EC Number |
Natural Substrates |
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2.7.7.23 | more |
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a bifunctional enzyme catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase, the enzyme catalyzes the two reactions, acetyl transfer and uridyl transfer, at two independent domains, regulation, overview |
2.7.7.23 | more |
N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is a pivotal bifunctional enzyme, its N- and C-terminal domains catalyzes uridyltransferase, EC 2.7.7.23, and acetyltransferase, EC 2.3.1.157, activities, respectively |
2.7.7.23 | more |
the bifunctional role of GlmU arises from two independent domains of the enzyme which possess acetyltransferase, EC 2.3.1.157, and uridyltransferase, EC 2.7.7.23, activities. The acetyltransferase domain, found in the C-terminus of the protein, is responsible for the first step of the reaction, in which an acetyl group is transferred from AcCoA to GlcN-1-P forming GlcNAc-1-P. GlcNAc-1-P then serves as a substrate for the uridyltransferase active site in the N-terminus of the enzyme which forms UDP-GlcNAc |
2.7.7.23 | more |
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. Acetyltransfer precedes uridyltransfer with both the acetyltransferase and uridyltransferase reactions taking place in two separable active sites in bifunctional GlmU where the acetyltransferase domain of GlmU does not show homology with its eukaryotic counterpart |
2.7.7.23 | more |
the N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU) enzyme is a bifunctional enzyme with both acetyltransferase and uridylyltransferase (pyrophosphorylase) activities, catalyzing the reactions of EC 2.3.1.157, N-acetylglucosamine-1-phosphate uridyltransferase, and 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase. The synthesis of the two metabolic intermediates N-acetylglucosamine-1-phosphate (GlcNAc-1-P) and UDP-GlcNAc is catalyzed by the C- and N-terminal domains, respectively. UDP-GlcNAc is a key metabolite essential for the synthesis of peptidoglycan, disaccharide linker, arabinogalactan and mycothiols |
2.7.7.23 | N-acetyl-D-glucosamine 1-phosphate + UTP |
- |
2.7.7.23 | N-acetylglucosamine 1-phosphate + uridine 5'-triphosphate |
- |
2.7.7.23 | UTP + N-acetyl-alpha-D-galactosamine 1-phosphate |
- |
2.7.7.23 | UTP + N-acetyl-alpha-D-galactosamine 1-phosphate |
reaction of EC 2.7.7.83 |
2.7.7.23 | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate |
involved in the synthesis of UDP-N-acetyl-galactoseamine, which is important for cyst wall synthesis |