Discovery of a monomeric flavin-containing opine dehydrogenase from bacteria.

IF 1.4 4区生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY

Bioscience, Biotechnology, and Biochemistry Pub Date : 2025-06-23 DOI:10.1093/bbb/zbaf096

Seiya Watanabe, Kentaroh Yoshiwara, Mizue Date, Yasunori Watanabe

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引用次数: 0

Abstract

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.

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从细菌中发现单体含黄素的阿片脱氢酶。

毒碱，如野棕榈碱和章鱼碱，是由根癌农杆菌在树冠瘿中特异性产生的，并被毒碱脱氢酶（OpnDH）特异性地分解。已知的OpnDH由α-， β-和γ-亚基组成，其中含有FAD， FMN和两个铁硫簇作为辅因子。本文中，我们从altamirensis金黄色单胞菌（Aureimonas altamirensis, AaOdhB3）中鉴定出一种新型含fad的OpnDH，它由一个多肽组成，与异质酶β-亚基的序列同源性仅为~ 22%。AaOdhB3是一种单体结构，对野碱具有严格的特异性。晶体学分析表明，FAD的整体结构和结合方式与d -氨基酸氧化酶超家族成员相似。位点定向诱变分析和与该蛋白家族其他成员的结构比较表明，Arg312（和Arg247）对底物识别具有重要意义，而与产自瘤胃杆菌的桑索普代谢相关的果糖基氨基酸氧化酶在系统发育和生理上与OdhB3接近。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Bioscience, Biotechnology, and Biochemistry 生物-生化与分子生物学

CiteScore

3.50

自引率

0.00%

发文量

183

审稿时长

1 months

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).