منابع مشابه
Deoxyribose Phosphate Aldolase from Rat Liver.
The activity and properties of deoxyribose phosphate aldolase from Escherichia coli and Lactobacillus plantarum have been described in detail by Racker (1) and Pricer and Horecker (2). The enzyme from E. coli was shown to be active at pH values between 6.0 and 8.0 in tris(hydroxymethyl)aminomethane and phosphate buffers without exhibiting a sharp optimum (1). The enzyme from L. plunturum was sh...
متن کاملAcrolein, 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 ...
متن کاملDeoxyribose Aldolase from Lactobacihs plantarum
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 ...
متن کاملLinking coupled motions and entropic effects to the catalytic activity of 2-deoxyribose-5-phosphate aldolase (DERA)
DERA, 2-deoxyribose-5-phosphate aldolase, catalyzes the retro-aldol cleavage of 2-deoxy-ribose-5phosphate (dR5P) into glyceraldehyde-3-phosphate (G3P) and acetaldehyde in a branch of the pentose phosphate pathway. In addition to the physiological reaction, DERA also catalyzes the reverse addition reaction and, hence, is an interesting candidate for bio-catalysis of carbo-ligation reactions, whi...
متن کاملPresence of a novel phosphopentomutase and a 2-deoxyribose 5-phosphate aldolase reveals a metabolic link between pentoses and central carbon metabolism in the hyperthermophilic archaeon Thermococcus kodakaraensis.
Numerous bacteria and mammalian cells harbor two enzymes, phosphopentomutase (PPM) and 2-deoxyribose 5-phosphate aldolase (DERA), involved in the interconversion between nucleosides and central carbon metabolism. In this study, we have examined the presence of this metabolic link in the hyperthermophilic archaeon, Thermococcus kodakaraensis KOD1. A search of the genome sequence of this strain r...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1967
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)96331-3