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Results 1 - 10 of 11 > >>
EC Number General Information Commentary Reference
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16malfunction deletion of the isozyme is lethal 759211
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16metabolism glutamine: fructose-6-phosphate amidotransferase (GFAT) enzymes catalyse the first committed step of the hexosamine biosynthesis pathway (HBP) using glutamine and fructose-6-phosphate to form glucosamine-6-phosphate (GlcN6P) 759211
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16more mutation of residue Ser593 enhances the flexibility of the protein, which ultimately leads to increased enzyme activity, molecular dynamics simulation, homology modeling, and protein-ligand docking, overview -, 758961
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16more the glutaminase domain catalyzes the conversion of glutamine to glutamic acid with the release of ammonia. A catalytically important cysteinyl (Cys1) has been suggested to act as the mechanistic nucleophile after being activated by the N-terminal amine of the glutaminase domain (i.e. its own alpha-amine). Using molecular dynamics (MD) and quantum mechanics/molecular mechanics (QM/MM) computational methods, the active site of the glutaminase domain, the protonation state of its N-terminal amine, substrate binding, and catalytic mechanism are analysed, potential for an active site histidyl (His71) to alternatively act as the required base. A tetrahedral oxyanion intermediate is formed during the mechanism, stabilized by a water and two enzyme residues: Asn98 and Gly99. The overall rate-limiting step of the mechanism is the nucleophilic attack of a water on the thioester cross-linked intermediate with a barrier of 74.4 kJ/mol. An alternate mechanism in which His71 acts as the nucleophile-activating base, and which requires the Cys1 alpha-amine to be protonated, is calculated to be enzymatically feasible but to have a much higher overall rate-limiting barrier of 93.7 kJ/mol. Structure-function analysis and enzyme-substrate binding, overview 760122
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16more the residues involved in substrate binding are conserved in both Drosophila melanogaster GFAT1 and GFAT2 isozymes 759211
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16physiological function a GlmS deletion mutant is defective in growth unless media are supplemented with D-glucosamine. The mutant is highly sensitive to detergents, hydrophobic antibiotics, and bile salts compared to the wild-type. Mutant secretes higher amounts of beta-lactamase than the wild-type in culture supernatant fractions and is attenuated in cell culture models of Salmonella infection -, 737569
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16physiological function glucosamine-6-phosphate N-acetyltransferase (GNA1), catalyzing acetyl transfer from acetyl-coenzyme A to glucosamine-6-phosphate (GlcN-6P) and glutamine-fructose-6-phosphate aminotransferase (GlmS) catalyzing the formation of GlcN-6P from fructose-6-phosphate (Fru-6P), are two key enzymes in Bacillus subtilis for the bioproduction of N-acetylglucosamine (GlcNAc) -, 756261
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16physiological function glucosamine-6-phosphate synthase (GlmS) is a key enzyme in the biosynthesis of hexosamine 760122
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16physiological function glucosamine-6-phosphate synthase is an important enzyme for bacterial and fungal cell wall synthesis -, 758967
Show all pathways known for 2.6.1.16Display the word mapDisplay the reaction diagram Show all sequences 2.6.1.16physiological function glutamine:fructose-6-phosphate amidotransferase is a rate-limiting enzyme in the hexoamine biosynthetic pathway and plays an important role in type 2 diabetes 703705
Results 1 - 10 of 11 > >>