Acrolein, an irreversible active-site-directed inhibitor of deoxyribose 5-phosphate aldolase?
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Acrolein, an irreversible active-site-directed inhibitor of deoxyribose 5-phosphate aldolase?
The enzyme deoxyribose 5-phosphate aldolase was irreversibly inactivated by the substrate analogue acrolein with a pseudo-first-order rate constant of 0.324 min-1 and a Ki (apparent) of 2.7 x 10(-4) m. No inactivation was observed after prolonged incubation with the epoxide analogues glycidol phosphate and glycidaldehyde. It is suggested that the acrolein is first activated by forming a Schiff ...
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The fermentation of deoxyribose in Escherichia coli (1, 2) and in Lactobacillus plantarum (3, 4) appears to involve 2-deoxyribose 5-phosphate as an intermediate. Racker (2) has described an enzyme, deoxyribose phosphate aldolase, which catal.yzes the reversible cleavage of deoxyribose 5-phosphate to acetaldehyde and glyceraldehyde 3-phosphate. The enzyme occurs in E. coli and in animal tissues ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1976
ISSN: 0264-6021
DOI: 10.1042/bj1530495