Studies on N-acetylneuraminic acid aldolase
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Printed in Great Britain Studies on N - Acetylneuraminic Acid Aldolase By J . E . G . BARNETT
N-Acetylneuraminic acid aldolase from Glostridium perfringens was irreversiblv inactivated by 1 mM-bromopyruvate with a half-life of 4.2min at pH 7.2 and 370C. The rate of inactivation was diminished in the presence of pyruvate but not with N-acetyl-D-mannosamine, indicating that the inhibitor acted at, or close to, the pyruvate-binding site. The apparent K, for bromopyruvate, calculated from t...
متن کاملCorrigendum: Characterization of a novel N-acetylneuraminic acid lyase favoring industrial N-acetylneuraminic acid synthesis process
The original version of this article contained an error in testing the kinetic parameters of CgNal towards pyruvate, in which the concentration of ManNAc (50 mM) was not in excess. This error was corrected by re-running the assay in the presence of excessive ManNAc (180 mM). The corrected kinetic parameters of CgNal towards pyruvate are shown in Table 1. These changes do not change the conclusi...
متن کاملCharacterization of a novel N-acetylneuraminic acid lyase favoring N-acetylneuraminic acid synthesis
N-Acetylneuraminic acid lyase (NAL, E.C. number 4.1.3.3) is a Class I aldolase that catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (Neu5Ac) from pyruvate and N-acetyl-D-mannosamine (ManNAc). Due to the equilibrium favoring Neu5Ac cleavage, the enzyme catalyzes the rate-limiting step of two biocatalytic reactions producing Neu5Ac in industry. We report the biochemical charact...
متن کاملSynthesis of N-acetylneuraminic acid and of CMP-N-acetylneuraminic acid in the rat liver cell.
Adult male rats, under starving and normal conditions, were injected intravenously with N-acetyl[3H]mannosamine and after various time intervals the specific radioactivities of free N-acetylneuraminic acid (NeuAc) and CMP-N-acetylneuraminic acid were determined in the liver. The specific radioactivity of free NeuAc was high even within 20s after injection; the maximum was reached between 7 and ...
متن کاملCytidine Monophospho-N- Acetylneuraminic Acid Hydroxylase (CMAH)
Introduction . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1560 Databanks . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1561 Name and History . . . ....
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1971
ISSN: 0306-3283
DOI: 10.1042/bj1250275