Literature DB >> 7082642

Kinetic studies on the O-methylation of dopamine by human brain membrane-bound catechol O-methyltransferase.

A J Rivett, J A Roth.   

Abstract

Km values for dopamine and S-adenosylmethionine (AdoMet) of human brain membrane-bound catechol O-methyltransferase are 3.3 microM and 3.1 microM, respectively. S-Adenosylhomocysteine is a very potent competitive inhibitor with respect to AdoMet with a Ki value of 1 microM. Product inhibition patterns strongly support a steady-state compulsory-order ternary complex mechanism in which AdoMet binds to the enzyme before dopamine. Inhibition of membrane-bound COMT by tropolone is competitive with respect to dopamine (Ki = 5 microM) and uncompetitive with respect to AdoMet and is consistent with this type of mechanism. The mechanism proposed is different from that suggested for soluble catechol O-methyltransferases.

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Year:  1982        PMID： 7082642     DOI： 10.1021/bi00537a006

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


  18 in total

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3.  Kinetics and inhibition studies of catechol O-methyltransferase from the yeast Candida tropicalis.

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9.  Kinetic and inhibition studies on catechol-O-methyltransferase affinity labelling by N-(3,4-dihydroxyphenyl)maleimide.

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10.  Homeostatic mechanisms in dopamine synthesis and release: a mathematical model.

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