作者: C C Chang , A Laghai , M H O'Leary , H G Floss
DOI: 10.1016/S0021-9258(18)34816-6
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摘要: Aspartate beta-decarboxylase catalyzes abortive decarboxylation/transamination of [2-3H]aspartate with at least 17% internal transfer tritium to the pro-S position C-4' resulting pyridoxamine phosphate. In normal beta-decarboxylation reaction, 1.06% from alpha-position aspartate appears in product alanine. The enzyme slow hydrogen exchange beta-position alanine but not aspartate. replacement beta-carboxyl group by occurs an inversion mode. These results are interpreted terms a two-base mechanism.