Simultaneous Measurement of Glucose-6-phosphate 3‑Dehydrogenase (NtdC) Catalysis and the Nonenzymatic Reaction of Its Product: Kinetics and Isotope Effects on the First Step in Kanosamine Biosynthesis

• Published in: Biochemistry (Easton) Vol. 56; no. 14; pp. 2001 - 2009
• Main Authors: Vetter, Natasha D, Palmer, David R. J
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 11.04.2017
• Subjects: Bacillus subtilis - genetics; Bacillus subtilis - metabolism; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Biocatalysis; Deuterium; Escherichia coli - genetics; Escherichia coli - metabolism; Gene Expression Regulation, Bacterial; Glucosamine - biosynthesis; Glucose-6-Phosphate; Glucosephosphate Dehydrogenase - genetics; Glucosephosphate Dehydrogenase - metabolism; Glutamic Acid - metabolism; Hydrogen-Ion Concentration; Kinetics; NAD - metabolism; Operon; Oxidation-Reduction; Protons; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Thermodynamics

Glucose-6-phosphate 3-dehydrogenase (NtdC) is an NAD-dependent oxidoreductase encoded in the NTD operon of Bacillus subtilis. The oxidation of glucose 6-phosphate by NtdC is the first step in kanosamine biosynthesis. The product, 3-oxo-d-glucose 6-phosphate (3oG6P), has never been synthesized or iso...