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Arch Biochem Biophys. 1988 Feb 1;260(2):601-8.

Substrate specificity of nicotinamide methyltransferase isolated from porcine liver.

Author information

1
Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254.

Abstract

Nicotinamide methyltransferase (EC 2.1.1.1) has been purified over 1300-fold from porcine liver. The enzyme is electrophoretically homogeneous, exhibiting a relative molecular mass of 27,000. In addition to acting on nicotinamide and close structural analogs such as thionicotinamide and 3-acetylpyridine, the enzyme actively accommodates poor analogs such as quinoline, isoquinoline, and 1,2,3,4-tetrahydroisoquinoline as methyl group acceptors. The enzyme may thus have the function of detoxicating numerous alkaloids in vivo. In some cases, the action of the enzyme might paradoxically increase the toxicities of substrates, but the hepatotoxic antibiotic pyrazinamide, which we considered as potentially such an enzyme-activated electrophile, did not function detectably as a substrate for the isolated enzyme.

PMID:
2963591
DOI:
10.1016/0003-9861(88)90487-0
[Indexed for MEDLINE]

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