Function
Has high formaldehyde dehydrogenase activity in the presence of glutathione and catalyzes the oxidation of normal alcohols in a reaction that is not GSH-dependent. In addition, hemithiolacetals other than those formed from GSH, including omega-thiol fatty acids, also are substrates. Also acts as a S-nitroso-glutathione reductase by catalyzing the NADH-dependent reduction of S-nitrosoglutathione.
Biological Context
Subcellular Location: Cytoplasm
Product Specifications
Recombinant Escherichia coli S- (hydroxymethyl)glutathione dehydrogenase (frmA) is a recombinant protein from Escherichia coli (strain UTI89 / UPEC), expressed in E.coli, covering amino acids 1-369aa, with N-terminal 10xHis-tagged and C-terminal Myc-tagged tag, molecular weight 46.8kDa, purity Greater than 90% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications. Explore more Enzyme proteins →
