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Results 1 - 7 of 7
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EC Number Reaction Commentary Reference
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate also N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = UDP-N-acetyl-D-glucosamine + diphosphate -, 687124
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate both reactions of bifunctional GlmU follow Michaelis Menten ordered bi-bi mechanism involving an obligatory order of binding of substrates to the enzyme 720872
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate substrate recognition, and catalytic mechanism for acetyltransfer involving His374, Asn397 and Ala391, overview 720042
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate the 2-amino group of glucosamine-1-phosphate is positioned in proximity to the acetyl-CoA to facilitate direct attack on its thioester by a ternary complex mechanism 677026
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate the catalytic mechanism is a SN2, bimolecular nucleophilic substitution reaction, catalyzed by the C-terminal domain. His374 and Asn397 act as catalytic residues by enhancing the nucleophilicity of the attacking amino group of glucosamine 1-phosphate. Ser416 and Trp460, on a short helix, provide important interactions for substrate binding 720042
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate the enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase -, 288685
Show all pathways known for 2.3.1.157Display the word mapDisplay the reaction diagram Show all sequences 2.3.1.157acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate the multifunctional enzyme from Sulfolobus tokodaii {7} is also active with acetyl-CoA + alpha-D-galactosamine 1-phosphate (galactosamine-1-phosphate N-acetyltransferase), UTP + N-acetylglucosamine 1-phosphate (EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase) and UTP + N-acetyl-alpha-D-galactosamine 1-phosphate (EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase) -, 725249
Results 1 - 7 of 7
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