A functionally uncharacterized type-2 malate/L-lactate dehydrogenase family protein from Thermus thermophilus HB8 catalyzes stereospecific reduction of 2-keto-3-deoxy-D-gluconate.

Autor: Shimizu T; Faculty of Life, Environmental Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki, 305-8572, Japan.; Research Institute of Innovative Technology for the Earth (RITE), 9-2 Kizugawa-Shi, Kizugawadai, Kyoto, 619-0292, Japan., Nakamura A; Faculty of Life, Environmental Sciences, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki, 305-8572, Japan. nakamura.akira.fm@u.tsukuba.ac.jp.; Microbiology Research Center for Sustainability (MiCS), University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki, 305-8572, Japan. nakamura.akira.fm@u.tsukuba.ac.jp.
Jazyk: angličtina
Zdroj: Extremophiles : life under extreme conditions [Extremophiles] 2022 Nov 23; Vol. 26 (3), pp. 37. Date of Electronic Publication: 2022 Nov 23.
DOI: 10.1007/s00792-022-01282-z
Abstrakt: 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.
(© 2022. The Author(s), under exclusive licence to Springer Japan KK, part of Springer Nature.)
Databáze: MEDLINE
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