Catechol-0-Methyltransferase

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Abstract
The present knowledge on catechol-O-methyltransferase (COMT) (S-adenosylmethionine: catechol-O-methyltransferase, EC 2.1.1.6) is briefly reviewed. The kinetic mechanism of COMT and structural requirements of COMT inhibitors are treated in greater detail. An overall random mechanism with multiple possibilities of substrate and product binding allows a reasonable description of the kinetic data, although an ordered sequential mechanism cannot be excluded. COMT inhibitors may roughly be divided into five groups: (1) catechols acting as alternate substrates; (2) compounds devoid of catechol character, but isosteric with catechols; (3) analogues of metanephrin; (4) analogues of S-adenosy 1-methionine (SAM) and the strongly inhibiting product S-adenosy 1-homocysteine (SAH), and (5) divalent metal ions being either inhibitory (Ca^2+) or altering the ratio of m- to p-methylation of catechols. The difficulties in the evaluation of COMT function in brain are discussed.

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