Prosecution Insights
Last updated: October 02, 2026
Application No. 18/837,131

NOVEL LIPID PEROXIDATION SYSTEM AND METHOD FOR PREPARING BIOFUEL AND BIOPOLYMER USING SAME

Non-Final OA §103§112
Filed
Aug 08, 2024
Priority
Feb 11, 2022 — RE 10-2022-0018142 +1 more
Examiner
PAK, YONG D
Art Unit
Tech Center
Assignee
Korea Advanced Institute of Science and Technology
OA Round
1 (Non-Final)
75%
Grant Probability
Favorable
1-2
OA Rounds
8m
Est. Remaining
89%
With Interview

Examiner Intelligence

Grants 75% — above average
75%
Career Allowance Rate
711 granted / 953 resolved
+14.6% vs TC avg
Moderate +14% lift
Without
With
+14.3%
Interview Lift
resolved cases with interview
Typical timeline
2y 10m
Avg Prosecution
62 currently pending
Career history
1006
Total Applications
across all art units

Statute-Specific Performance

§101
6.8%
-33.2% vs TC avg
§103
23.1%
-16.9% vs TC avg
§102
18.9%
-21.1% vs TC avg
§112
32.5%
-7.5% vs TC avg
Black line = Tech Center average estimate • Based on career data from 953 resolved cases

Office Action

§103 §112
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 This application is a 371 of PCT/KR2023/001999. The response filed on July 17, 2026 has been entered. Election/Restrictions Applicant’s election without traverse of Group I with a species election of (1) The strain of the bacterium: Rhodococcus opacus (2) Peroxidase: lignin peroxidase gene from Phanerochaete carnosa (3) Other genes/enzymes introduced into the bacterium: laccase-like multicopper oxidase (LMCO)-encoding gene from Aspergillus flavus (4) Gene(s) that are deleted: i) a 4-dichlorophenol 6-monooxygenase-encoding gene; or ii) a 2-dehydropantoate 2-reductase-encoding gene (5) other modification: a promoter of a monoacylglycerol (MAG) lipase-encoding gene is replaced with an inducible promoter in the reply filed on July 17, 2026 is acknowledged. Claims 5, 10-12, and 14-21withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a nonelected species (claims 5 and 10-12) and invention (claims 14-21), there being no allowable generic or linking claim. Election was made without traverse in the reply filed on July 17, 2026. Status of Claims Claims 1-21 and 44-45 are pending. Claims 5, 10-12 and 14-21 are withdrawn. Claims 1-4, 6-9, 13, and 44-45 are pending. Information Disclosure Statement The information disclosure statement (IDS) submitted on August 8, 2024 and December 13, 2024 are in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner. Priority Acknowledgment is made of applicant’s claim for foreign priority under 35 U.S.C. 119 (a)-(d). Receipt is acknowledged of certified copies of papers required by 37 CFR 1.55. Specification The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code, page 3, for example. Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code. See MPEP § 608.01. Applicant’s cooperation is requested in reviewing the specification for additional embedded hyperlink and/or other form of browser-executable code that may be present in the specification and making the appropriate correction(s). 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. Claim 6 is 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 6 recites the phrase “a promoter of a monoglycerol (MAG) lipase-encoding gene is replaced with an inducible promoter”. The metes and bounds of the phrase in the context of the claim are not clear. It is unclear if the promoter of an endogenous MAG lipase encoding gene is replaced with an inducible promoter or the promoter of the peroxidase-encoding gene is replaced with an inducible promoter. Appropriate correction is requested. 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 1-4, 6-9, and 13 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention. MPEP 2111.01 states that ''[d]uring examination, the claims must be interpreted as broadly as their terms reasonably allow.'' In the instant case, the claims have been broadly interpreted to encompass (A) any recombinant bacterium, any recombinant gram-positive bacterium, or any recombinant Rhodococcus comprising (B) a heterologous gene encoding any peroxidase and any peroxidase belonging to EC 1.11.1.14, (C) promoter of a MAG lipase replaced with an inducible promoter, (D) deletion of a gene encoding 4-dichlorophenol-6-monooxygnease or a gene encoding 2-dehydropantoate 2-reducase, and (E) a gene encoding any laccase-like multicopper oxidase (LMCO), wherein (F) said bacterium of (A) has induced cell membrane lipid peroxidation ability and has a reduced cell membrane thickness compared to a parent strain. Therefore, the claims are drawn to a genus of bacterium having unknown structure but having the function of induced cell membrane lipid peroxidation ability and has a reduced cell membrane thickness compared to a parent strain. MPEP 2163 I. states that to “satisfy the written description requirement, a patent specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. MPEP 2163. II.A.3.(a) sates that “Possession may be shown in many ways. For example, possession may be shown by describing an actual reduction to practice of the claimed invention. Possession may also be shown by a clear depiction of the invention in detailed drawings or in structural chemical formulas which permit a person skilled in the art to clearly recognize that inventor had possession of the claimed invention. An adequate written description of the invention may be shown by any description of sufficient, relevant, identifying characteristics so long as a person skilled in the art would recognize that the inventor had possession of the claimed invention. According to MPEP 2163.II.A.3.(a).ii), “Satisfactory disclosure of a ‘representative number’ depends on whether one of skill in the art would recognize that the applicant was in possession of the necessary common attributes or features possessed by the members of the genus in view of the species disclosed. For inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus…Instead, the disclosure must adequately reflect the structural diversity of the claimed genus, either through the disclosure of sufficient species that are ‘representative of the full variety or scope of the genus,’ or by the establishment of ‘a reasonable structure-function correlation.’" The recitations of “peroxidase”, “laccase-like multicopper oxidase (LMCO)”, “promoter of a nonglycerol (MAG) lipase-encoding gene is replaced with an inducible promoter”, “induced cell membrane lipid peroxidation ability”, and “reduced cell membrane thickness compared to a parent strain” fail to provide a sufficient description of the genus as it merely describes the functional features of the genus without providing any definition of the structural features of the species within the genus. The specification does not specifically define any of the species that fall within the genus. The specification does not define any structural features commonly possessed by members of the genus that distinguish them from others. One skilled in the art therefore cannot, as one can do with a fully described genus, visualize or recognize the identity of the members of the genus. Peroxidases, lignin peroxidases (EC 1.11.1.14), and LMCO were known in art. However, peroxidase and LMCO having the function of imparting induced cell membrane lipid peroxidation ability and has a reduced cell membrane thickness to any recombinant bacterium, any recombinant gram-positive bacterium, or any recombinant Rhodococcus opacus was not known in the art. Further, genes encoding 4-dichlorophenol-6-monooxygnease, and genes encoding 2-dehydropantoate 2-reducase must be known in order to delete said genes in any bacterium, any recombinant gram-positive bacterium, or any recombinant Rhodococcus. The specification is limited to one example, a recombinant Rhodococcus opacus comprising a heterologous gene encoding the Phanerochaete carnosa lignin peroxidase having the amino acid sequence of SEQ ID NO:1, deletions of its endogenous genes encoding 4-dichlorophenol-6-monooxygenase and 2-dehydropantoate 2-reducase, replacing the promoter of its endogenous gene encoding MAG lipase with an inducible promoter, and an Aspergillus flavus gene encoding LMCO, wherein said Rhodococcus opacus has induced cell membrane lipid peroxidation ability and has a reduced cell membrane thickness. While MPEP 2163 acknowledges that in certain situations “one species adequately supports a genus,” it also acknowledges that “[f]or inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus.” In view of the widely variant species encompassed by the genus, the one example described above is not enough and does not constitute a representative number of species to describe the whole genus. Therefore, the specification fails to describe a representative species of the claimed genus. Further, the specification does not provide an actual reduction to practice of the genus because the specification fails to disclose the structure of the genes encoding 4-dichlorophenol-6-monooxygnease, and 2-dehydropantoate 2-reducase from non- Rhodococcus opacus which must be known in order to inactivate said genes in any bacterium, any recombinant gram-positive bacterium, or any recombinant Rhodococcus. The specification does not disclose the isolation or cloning of any non- Rhodococcus opacus genes encoding 4-dichlorophenol-6-monooxygnease and 2-dehydropantoate 2-reducase. Because Rhodococcus opacus comprising a deletion of its endogenous genes encoding 4-dichlorophenol-6-monooxygnease and 2-dehydropantoate 2-reducase is not representative of the entire genus of any bacterium, any recombinant gram-positive bacterium, or any recombinant Rhodococcus compsiing deletions of said gene and the specification does not disclose structural features shared by members of the genus, the description of the above modified Rhodococcus opacus would not have put the application in possession of the common structural attributes or features shared by members of the genus that structurally distinguish the members of the genus from other materials at the time of filing. Given this lack of description of the representative species encompassed by the genus of the claims, the specification fails to sufficiently describe the claimed invention in such full, clear, concise, and exact terms that a skilled artisan would recognize that applicants were in possession of the inventions of claims 1-4, 6-9, and 13. 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. 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. Claims 1-4, 13, and 44-45 is/are rejected under 35 U.S.C. 103 as being unpatentable over Yuan (WO 2016/154631– form PTO-1449) and K5UNT2_PHACS (UniProtKB/TrEMBL Database. December 11, 2019 – form PTO-892). Regarding claims 1 and 3-4, Yuan discloses a recombinant Rhodococcus opacus, a gram-positive bacterium, comprising a heterologous gene encoding a peroxidase or lignin peroxidase (lines 4-24 on page 2, lines 25-27 on page 19, Example 29, and claims 20 and 28-29). Yuan discloses secretion of proteins to the plasma membrane (lines 13-24 on page 18). Regarding claim 2, lignin peroxidase has an EC number of EC 1.11.1.14 (see Example 1 of the instant specification. Yuan does not disclose a gene encoding a Phanerochaete carnosa peroxidase having the amino acid sequence of SEQ ID NO:1 or the property of induced membrane lipid peroxidation ability and reduced cell membrane thickness compared to the parent strain. Regarding claim 1 and 44-45, K5UNT2 disclose a Phanerochaete carnosa peroxidase having 100% sequence identity to the peroxidase of the amino acid sequence of SEQ ID NO:1 and DNA encoding said peroxidase EMBL JH930477 (pages 1-2 and see the sequence alignment). Regarding claims 1 and 13, the property of induced membrane lipid peroxidation ability and property of reduced cell membrane thickness compared to the parent strain are an inherent property of a recombinant Rhodococcus opacus comprising a gene encoding the Phanerochaete carnosa peroxidase of K5UNT2 because said recombinant Rhodococcus opacus has identical chemical structure as the recombinant Rhodococcus opacus comprising a gene encoding the Phanerochaete carnosa peroxidase of SEQ ID NO:1 as described in the specification of the instant application (Examples 5 and 8-9). The recombinant Rhodococcus opacus comprising a gene encoding the Phanerochaete carnosa peroxidase of SEQ ID NO:1 described in Examples 5 and 8-9 has induced membrane lipid peroxidation ability and property of reduced cell membrane thickness compared to the parent strain. MPEP 2112.01 states that “Products of identical chemical composition can not have mutually exclusive properties.” In re Spada, 911 F.2d 705, 709, 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). A chemical composition and its properties are inseparable.” Since the recombinant Rhodococcus opacus comprising a gene encoding the Phanerochaete carnosa peroxidase of K5UNT2 has identical structure as the recombinant Rhodococcus opacus comprising a gene encoding the Phanerochaete carnosa peroxidase of SEQ ID NO:1 of the instant application, the recited property “induced membrane lipid peroxidation ability” and property of “reduced cell membrane thickness compared to the parent strain” are necessarily present and would flow naturally from following the suggestion of the prior art. MPEP 2112 II states that “[t]here is no requirement that a person of ordinary skill in the art would have recognized the inherent disclosure at the relevant time, but only that the subject matter is in fact inherent in the prior art reference.” Therefore, in combining the above references, it would have been obvious to one having ordinary skill in the art before the time the claimed invention was effectively filed to modify the Rhodococcus opacus of Yuan by substitute the gene encoding the peroxidase with another, such as the gene encoding the Phanerochaete carnosa peroxidase of K5UNT2, because one of ordinary skill in the art would have been able to carry out such a substitution, and the results were reasonably predictable. The rationale to support a conclusion that the claims would have been obvious is that the substitution of one known element (peroxidase) for another yields predictable results to one of ordinary skill in the art. One of ordinary skill in the art would have had a reasonable expectation of success since Yuan teaches a recombinant Rhodococcus opacus comprising a gene encoding a peroxidase and K5UNT2 teaches a gene encoding a Phanerochaete carnosa peroxidase having 100% sequence identity to sEQ ID NO:1 of the instant application. Therefore, the above references render claims 1-4, 13, and 44-45 prima facie obvious. Claim(s) 9 is/are rejected under 35 U.S.C. 103 as being unpatentable over Yuan (WO 2016/154631– form PTO-1449) and K5UNT2_PHACS (UniProtKB/TrEMBL Database – form PTO-892).as applied to claim1-4, 13, and 44-45 above, and further in view of Jiang (Adaptive evolution for fast growth on glucose and the effects on the regulation of glucose transport system in Clostridium tyrobutyricum. Biotechnol Bioeng. 2012 Mar;109(3):708-18. – form PTO-892). Yuan and K5UNT2_PHACS do not disclose glucose adaptive evolution of the recombinant Rhodococcus opacus. Regarding claim 9, Jiang discloses performing glucose adaptive evolution of a bacterium for fast growth on glucose (abstract). Therefore, in combining the above references, it would have been obvious to one having ordinary skill in the art before the time the claimed invention was effectively filed to modify the bacterium by performing glucose adaptive evolution. One having ordinary skill in the art would have been motivated to do so in order to provide the bacterium having faster growth. One of ordinary skill in the art would have had a reasonable expectation of success since Yuan teaches a recombinant Rhodococcus opacus comprising a gene encoding a peroxidase, K5UNT2 teaches a gene encoding a Phanerochaete carnosa peroxidase having 100% sequence identity to sEQ ID NO:1 of the instant application, and Jiang teaches how to perform glucose adaptive evolution. Therefore, the above references render claims 1-4, 9, 13, and 44-45 prima facie obvious. Conclusion Claims 1-21 and 44-45 are pending. Claims 5, 10-12 and 14-21 are withdrawn. Claims 1-4, 6-9, 13, and 44-45 are rejected. Any inquiry concerning this communication or earlier communications from the examiner should be directed to YONG D PAK whose telephone number is (571)272-0935. The examiner can normally be reached M-Th: 5:30 am - 3:30 pm. 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, Robert Mondesi can be reached on 408-918-7584. 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. /YONG D PAK/Primary Examiner, Art Unit 1652 Sequence alignment of the peroxidase of SEQ ID NO:2 of the instant application (“Qy”) and peroxidase of K5UNT2 (“Db”) K5UNT2_PHACS ID K5UNT2_PHACS Unreviewed; 372 AA. AC K5UNT2; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 02-APR-2025, entry version 45. DE RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051}; DE EC=1.11.1.- {ECO:0000256|RuleBase:RU363051}; GN ORFNames=PHACADRAFT_263501 {ECO:0000313|EMBL:EKM51406.1}; OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora OS carnosa). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC Polyporales; Phanerochaetaceae; Phanerochaete. OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM51406.1, ECO:0000313|Proteomes:UP000008370}; RN [1] {ECO:0000313|EMBL:EKM51406.1, ECO:0000313|Proteomes:UP000008370} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM51406.1, RC ECO:0000313|Proteomes:UP000008370}; RX PubMed=22937793; DOI=10.1186/1471-2164-13-444; RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A., RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E., RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M., RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S., RA Grigoriev I.V., Master E.R.; RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P. RT chrysosporium, to elucidate the genetic basis of the distinct wood types RT they colonize."; RL BMC Genomics 13:444-444(2012). CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|PIRSR:PIRSR601621-2, CC ECO:0000256|RuleBase:RU363051}; CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR601621- CC 2, ECO:0000256|RuleBase:RU363051}; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Evidence={ECO:0000256|PIRSR:PIRSR601621-2}; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. CC {ECO:0000256|PIRSR:PIRSR601621-2}; CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily. CC {ECO:0000256|ARBA:ARBA00006089, ECO:0000256|RuleBase:RU363051}. 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; JH930477; EKM51406.1; -; Genomic_DNA. DR RefSeq; XP_007400547.1; XM_007400485.1. DR AlphaFoldDB; K5UNT2; -. DR SMR; K5UNT2; -. DR STRING; 650164.K5UNT2; -. DR GeneID; 18918570; -. DR KEGG; pco:PHACADRAFT_263501; -. DR HOGENOM; CLU_041038_0_1_1; -. DR InParanoid; K5UNT2; -. DR OrthoDB; 2113341at2759; -. DR Proteomes; UP000008370; Unassembled WGS sequence. DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW. DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:TreeGrafter. DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW. DR GO; GO:0000302; P:response to reactive oxygen species; IEA:TreeGrafter. DR CDD; cd00692; ligninase; 1. DR Gene3D; 1.10.520.10; -; 1. DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1. DR InterPro; IPR044831; Ccp1-like. DR InterPro; IPR002016; Haem_peroxidase. DR InterPro; IPR010255; Haem_peroxidase_sf. DR InterPro; IPR001621; Ligninase. DR InterPro; IPR024589; Ligninase_C. DR InterPro; IPR019794; Peroxidases_AS. DR InterPro; IPR019793; Peroxidases_heam-ligand_BS. DR PANTHER; PTHR31356:SF66; CATALASE-PEROXIDASE; 1. DR PANTHER; PTHR31356; THYLAKOID LUMENAL 29 KDA PROTEIN, CHLOROPLASTIC-RELATED; 1. DR Pfam; PF00141; peroxidase; 1. DR Pfam; PF11895; Peroxidase_ext; 1. DR PRINTS; PR00462; LIGNINASE. DR PRINTS; PR00458; PEROXIDASE. DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1. DR PROSITE; PS00435; PEROXIDASE_1; 1. DR PROSITE; PS00436; PEROXIDASE_2; 1. DR PROSITE; PS50873; PEROXIDASE_4; 1. PE 3: Inferred from homology; KW Calcium {ECO:0000256|PIRSR:PIRSR601621-2, ECO:0000256|RuleBase:RU363051}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR601621-4}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR601621-2}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR601621-2}; KW Lignin degradation {ECO:0000256|ARBA:ARBA00023185}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR601621-2}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU363051}; KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU363051}; KW Reference proteome {ECO:0000313|Proteomes:UP000008370}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU363051}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|RuleBase:RU363051" FT CHAIN 22..372 FT /note="Peroxidase" FT /evidence="ECO:0000256|RuleBase:RU363051" FT /id="PRO_5006992909" FT DOMAIN 131..317 FT /note="Plant heme peroxidase family profile" FT /evidence="ECO:0000259|PROSITE:PS50873" FT REGION 349..372 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 349..362 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 75 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR601621-1" FT BINDING 76 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2" FT BINDING 94 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2" FT BINDING 96 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2" FT BINDING 98 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2" FT BINDING 204 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2" FT BINDING 205 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2" FT BINDING 222 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2" FT BINDING 224 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2" FT BINDING 229 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR601621-2" FT SITE 71 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR601621-3" FT DISULFID 31..43 FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4" FT DISULFID 42..313 FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4" FT DISULFID 62..148 FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4" FT DISULFID 277..345 FT /evidence="ECO:0000256|PIRSR:PIRSR601621-4" SQ SEQUENCE 372 AA; 39216 MW; 867F7268C88FC737 CRC64; Query Match 100.0%; Score 1945; Length 372; Best Local Similarity 100.0%; Matches 372; Conservative 0; Mismatches 0; Indels 0; Gaps 0; Qy 1 MAFKQLIVAISIALSLQVTQAVVLKDKRATCSNGASVGDESCCAWFDVLDDIQQNLFNGG 60 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 1 MAFKQLIVAISIALSLQVTQAVVLKDKRATCSNGASVGDESCCAWFDVLDDIQQNLFNGG 60 Qy 61 QCGAEAHESIRLVFHDSIAISPAMEAQGKFGGGGADGSIILFDEIETAFHPNIGLDEVVN 120 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 61 QCGAEAHESIRLVFHDSIAISPAMEAQGKFGGGGADGSIILFDEIETAFHPNIGLDEVVN 120 Qy 121 LQKPFIAKHGVTPGDFIAFAGAVAMSNCPGAPQMNFFTGRAPATQAAPDGLVPEPFHTVD 180 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 121 LQKPFIAKHGVTPGDFIAFAGAVAMSNCPGAPQMNFFTGRAPATQAAPDGLVPEPFHTVD 180 Qy 181 QIIDRVNDAGQFDELELVWMLSAHSVAASNDVDPTVQGLPFDSTPGVFDSQFFVETQLRG 240 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 181 QIIDRVNDAGQFDELELVWMLSAHSVAASNDVDPTVQGLPFDSTPGVFDSQFFVETQLRG 240 Qy 241 VLFPGSGGNQGEVESGLAGEIRLQSDHTLARDSRTACEWQSFVNNQSKLTSDFQFIFLAL 300 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 241 VLFPGSGGNQGEVESGLAGEIRLQSDHTLARDSRTACEWQSFVNNQSKLTSDFQFIFLAL 300 Qy 301 TQLGQNPDAMTDCSAVIPISKPIPGNGPFSFFPAGKTSADVEQACASTPFPSLTTLPGPT 360 |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||| Db 301 TQLGQNPDAMTDCSAVIPISKPIPGNGPFSFFPAGKTSADVEQACASTPFPSLTTLPGPT 360 Qy 361 TSVARIPPPPGA 372 |||||||||||| Db 361 TSVARIPPPPGA 372
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Prosecution Timeline

Aug 08, 2024
Application Filed
Sep 22, 2026
Non-Final Rejection mailed — §103, §112 (current)

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Study what changed to get past this examiner. Based on 5 most recent grants.

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Prosecution Projections

1-2
Expected OA Rounds
75%
Grant Probability
89%
With Interview (+14.3%)
2y 10m (~8m remaining)
Median Time to Grant
Low
PTA Risk
Based on 953 resolved cases by this examiner. Grant probability derived from career allowance rate.

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