期刊
FEBS LETTERS
卷 595, 期 23, 页码 2931-2941出版社
WILEY
DOI: 10.1002/1873-3468.14222
关键词
acetylornithine aminotransferase; amino acid racemase; cysteine lyase; d-amino acid metabolism; multifunctional enzyme; Thermotoga maritima
资金
- Kitasato University Research Grant for Young Researchers
- Japan Society for the Promotion of Science (JSPS) KAKENHI [21K05348]
- Grants-in-Aid for Scientific Research [21K05348] Funding Source: KAKEN
The hyperthermophilic bacterium Thermotoga maritima has a peptidoglycan containing unusual d-lysine, and a novel acetylornithine aminotransferase TM1785 has been identified with diverse enzymatic activities, shedding light on d-amino acid metabolism.
The hyperthermophilic bacterium Thermotoga maritima peptidoglycan contains unusual d-lysine alongside typical d-alanine and d-glutamate. We previously identified lysine racemase and threonine dehydratase, but knowledge of d-amino acid metabolism remains limited. Herein, we identified and characterized T. maritima acetylornithine aminotransferase TM1785. The enzyme was most active towards acetyl-l-ornithine, but also utilized l-glutamate, l-ornithine and acetyl-l-lysine as amino donors, and 2-oxoglutarate was the preferred amino acceptor. TM1785 also displayed racemase activity towards four amino acids and lyase activity towards l-cysteine, but no dehydratase activity towards l-serine, l-threonine or corresponding d-amino acids. Catalytic efficiency (k(cat)/K-m) was highest for aminotransferase activity and lowest for racemase activity. TM1785 is a novel acetylornithine aminotransferase associated with l-arginine biosynthesis that possesses two additional distinct activities.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据