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A Simplified Assay for Coenzyme M (HSCH2CH2SO3)

1974; Elsevier BV; Volume: 249; Issue: 15 Linguagem: Inglês

10.1016/s0021-9258(19)42404-6

1083-351X

Craig D. Taylor, R. S. Wolfe,

Metalloenzymes and iron-sulfur proteins

Abstract The methylation of 2,2'-dithiodiethanesulfonic acid ((S-CoM)2) by methylcobalamin-coenzyme M methyltransferase requires an additional acidic protein, when NADPH is used as the electron source. This protein component and NADPH may be replaced by sodium borohydride which acts by reducing (S-CoM)2 to 2-mercaptoethanesulfonic acid (HS-CoM) prior to methylation. Evidence suggests that reduction by borohydride is chemical rather than enzyme directed. Catalysis by 100-fold purified methyltransferase requires only methylcobalamin and HS-CoM. The assay is accurate, reliable, and may be used to determine the usual enzyme kinetic parameters.