Differences in coenzyme specificity of the N5-methyltetrahydrofolate-homocysteine methyltransferases of various species: implications for corrin binding loci.

Abstract:

:Investigations of the coenzyme specificity of N5-methyltetrahydrofolate-homocysteine methyltransferases of diverse biological origin revealed previously unrecognized differences between Escherichia coli methyltransferase and the corresponding enzymes of other species. Cyanocobalamin (CNCbl) actively supports methyltransferase in extracts of animal tissues and E. coli. Cobinamide is more active than CNCbl with rat liver methyltransferase; however, it is non-competitively inhibitory with E. coli enzyme. E. coli methyltransferase, but not rat liver enzyme, is competitively inhibited by alpha-ribazole 3'-phosphate and 5,6-dimethyl-benzimidazole, two moieties of the nucleotide loop. This suggests that animal enzyme binds its corrinoid coenzyme at a site on the corrin macro-ring, while E. coli enzyme binds to the nucleotide loop as well as the macro-ring.

authors

Beck WS,Thorndike J

doi

10.1016/0006-291x(84)91415-3

subject

Has Abstract

pub_date

1984-04-16 00:00:00

pages

74-80

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(84)91415-3

journal_volume

120

pub_type

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