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B6db references: 82142522

type Journal Article
authors Chang, C. C.; Laghai, A.; O'Leary, M. H.; Floss, H. G.
title Some stereochemical features of aspartate beta-decarboxylase
journal J Biol Chem
ui 82142522
year (1982)
volume 257
number 7
pages 3564-9.
keywords Alcaligenes/enzymology
abstract Aspartate beta-decarboxylase catalyzes abortive decarboxylation/transamination of [2-3H]aspartate with at least 17% internal transfer of tritium to the pro-S position at C-4' of the resulting pyridoxamine phosphate. In the normal beta-decarboxylation reaction, at least 1.06% of the tritium from the alpha-position of aspartate appears in the product alanine. The enzyme catalyzes slow hydrogen exchange from the beta-position of alanine but not aspartate. The replacement of the beta-carboxyl group of aspartate by hydrogen occurs in an inversion mode. These results are interpreted in terms of a two-base mechanism.
last changed 2002/11/12 16:17

B6db references