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Purification and characterization of hydroxypyruvate reductase from the facultative methylotroph Methylobacterium extorquens AM1.

Hydroxypyruvate reductase was purified to homogeneity from the facultative methylotroph Methylobacterium extorquens AM1. It has a molecular mass of about 71 kDa, and it consists of two identical subunits with a molecular mass of about 37 kDa. This enzyme uses both NADH (Km = 0.04 mM) and NADPH (Km =...

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Bibliographic Details
Published in:J Bacteriol
Main Authors: Chistoserdova, L V, Lidstrom, M E
Format: Artigo
Language:Inglês
Published: American Society for Microbiology (ASM) 1991
Subjects:
Online Access:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC209229/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1657886/
https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.173.22.7228-7232.1991
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