Glucosamine-6-phosphate deaminase
نویسندگان
چکیده
منابع مشابه
Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution.
BACKGROUND Glucosamine 6-phosphate deaminase from Escherichia coli is an allosteric hexameric enzyme which catalyzes the reversible conversion of D-glucosamine 6-phosphate into D-fructose 6-phosphate and ammonium ion and is activated by N-acetyl-D-glucosamine 6-phosphate. Mechanistically, it belongs to the group of aldoseketose isomerases, but its reaction also accomplishes a simultaneous amina...
متن کاملGlucosamine metabolism. V. Enzymatic synthesis of glucosamine 6-phosphate.
Studies in viva on the biosynthesis of n-glucosamine, with the use of specifically labeled glucose in the rat (1,2) and in group A streptococci (3-5) showed that the glucose carbon chain was preserved during its conversion to the hexosamine. Leloir and Cardini (6, 7) noted that extracts obtained from Neurospora crassa converted glutamine and hexose phosphate to glutamic acid and a product tenta...
متن کاملGlucose-6-phosphate as a probe for the glucosamine-6-phosphate N-acetyltransferase Michaelis complex.
Glucosamine-6-phosphate N-acetyltransferase (GNA1) catalyses the N-acetylation of d-glucosamine-6-phosphate (GlcN-6P), using acetyl-CoA as an acetyl donor. The product GlcNAc-6P is an intermediate in the biosynthesis UDP-GlcNAc. GNA1 is part of the GCN5-related acetyl transferase family (GNATs), which employ a wide range of acceptor substrates. GNA1 has been genetically validated as an antifung...
متن کاملAllosteric Activation of Escherichia coli Glucosamine-6-Phosphate Deaminase (NagB) In Vivo Justified by Intracellular Amino Sugar Metabolite Concentrations.
UNLABELLED We have investigated the impact of growth on glucosamine (GlcN) and N-acetylglucosamine (GlcNAc) on cellular metabolism by quantifying glycolytic metabolites in Escherichia coli Growth on GlcNAc increased intracellular pools of both GlcNAc6P and GlcN6P 10- to 20-fold compared to growth on glucose. Growth on GlcN produced a 100-fold increase in GlcN6P but only a slight increase in Glc...
متن کاملN-Acetylation of glucosamine-6-phosphate in Leuconostoc mesenteroides.
A partially purified enzyme (120-fold) from Leuconostoc mesenteroides catalyzed the reversible N-acetylation of d-glucosamine-6-phosphate. Coenzyme A was not required and inhibited the reaction rate. Neither d-glucosamine nor N-acetyl-d-glucosamine served as a substrate for the reversible reaction. The enzyme preparation retained 50% of its original activity after 5 min at 100 C. The K(m) for a...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta
سال: 1956
ISSN: 0006-3002
DOI: 10.1016/0006-3002(56)90124-x