Enzymatic characterization of a thermostable 6-phosphogluconate dehydrogenase from <i>Hydrogenobacter thermophilus</i> and its application for NADH regeneration.

ABSTRACT: 6-Phosphogluconate dehydrogenases (6PGDHs) are widely existing as reduced cofactor (NADH/NADPH) regeneration biocatalysts. Herein, a thermostable 6PGDH from Hydrogenobacter thermophilus (Ht6PGDH) was overexpressed in Escherichia coli and enzymologically characterized. Ht6PGDH exhibited exceptional stability and catalytic activity under high-temperature conditions, with an optimum temperature of 85 °C and the ability to maintain high activity for prolonged periods at 70 °C, which could be purified through a one-step heat treatment. Moreover, Ht6PGDH exhibited a preference for NAD⁺ with a K _m value of 0.4 mM and a k _cat value of 28.6 s⁻¹, demonstrating a significant preference over NADP⁺. These properties rend

SUBMITTER: Feng X 

PROVIDER: S-EPMC11621248 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature