Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
DETAILED ACTION
Applicant’s response filed on 01/21/2026 is duly acknowledged.
Claims 2, 5, 7, 8, 10, 11, 18-31 and 38 have been canceled by applicants.
Claims 1, 3, 4, 6, 9, 12-17, 32-37, 39 and 40, as amended, are pending in this application.
Election/Restrictions
Applicant’s election without traverse of Group I (Claims 1, 3, 4, 6, 9, 12-17 and 32; directed to “An engineered b-hydroxybutyrate dehydrogenase…”; elected “Species A”) in the reply filed on 01/21/2026 (see REM, p. 7-8) is acknowledged.
It is to be noted that applicants additionally stated that claims 1, 3, 4, 6 and 12-17 read on the elected species A (see REM, p. 8). However, only claims 1, 3, 4 and 6 read on the elected Species A, and therefore, claims 9, 12-17 and 32 have been withdrawn as reading specifically on the non-elected Species B.
Additionally, claims 33-37, 39 and 40 (drawn to non-elected inventions of Groups II-V) have been withdrawn.
Thus, claims 9, 12-17, 32-37, 39 and 40 (non-elected “species B”, and non-elected inventions of Groups II-V) have been withdrawn from further considerations.
Claims 1, 3, 4, and 6 (elected invention of Group I, without traverse; directed to “An engineered b-hydroxybutyrate dehydrogenase…”), as they read on the elected Species A, have been examined on their merits in this action hereinafter.
Priority
This application claims a domestic benefit from US provisional application 63/365,252 filed on 05/24/2022.
Specification
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code (see SPEC, p. 32, [0253]). Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claims 1, 3, 4 and 6 (as currently amended) are rejected 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 applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 1 as currently amended recites the limitation "the wild-type" in line 2. There is insufficient antecedent basis for this limitation in the claim. Appropriate correction is required.
It is to be noted that instant disclosure of record does not specifically define as to what constitutes a “wild-type” b-hydroxybutyrate dehydrogenase (BHBDh) enzyme (see SPEC, p. 2, [009], [065], [073], for instance), which for the purposes of this office action hereinafter, has been interpreted to encompass naturally existing b-hydroxybutyrate dehydrogenase enzyme from which the claimed “engineered b-hydroxybutyrate dehydrogenase” enzyme has been obtained from.
In addition, amended claim 1 recites the limitations “provided at least one of the amino acids at a position in said sequence corresponding to positions 165-188 is different from the amino acid occupying the corresponding position according to SEQ ID NO: 3”, which introduces ambiguity as to the identity of “wild-type” BHBDh enzyme because as per instant claim 6, BHBDh comprising the SEQ ID NO: 3 is also claimed as an “engineered b-hydroxybutyrate dehydrogenase” enzyme (which is a known naturally existing microbial hydroxybutyrate dehydrogenase enzyme from Thermus thermophilus; see 103(a) rejection discussed below). Thus, the metes and bounds of the claimed product does not appear to be properly defined. The dependent claims 3 and 4 do not clarify this point and therefore, they are also deemed indefinite for the same reasons as discussed above. Appropriate correction and/or explanation is required.
NOTICE: 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.
Claim Rejections - 35 USC § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claims 1, 3 and 4 (as currently amended) are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Kratzsch et al (US 10,508,267 B2; USPAT cited in applicant’s IDS dated 09/26/2025).
Claim 1 as currently presented is as follows:
“1. (Currently Amended) An engineered b-hydroxybutyrate dehydrogenase (BHBDh) with increased thermal stability as compared to the wild-type;
wherein the engineered BHBDh comprises a sequence having at least 90% sequence identity to any one of SEQ ID NOs: 1-7 or 12-20, provided at least one of the amino acids at a position in said sequence corresponding to positions 165-188 is different from the amino acid occupying the corresponding position according to SEQ ID NO: 3.”
See also limitations of instant claims 3 and 4, as presented.
It is noted that instant specification (SPEC, p. 21, [0187]) states the following:
PNG
media_image1.png
116
693
media_image1.png
Greyscale
Kratzsch et al (2019), while teaching mutant 3-hydroxybutyrate dehydrogenase from Alcaligenes faecalis (AfBHBDh) including methods and uses thereof (regarding instant claim 1), disclose an engineered beta-hydroxybutyrate dehydrogenase (BHBDh) with increased thermal stability as compared to the wild-type (col 15, ln 20-23 – “That is, a nucleic acid encoding a mutant 3-HBDH of the invention can be introduced into a suitable host cell(s) to produce the respective protein by recombinant means”; col 2, ln 23-34 – “…there are many sites at the wild-type enzyme which allow for mutations, which increase thermal stability and/or affinity for substrate and/or cofactor of the mutant relative to the wild-type enzyme….Particularly, the amino acid may be substituted with Ile (253Ile), Ala (253Ala) or Cys (253Cys) to increase affinity for substrate and/or cofactor (for 3-hydroxybutyrate and/or carba-NAD) and optionally thermal stability"); wherein they disclose the engineered BHBDh comprising a sequence having at least 90% sequence identity to SEQ ID NO: 1 of the instant claim 1 (see col 59, claim 1 – “A mutant 3-hydroxybutyrate dehydrogenase (3-HBDH) from Alcaligenes faecalis with improved performance relative to the wild-type 3-HBDH, wherein the mutant comprises an amino acid sequence that is at least 80% identical to the amino acid sequence of SEQ ID NO: 1”; It is to be noted that amino acids 1-260 of the disclosed SEQ ID NO: 1 exhibits 100% sequence identity to the instantly claimed SEQ ID NO: 1; see amino acid sequence homology shown below), and wherein at least one of the amino acids at a position in said sequence corresponding to positions 165-188 is different from the amino acid occupying the corresponding position according to SEQ ID NO: 3 (it is noted that the amino acids residues 174-197 of the disclosed SEQ ID NO: 1 exhibit 45% identity to amino acid residues 165-188 of the instantly claimed SEQ ID NO: 3; It is also noted that the disclosed SEQ ID NO: 1 and instantly claimed SEQ ID NO: 3 differ at 9 amino acid residues in positions 165-188 of SEQ ID NO: 3; see alignment below).
SEQUENCE ALIGNMENTS
Issued patent database (instant Claim 1; SEQ ID NO: 1)
RESULT 1
US-16-014-355-1
Sequence 1, US/16014355
Patent No. 10508267
GENERAL INFORMATION
APPLICANT: Roche Diagnostics Operations, Inc.
APPLICANT: Roche Diabetes Care, Inc.
TITLE OF INVENTION: Mutant 3 Hydroxybutyrate Dehygrogenase from Alcaligenes faecalis
TITLE OF INVENTION: as well as methods and uses involving the same
FILE REFERENCE: R69992PC
CURRENT APPLICATION NUMBER: US/16/014,355
CURRENT FILING DATE: 2018-06-21
NUMBER OF SEQ ID NOS: 16
SEQ ID NO 1
LENGTH: 260
TYPE: PRT
ORGANISM: Alcaligenes faecalis
Query Match 100.0%; Score 1303; Length 260;
Best Local Similarity 100.0%;
Matches 260; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MLKGKKAVVTGSTSGIGLAMATELAKAGADVVINGFGQPEDIERERSTLESKFGVKAYYL 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MLKGKKAVVTGSTSGIGLAMATELAKAGADVVINGFGQPEDIERERSTLESKFGVKAYYL 60
Qy 61 NADLSDAQATRDFIAKAAEALGGLDILVNNAGIQHTAPIEEFPVDKWNAIIALNLSAVFH 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 NADLSDAQATRDFIAKAAEALGGLDILVNNAGIQHTAPIEEFPVDKWNAIIALNLSAVFH 120
Qy 121 GTAAALPIMQKQGWGRIINIASAHGLVASVNKSAYVAAKHGVVGLTKVTALENAGKGITC 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 GTAAALPIMQKQGWGRIINIASAHGLVASVNKSAYVAAKHGVVGLTKVTALENAGKGITC 180
Qy 181 NAICPGWVRTPLVEKQIEAISQQKGIDIEAAARELLAEKQPSLQFVTPEQLGGAAVFLSS 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 NAICPGWVRTPLVEKQIEAISQQKGIDIEAAARELLAEKQPSLQFVTPEQLGGAAVFLSS 240
Qy 241 AAADQMTGTTLSLDGGWTAR 260
||||||||||||||||||||
Db 241 AAADQMTGTTLSLDGGWTAR 260
AA sequence alignment of disclosed SEQ ID NO: 1 (AfBHBDh) and claimed SEQ ID NO: 3 (TtBHBDh; instant claim 1)
Title: AASEQ1_04302026_125834
Perfect score: 1303
Sequence: 1 MLKGKKAVVTGSTSGIGLAM..........AAADQMTGTTLSLDGGWTAR 260
Scoring table: BLOSUM62
Gapop 10.0 , Gapext 0.5
Searched: 1 seqs, 251 residues
Total number of hits satisfying chosen parameters: 1
Minimum DB seq length: 0
Maximum DB seq length: inf
Post-processing: Minimum Match 0%
Maximum Match 100%
Listing first 50 summaries
Database : AASEQ2_04302026_125905.fasta:*
SUMMARIES
%
Result Query
No. Score Match Length DB ID Description
----------------------------------------------------------------------------
1 552.5 42.4 251 1 AASEQ2_04302026_125905
RESULT 1
AASEQ2_04302026_125905
Query Match 42.4%; Score 552.5; DB 1; Length 251;
Best Local Similarity 45.6%;
Matches 120; Conservative 45; Mismatches 75; Indels 23; Gaps 5;
Qy 4 GKKAVVTGSTSGIGLAMATELAKAGADVVINGFGQPEDIERERSTLESKFGVKAYYLNAD 63
|: :|||: ||||||:| |: || |::: |: |: | | : | || ||
Db 6 GRTVLVTGAGSGIGLAIA RAFAREGARVLVH------DV-RDASRLAEELG--GVYLQAD 56
Qy 64 LSDAQATRDFIAKAAEALG------GLDILVNNAGIQHTAPIEEFPVDKWNAIIALNLSA 117
|:| | |||| |:|:|||||| || ||:||||:: | :: : |:|
Db 57 LAD--------PKEVEALGKEAAAMGVDVLVNNAGFQHIAPVEEFPLEVWQRMLQVMLTA 108
Qy 118 VFHGTAAALPIMQKQGWGRIINIASAHGLVASVNKSAYVAAKHGVVGLTKVTALENAGKG 177
| | | || |:::|||||:|||| |||||| ||||::||||::|||| ||| |
Db 109 PFQLTQALLPGMKRRGWGRILNIASIHGLVASPYKSAYISAKHGLLGLTKTVALEAGPHG 168
Qy 178 ITCNAICPGWVRTPLVEKQIEAISQQKGIDIEAAARELLAEKQPSLQFVTPEQLGGAAVF 237
:| ||| | :||||||| ||: :: || | | :: : : : ||:: |:|
Db 169 VTVNAIA PAYVRTPLVEGQIQDQAKTLGIPPEEVAEKVFLAQAAIKRLIAPEEVAELALF 228
Qy 238 LSSAAADQMTGTTLSLDGGWTAR 260
|:| | :|| :| |||||
Db 229 LASEKASAITGAVFPIDLGWTAR 251
Regarding instant claims 3 and 4, Kratzsch et al disclose the engineered BHBDh comprising a modification at one or more amino acid positions selected from: (a) a position corresponding to position 175 of the amino acid sequence set forth in SEQ ID NO: 3 (it is noted that the disclosed SEQ ID NO: 1 amino acid residue 184 exhibits a Cys, in place of wild-type Ala residue, at the corresponding position 175 of claimed SEQ ID NO: 3). In addition, Kratzsch et al also disclose the engineered BHBDh comprising a modification at: (b) a position corresponding to position 177 of the amino acid sequence set forth in SEQ ID NO: 3, wherein the modification includes a substitution of the amino acid residue Ala with an amino acid residue Gly (see disclosed SEQ ID NO: 1 amino ·acids residues 186 exhibits a Gly at the corresponding position of SEQ ID NO: 3 position 177 Ala); and (c) a position corresponding to position 178 of the amino acid sequence set forth in SEQ ID NO: 3, wherein the modification includes a substitution of the amino acid residue Tyr with an amino acid residue Trp (see disclosed SEQ ID NO: 1 amino acids residues 187 exhibits a Trp at the corresponding position of SEQ ID NO: 3 position 178 Tyr). Thus, the disclosure of Kratzsch et al meets all the limitations of instant claims 1, 3 and 4 as currently presented.
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.
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 6 (as currently presented) is rejected under 35 U.S.C. 103 as being unpatentable over Kratzsch et al (US 10,508,267 B2; USPAT cited in applicant’s IDS dated 09/26/2025) in view of F6DFM9_THEG (2011; NPL cited in IDS dated 09/26/2025, citation no. 029).
Claim 6 recited the following:
“6. (Currently Amended) The engineered BHBDh of claim 1, comprising a sequence having at least 90% sequence identity to any one of SEQ ID NOs: 3-5.”
The detailed teachings and/or suggestions from the cited prior art reference of Kratzsch et al as they pertain to claims 1, 3 and 4 have been discussed above, and are further relied upon hereinafter in the same manner.
However, Kratzsch et al do not disclose the engineered BHBDh comprising “a sequence having at least 90% sequence identity to any one of SEQ ID NOs: 3-5” (it is noted that SEQ ID NO: 3 corresponds to TtBHBDh, the enzyme derived from Thermus thermophilus bacteria; see instant SPEC, [0158]-[0159], [0187]).
F6DFM9_THETG (2011; UniProt accession number; see sequence homology details below) discloses 3-hydroxybutyrate dehydrogenase from Thermus thermophilus (see p. 1), comprising a sequence having at least 90% sequence identity to SEQ ID NO: 3 (F6DFM9_ THETG amino acids 1 -251 exhibits 100% amino acid sequence identity to instantly claimed SEQ ID NO: 3).
SEQUENCE ALIGNMENTS
UNIPROT DATABASE (instant SEQ ID NO: 3)
RESULT 1
F6DFM9_THETG
ID F6DFM9_THETG Unreviewed; 251 AA.
AC F6DFM9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 18-JUN-2025, entry version 62.
DE SubName: Full=3-hydroxybutyrate dehydrogenase {ECO:0000313|EMBL:AEG33115.1};
GN OrderedLocusNames=Ththe16_0694 {ECO:0000313|EMBL:AEG33115.1};
OS Thermus thermophilus (strain SG0.5JP17-16).
OC Bacteria; Thermotogati; Deinococcota; Deinococci; Thermales; Thermaceae;
OC Thermus.
OX NCBI_TaxID=762633 {ECO:0000313|EMBL:AEG33115.1, ECO:0000313|Proteomes:UP000009233};
RN [1] {ECO:0000313|EMBL:AEG33115.1, ECO:0000313|Proteomes:UP000009233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG0.5JP17-16 {ECO:0000313|EMBL:AEG33115.1,
RC ECO:0000313|Proteomes:UP000009233};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Allgaier M., Hugenholtz P., Singer S.,
RA Gladden J., Woyke T.;
RT "Complete sequence of chromosome of Thermus thermophilus SG0.5JP17-16.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000009233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG0.5JP17-16 {ECO:0000313|Proteomes:UP000009233};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Allgaier M., Hugenholtz P., Singer S.,
RA Gladden J., Woyke T.;
RT "Complete sequence of chromosome of Thermus thermophilus SG0.5JP17-16.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002777; AEG33115.1; -; Genomic_DNA.
DR RefSeq; WP_014510095.1; NC_017272.1.
DR AlphaFoldDB; F6DFM9; -.
DR KEGG; tts:Ththe16_0694; -.
DR PATRIC; fig|762633.3.peg.695; -.
DR HOGENOM; CLU_010194_1_0_0; -.
DR Proteomes; UP000009233; Chromosome.
DR GO; GO:0003858; F:3-hydroxybutyrate dehydrogenase activity; IEA:InterPro.
DR FunFam; 3.40.50.720:FF:000084; Short-chain dehydrogenase reductase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR011294; 3-OHbutyrate_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR050259; SDR.
DR InterPro; IPR002347; SDR_fam.
DR NCBIfam; TIGR01963; PHB_DH; 1.
DR NCBIfam; NF009093; PRK12429.1; 1.
DR PANTHER; PTHR42879; 3-OXOACYL-(ACYL-CARRIER-PROTEIN) REDUCTASE; 1.
DR PANTHER; PTHR42879:SF2; 3-OXOACYL-[ACYL-CARRIER-PROTEIN] REDUCTASE FABG; 1.
DR Pfam; PF13561; adh_short_C2; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
SQ SEQUENCE 251 AA; 26516 MW; 6B9F705E1128C129 CRC64;
Query Match 100.0%; Score 1249; Length 251;
Best Local Similarity 100.0%;
Matches 251; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MGAFSGRTVLVTGAGSGIGLAIA RAFAREGARVLVHDVRDASRLAEELGGVYLQADLADP 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MGAFSGRTVLVTGAGSGIGLAIA RAFAREGARVLVHDVRDASRLAEELGGVYLQADLADP 60
Qy 61 KEVEALGKEAAAMGVDVLVNNAGFQHIAPVEEFPLEVWQRMLQVMLTAPFQLTQALLPGM 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 KEVEALGKEAAAMGVDVLVNNAGFQHIAPVEEFPLEVWQRMLQVMLTAPFQLTQALLPGM 120
Qy 121 KRRGWGRILNIASIHGLVASPYKSAYISAKHGLLGLTKTVALEAGPHGVTVNAIA PAYVR 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 KRRGWGRILNIASIHGLVASPYKSAYISAKHGLLGLTKTVALEAGPHGVTVNAIA PAYVR 180
Qy 181 TPLVEGQIQDQAKTLGIPPEEVAEKVFLAQAAIKRLIAPEEVAELALFLASEKASAITGA 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 TPLVEGQIQDQAKTLGIPPEEVAEKVFLAQAAIKRLIAPEEVAELALFLASEKASAITGA 240
Qy 241 VFPIDLGWTAR 251
|||||||||||
Db 241 VFPIDLGWTAR 251
Since Kratzsch et al already disclose preparation of mutant 3-HBDH enzymes with increased thermal stability (see detailed teachings above; col 2, ln 23-34; col 15, ln 20-23), and the fact that F6DFM9_ THETG discloses 3-hydroxybutyrate dehydrogenase derived from Thermus thermophilus (p. 1 ) having the same amino acid sequence, to an artisan of ordinary skill in the art, it would have been obvious that the 3-hydroxybutyrate dehydrogenase of F6DFM9_ THETG could have been combined with the method of Kratzsch et al to provide a thermotolerant engineered 3-hydroxybutyrate dehydrogenase derived from Thermus thermophilus which is already adapted to grow and function at higher temperatures. Since, the methods for making such engineered mutants or amino acid substitution variants of such BHBDh enzymes have already been disclosed by Kratzsch et al, such substitution(s) and/or modification(s) would have been deemed obvious and/or fully contemplated by an artisan of ordinary skill, at least for the advantage of preparing engineered mutant BHBDh enzymes that can efficiently function at higher temperatures compared to enzymes from other microbial sources, unless evidence/data provided on record to the contrary commensurate with the scope of the invention as currently being claimed (which is currently lacking on record; see instant disclosure SPEC, Example 1, for instance).
Thus the claim as a whole would have been prima facie obvious to a person of ordinary skill in the art before the effective filing date of the invention as generically claimed.
As per MPEP 2111.01, during examination, the claims must be interpreted as broadly as their terms reasonably allow. In re American Academy of Science Tech Center, F.3d, 2004 WL 1067528 (Fed. Cir. May 13, 2004)(The USPTO uses a different standard for construing claims than that used by district courts; during examination the USPTO must give claims their broadest reasonable interpretation.). This means that the words of the claim must be given their plain meaning unless applicant has provided a clear definition in the specification. In re Zletz, 893 F.2d 319, 321, 13 USPQ2d 1320, 1322 (Fed. Cir. 1989).
Conclusion
Pertinent prior art:
1. Beck et al (US 10,704,029; USPAT cited as ref. [A] on PTO 892 form)- “Mutant 3-hydroxybutyrate dehydrogenase from Rhodobacter sphaeroides as well as methods and uses involving the same” (disclose mutant 3-hydroxybutyrate dehydrogenase (3-HBDH) enzymes with improved performance relative to the wild-type 3-HBDH enzyme, including thermal stability and affinity for substrates and/or co-factor NAD; see Abstract, col 1, ln 60-67, Tables 1-2, and claim 1, for instance).
Any inquiry concerning this communication or earlier communications from the examiner should be directed to SATYENDRA K. SINGH whose telephone number is (571)272-8790. The examiner can normally be reached M-F 8:00- 5:00.
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.
SATYENDRA K. SINGH
Primary Examiner
Art Unit 1657
/SATYENDRA K SINGH/Primary Examiner, Art Unit 1657
Prosecution Insights