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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Vydáno v:	J Bacteriol
Hlavní autoři:	Chistoserdova, L V, Lidstrom, M E
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	American Society for Microbiology (ASM) 1991
Témata:	Research Article
On-line přístup:	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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