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
Activity	4.1.1.12
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