Add time:07/25/2019         Source:sciencedirect.com

Despite its structural similarity to catechol, 2,3-dihydroxypyridine is not a substrate but a “dead-end” inhibitor of purified pig liver catechol-O-methyltransferase. It inhibits the methylation of 3,4-dihydroxyphenylacetic acid competitively with an inhibitor constant of 15 μM. Against the methyl donor, S-adenosyl-l-methionine, it is an uncompetitive inhibitor (K′i = 85 μM). Clearly, although 2,3-dihydroxypyridine interacts with the catechol-binding site of the enzyme, the presence of a nitrogen in the ring alters its susceptibility to O-methylation.

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