期刊
EXTREMOPHILES
卷 26, 期 3, 页码 -出版社
SPRINGER JAPAN KK
DOI: 10.1007/s00792-022-01282-z
关键词
2-keto-3-deoxy-d-gluconate; Type-2 malate; l-Lactate dehydrogenase; Thermus thermophiles; Extremozyme
A previously unidentified protein (TTHB078) from Thermus thermophilus HB8 exhibits a novel reductase activity on KDG. This enzyme, named KdgG, uses NADH and NADPH as electron donors and catalyzes the reversible reduction of KDG to form 3-deoxy-d-mannonate.
2-Keto-3-deoxy- d-gluconate (KDG) is an important intermediate found in various sugars, sugar acids and polysaccharide catabolic pathways. Here, we report that a functionally uncharacterized type-2 malate/l-lactate dehydrogenase family protein (TTHB078) from Thermus thermophilus HB8 catalyzes a novel reaction, NAD(P)H-dependent reductase activity on KDG. This enzyme, designated KdgG, utilizes both NADH and NADPH as electron donors, but higher activity was observed with NADH. Analysis of the reaction product revealed that KdgG catalyzes reversible reduction of KDG to form 3-deoxy-d-mannonate. Molecular phylogenetic analysis indicated that KdgG and its homologs distributed in the genus Thermus form a novel clade among type-2 malate/l-lactate dehydrogenase family proteins.
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