{"title":"从细菌中发现单体含黄素的阿片脱氢酶。","authors":"Seiya Watanabe, Kentaroh Yoshiwara, Mizue Date, Yasunori Watanabe","doi":"10.1093/bbb/zbaf096","DOIUrl":null,"url":null,"abstract":"<p><p>Opines, such as nopaline and octopine, are specifically produced in the crown gall by Agrobacterium tumefaciens, and specifically catabolized by opine dehydrogenase (OpnDH) from them. Known OpnDH consists of α-, β-, and γ-subunits, which contain FAD, FMN, and two iron-sulfur clusters as cofactors. We herein identified a novel type of FAD-containing OpnDH from Aureimonas altamirensis (AaOdhB3), consisting of a single polypeptide and only ∼22% sequence identity with the β-subunit of the heteromeric enzyme. AaOdhB3, a monomeric structure, exhibited strict specificity towards nopaline. A crystallographic analysis revealed that the overall structure and binding mode of FAD were similar to those of D-amino acid oxidase superfamily members. A site-directed mutagenic analysis and structural comparisons with other members of this protein family indicated the significance of Arg312 (and Arg247) for the substrate recognition, and fructosyl-amino acid oxidase, related to santhopine metabolism from A. tumefaciens, was phylogenetically and physiologically close to OdhB3.</p>","PeriodicalId":9175,"journal":{"name":"Bioscience, Biotechnology, and Biochemistry","volume":" ","pages":""},"PeriodicalIF":1.4000,"publicationDate":"2025-06-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Discovery of a monomeric flavin-containing opine dehydrogenase from bacteria.\",\"authors\":\"Seiya Watanabe, Kentaroh Yoshiwara, Mizue Date, Yasunori Watanabe\",\"doi\":\"10.1093/bbb/zbaf096\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Opines, such as nopaline and octopine, are specifically produced in the crown gall by Agrobacterium tumefaciens, and specifically catabolized by opine dehydrogenase (OpnDH) from them. Known OpnDH consists of α-, β-, and γ-subunits, which contain FAD, FMN, and two iron-sulfur clusters as cofactors. We herein identified a novel type of FAD-containing OpnDH from Aureimonas altamirensis (AaOdhB3), consisting of a single polypeptide and only ∼22% sequence identity with the β-subunit of the heteromeric enzyme. AaOdhB3, a monomeric structure, exhibited strict specificity towards nopaline. A crystallographic analysis revealed that the overall structure and binding mode of FAD were similar to those of D-amino acid oxidase superfamily members. A site-directed mutagenic analysis and structural comparisons with other members of this protein family indicated the significance of Arg312 (and Arg247) for the substrate recognition, and fructosyl-amino acid oxidase, related to santhopine metabolism from A. tumefaciens, was phylogenetically and physiologically close to OdhB3.</p>\",\"PeriodicalId\":9175,\"journal\":{\"name\":\"Bioscience, Biotechnology, and Biochemistry\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":1.4000,\"publicationDate\":\"2025-06-23\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Bioscience, Biotechnology, and Biochemistry\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://doi.org/10.1093/bbb/zbaf096\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bioscience, Biotechnology, and Biochemistry","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.1093/bbb/zbaf096","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Discovery of a monomeric flavin-containing opine dehydrogenase from bacteria.
Opines, such as nopaline and octopine, are specifically produced in the crown gall by Agrobacterium tumefaciens, and specifically catabolized by opine dehydrogenase (OpnDH) from them. Known OpnDH consists of α-, β-, and γ-subunits, which contain FAD, FMN, and two iron-sulfur clusters as cofactors. We herein identified a novel type of FAD-containing OpnDH from Aureimonas altamirensis (AaOdhB3), consisting of a single polypeptide and only ∼22% sequence identity with the β-subunit of the heteromeric enzyme. AaOdhB3, a monomeric structure, exhibited strict specificity towards nopaline. A crystallographic analysis revealed that the overall structure and binding mode of FAD were similar to those of D-amino acid oxidase superfamily members. A site-directed mutagenic analysis and structural comparisons with other members of this protein family indicated the significance of Arg312 (and Arg247) for the substrate recognition, and fructosyl-amino acid oxidase, related to santhopine metabolism from A. tumefaciens, was phylogenetically and physiologically close to OdhB3.
期刊介绍：
Bioscience, Biotechnology, and Biochemistry publishes high-quality papers providing chemical and biological analyses of vital phenomena exhibited by animals, plants, and microorganisms, the chemical structures and functions of their products, and related matters. The Journal plays a major role in communicating to a global audience outstanding basic and applied research in all fields subsumed by the Japan Society for Bioscience, Biotechnology, and Agrochemistry (JSBBA).
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