-17), that can be modified to include the PitA gene from E. coli (Col. 20, lines 14-19 & 45-61) with 100% identity in sequence to Seq ID No: 1 of instant application (Hirano SEQ ID NO: 2).
Regarding claims 1-5 & 12: C. stationis with an enhanced phosphate importer activity encoded by a pit gene (PitA, from E. coli, 85% or 99% or higher identity to SEQ ID NO:1), having purine nucleotide production ability. Claim 6 of ‘750 renders obvious claims 1-5 &12 of the instant application because neither the C. stationis of claim 6 of ‘750 or claims 1-5 & 12 of the instant application are not limited to only having the modifications claimed, and could reasonably have both the known modification of PitA as taught by Hirano and an enzyme with enhanced glycine degradation activity. Claim 7 of ‘750 which improperly depends on any one of claims 1 to 6 explicitly recites wherein the microorganism has an increased purine nucleotide producing ability compared to a non-modified microorganism.
Thus, it would have been obvious to one of ordinary skill in the art to combine the known modification to C. stationis from Hirano with the C. stationis taught by ‘750 with the result of the composition of claims 1-5 & 12 of the instant application. One would have been motivated to do so because Hirano teaches that the inclusion of PitA from E. coli is an exemplary modification for increasing phosphate importation in coryneform bacteria (Col. 20, lines 46-48) and phosphate is explicitly required for purine nucleotide synthesis.
Claims 1-5 & 12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 & 4-6 of U.S. Patent Application No. 19/135,746 in view of Hirano as applied to claims 1-10 &12 above. Although the claims at issue are not identical, they are not patentably distinct from each other because claims 1-5 & 12 of the instant application are rendered obvious by claim 5 of ‘746 which depends on claims 4 & 1. Claim 5 of ‘746 recites a C. stationis with purine nucleotide producing ability and an enzyme with enhanced serine hydroxy methyltransferase activity compared to endogenous activity thereof.
Hirano teaches two strains of the same species of bacteria as recited in the instant application Corynebacterium stationis (Col. 5, lines 16-17), that can be modified to include the PitA gene from E. coli (Col. 20, lines 14-19 & 45-61) with 100% identity in sequence to Seq ID No: 1 of instant application (Hirano SEQ ID NO: 2).
Regarding claims 1-5 & 12: C. stationis with an enhanced phosphate importer activity encoded by a pit gene (PitA, from E. coli, 85% or 99% or higher identity to SEQ ID NO:1), having purine nucleotide production ability. Claim 5 of ‘746 renders obvious claims 1-5 &12 of the instant application because neither the C. stationis of claim 5 of ‘746 nor claims 1-5 & 12 of the instant application are limited to only having the modifications claimed, and could reasonably have both the known modification of PitA as taught by Hirano and enhanced serine hydroxy methyltransferase activity. Claim 6 of ‘746 which improperly depends on any one of claims 1 to 5 explicitly recites wherein the microorganism has an increased purine nucleotide producing ability compared to a non-modified microorganism.
Thus, it would have been obvious to one of ordinary skill in the art to combine the known modification to C. stationis from Hirano with the C. stationis taught by ‘746 with the result of the composition of claims 1-5 & 12 of the instant application. One would have been motivated to do so because Hirano teaches that the inclusion of PitA from E. coli is an exemplary modification for increasing phosphate importation in coryneform bacteria (Col. 20, lines 46-48) and phosphate is explicitly required for purine nucleotide synthesis.
Claims 1-5 & 12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 & 4-6 of U.S. Patent Application No. 19/135,744 in view of Hirano as applied to claims 1-10 &12 above. Although the claims at issue are not identical, they are not patentably distinct from each other because claims 1-5 & 12 of the instant application are rendered obvious by claim 5 of ‘744 which depends on claims 4 & 1. Claim 5 of ‘744 recites a C. stationis with purine nucleotide producing ability and an enzyme with weakened serine dehydratase activity compared to endogenous activity thereof.
Hirano teaches two strains of the same species of bacteria as recited in the instant application Corynebacterium stationis (Col. 5, lines 16-17), that can be modified to include the PitA gene from E. coli (Col. 20, lines 14-19 & 45-61) with 100% identity in sequence to Seq ID No: 1 of instant application (Hirano SEQ ID NO: 2).
Regarding claims 1-5 & 12: C. stationis with an enhanced phosphate importer activity encoded by a pit gene (PitA, from E. coli, 85% or 99% or higher identity to SEQ ID NO:1), having purine nucleotide production ability. Claim 5 of ‘744 renders obvious claims 1-5 &12 of the instant application because neither the C. stationis of claim 5 of ‘744 or claims 1-5 & 12 of the instant application are not limited to only having the modifications claimed, and could reasonably have both the known modification of PitA as taught by Hirano and weakened serine dehydratase activity.
Thus, it would have been obvious to one of ordinary skill in the art to combine the known modification to C. stationis from Hirano with the C. stationis taught by ‘744 with the result of the composition of claims 1-5 & 12 of the instant application. One would have been motivated to do so because Hirano teaches that the inclusion of PitA from E. coli is an exemplary modification for increasing phosphate importation in coryneform bacteria (Col. 20, lines 46-48) and phosphate is explicitly required for purine nucleotide synthesis.
Claims 1-5 & 12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 & 4-6 of U.S. Patent Application No. 19/135,742 in view of Hirano as applied to claims 1-10 &12 above. Although the claims at issue are not identical, they are not patentably distinct from each other because claims 1-5 & 12 of the instant application are rendered obvious by claim 5 of ‘742 which depends on claims 4 & 1. Claim 5 of ‘742 recites a C. stationis with purine nucleotide producing ability and an enzyme with weakened formate dehydrogenase activity compared to endogenous activity thereof.
Hirano teaches two strains of the same species of bacteria as recited in the instant application Corynebacterium stationis (Col. 5, lines 16-17), that can be modified to include the PitA gene from E. coli (Col. 20, lines 14-19 & 45-61) with 100% identity in sequence to Seq ID No: 1 of instant application (Hirano SEQ ID NO: 2).
Regarding claims 1-5 & 12: C. stationis with an enhanced phosphate importer activity encoded by a pit gene (PitA, from E. coli, 85% or 99% or higher identity to SEQ ID NO:1), having purine nucleotide production ability. Claim 5 of ‘742 renders obvious claims 1-5 &12 of the instant application because neither the C. stationis of claim 5 of ‘742 or claims 1-5 & 12 of the instant application are not limited to only having the modifications claimed, and could reasonably have both the known modification of PitA as taught by Hirano and weakened formate dehydrogenase activity. Claim 6 of ‘742 which improperly depends on any one of claims 1 to 5 explicitly recites wherein the microorganism has an increased purine nucleotide producing ability compared to a non-modified microorganism.
Thus, it would have been obvious to one of ordinary skill in the art to combine the known modification to C. stationis from Hirano with the C. stationis taught by ‘742 with the result of the composition of claims 1-5 & 12 of the instant application. One would have been motivated to do so because Hirano teaches that the inclusion of PitA from E. coli is an exemplary modification for increasing phosphate importation in coryneform bacteria (Col. 20, lines 46-48) and phosphate is explicitly required for purine nucleotide synthesis.
Claims 1-5 & 12 are rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1 & 4-6 of U.S. Patent Application No. 19/126,551 in view of Hirano as applied to claims 1-10 &12 above. Although the claims at issue are not identical, they are not patentably distinct from each other because claims 1-5 & 12 of the instant application are rendered obvious by claim 5 of ‘551 which depends on claim 1. Claim 5 of ‘551 recites a C. stationis with purine nucleotide producing ability and an enzyme with an enhanced Mn transporter activity.
Hirano teaches two strains of the same species of bacteria as recited in the instant application Corynebacterium stationis (Col. 5, lines 16-17), that can be modified to include the PitA gene from E. coli (Col. 20, lines 14-19 & 45-61) with 100% identity in sequence to Seq ID No: 1 of instant application (Hirano SEQ ID NO: 2).
Regarding claims 1-5 & 12: C. stationis with an enhanced phosphate importer activity encoded by a pit gene (PitA, from E. coli, 85% or 99% or higher identity to SEQ ID NO:1), having purine nucleotide production ability. Claim 5 of ‘551 renders obvious claims 1-5 &12 of the instant application because neither the C. stationis of claim 5 of ‘551 or claims 1-5 & 12 of the instant application are not limited to only having the modifications claimed, and could reasonably have both the known modification of PitA as taught by Hirano and an enhanced Mn transporter activity.
Thus, it would have been obvious to one of ordinary skill in the art to combine the known modification to C. stationis from Hirano with the C. stationis taught by ‘551 with the result of the composition of claims 1-5 & 12 of the instant application. One would have been motivated to do so because Hirano teaches that the inclusion of PitA from E. coli is an exemplary modification for increasing phosphate importation in coryneform bacteria (Col. 20, lines 46-48) and phosphate is explicitly required for purine nucleotide synthesis.
Claims 1-10 & 12 rejected on the ground of nonstatutory double patenting as being unpatentable over claims 8-9, & 11-13 of U.S. Patent Application No. 17/296,375 in view of Hirano as applied to claims 1-10 &12 above. Although the claims at issue are not identical, they are not patentably distinct from each other because the C. stationis of claims 1-10 & 12 of the instant application are not limited to only having the known modification of its phosphate importer system enhanced by a pit gene (PitA) as taught by Hirano, but could also include other modifications such as phosphate importer system enhanced by pstSCAB operon of claim 8 and its dependent claims 9 & 11-13 of ‘375. Claim 8 of ‘375 recites a method for producing a purine nucleotide comprising recovering the purine nucleotide from the culture medium or the microorganism. Claim 9 of ‘375, further limits the purine nucleotide to any one or more selected from the group consisting of 5’-Inosine Monophosphate, 5’-xanthosine monophosphate or 5’-guanosine monophosphate.
Hirano teaches two strains of the same species of bacteria as recited in the instant application Corynebacterium stationis (Col. 5, lines 16-17), that can be modified to include the PitA gene from E. coli (Col. 20, lines 14-19 & 45-61) with 100% identity in sequence to Seq ID No: 1 of instant application (Hirano SEQ ID NO: 2).
Regarding claims 1-6 & 12: C. stationis with an enhanced phosphate importer activity encoded by a pit gene (PitA, from E. coli, 85% or 99% or higher identity to SEQ ID NO:1), having purine nucleotide production ability consisting of one or more from: 5’-Inosine Monophosphate, 5’-xanthosine monophosphate or 5’-guanosine monophosphate. Claim 9 of ‘375 recites a method for producing a purine nucleotide comprising a C. stationis with a phosphate importation system with enhanced activity, encoded by pstSCAB operon, and recovering the purine nucleotide from the culture medium or the microorganism wherein the purine nucleotide is limited to any one or more selected from the group consisting of 5’-Inosine Monophosphate, 5’-xanthosine monophosphate or 5’-guanosine monophosphate. This renders obvious the C. stationis with the ability to produce 5’-Inosine Monophosphate, 5’-xanthosine monophosphate or 5’-guanosine monophosphate that has its phosphate importation system enhanced by the addition of a pit gene (PitA) as recited by claims 1-6 & 12 of the instant application since both the C. stationis of ‘375 and the instant application are not limited only having the modifications recited in the claims and the modification of C. stationis to include the PitA gene from E. coli for the purpose of enhancing phosphate importation is known in the art. Thus, it would have been obvious to one of ordinary skill in the art to combine the known modifications to C. stationis from Hirano with the C. stationis taught by ‘375 with the result of the composition of claims 1-6 & 12 of the instant application. One would have been motivated to do so because Hirano teaches that the inclusion of PitA from E. coli is an exemplary modification for increasing phosphate importation in coryneform bacteria (Col. 20, lines 46-48) and phosphate is explicitly required for purine nucleotide synthesis.
Regarding claim 7-9: A method for producing purine nucleotides, comprising culturing the modified C. stationis in a medium and then recovering those purine nucleotides from the media or from the microorganism wherein the purine nucleotide is limited to consisting of one or more from: 5’-Inosine Monophosphate, 5’-xanthosine monophosphate or 5’-guanosine monophosphate. As specified above claim 9 of ‘375 renders obvious the method of producing purine nucleotides comprising C. stationis with the ability to produce 5’-Inosine Monophosphate, 5’-xanthosine monophosphate or 5’-guanosine monophosphate that has its phosphate importation system enhanced by the addition of a pit gene (PitA) as recited by claims 7-9 of the instant application since both the C. stationis of ‘375 and the instant application are not limited only having the modifications recited in the claims and the modification of C. stationis to include the PitA gene from E. coli for the purpose of enhancing phosphate importation is known in the art as taught by Hirano.
Thus, it would have been obvious to one of ordinary skill in the art to combine the known modifications to C. stationis from Hirano with the C. stationis taught by ‘375 and further incorporated into the methods of claims 9 of ‘375 with the result of the methods of claims 7-9 of the instant application. One would have been motivated to do so because Hirano teaches that the inclusion of PitA from E. coli is an exemplary modification for increasing phosphate importation in coryneform bacteria (Col. 20, lines 46-48) and phosphate is explicitly required for purine nucleotide synthesis.
Conclusion
.
Claims 1-10 & 12 are rejected under 35 U.S.C. 103 as being unpatentable over Hirano further in view of Lee.
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/G.A.W./Examiner, Art Unit 1651
/MELENIE L GORDON/Supervisory Patent Examiner, Art Unit 1651