Characterization of N-acetylneuraminic acid synthase isoenzyme 1 from Campylobacter jejuni
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منابع مشابه
Characterization of N-acetylneuraminic acid synthase isoenzyme 1 from Campylobacter jejuni.
Escherichia coli NeuNAc (N-acetylneuraminic acid) synthase catalyses the condensation of PEP (phosphoenolpyruvate) and ManNAc (N-acetylmannosamine) to form NeuNAc and is encoded by the neuB gene. Campylobacter jejuni has three neuB genes, one of which is very similar to the E. coli neuB gene. We have characterized the C. jejuni neuraminic acid synthase with respect to acylamino sugar specificit...
متن کاملChemical characterization of Campylobacter jejuni lipopolysaccharides containing N-acetylneuraminic acid and 2,3-diamino-2,3-dideoxy-D-glucose.
Lipopolysaccharides (LPS) of four nonencapsulated strains of the human enteric pathogen Campylobacter jejuni were chemically characterized. When applied to two of the strains, extraction by a modified phenol-chloroform-petroleum ether method (H. Brade and C. Galanos, Eur. J. Biochem. 122:233-237, 1982) gave better yields of LPS than did extraction by the conventional hot phenol-water technique....
متن کاملPurification and characterization of N-acetylneuraminic acid-9-phosphate synthase from rat liver.
Sialic acids are a group of carboxylated amino sugars important for a variety of cellular functions. N-Acetylneuraminic acid (Neu5Ac) is the predominant sialic acid in nature. Neu5Ac-9-phosphate synthase catalyzes the formation of Neu5Ac-9-phosphate from N-acetylmannosamine-6-phosphate and phosphoenolpyruvate. Neu5Ac-9-phosphate synthase was purified 11,700-fold from rat liver cytosol to appare...
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...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 2004
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj20040218