EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
    2.7.7.23 | more |
glycosylation pathway |
Drosophila melanogaster |
? |
- |
? |
| 2.7.7.23 | more |
bifunctional enzyme that catalyzes two consecutive reactions leading to the biosynthesis of UDP-N-acetylglucosamine, in the first reaction, GlmU catalyzes the CoA-dependent acetylation of glucosamine-1-phosphate to afford N-acetylglucosamine-1-phosphate, in the second reaction, the UMP moiety from a UTP molecule is transferred to N-acetyl-alpha-D-glucosamine 1-phosphate to give the final product UDP-GlcNAc |
Mycobacterium tuberculosis |
? |
- |
? |
| 2.7.7.23 | more |
enzyme shows relaxed tolerance for modifications at N-acyl, C-3, C-4, and C-6 positions, with a preference for small substituent groups. The yields are low to moderate (10-65%) and some sugar-1-Ps fail to generate the corresponding UDP-sugars due to the steric problem |
Escherichia coli |
? |
- |
? |
| 2.7.7.23 | more |
enzyme additionally shows the activity of UTP-glucose-1-phosphate uridylyltransferase, EC 2.7.7.9 |
Arabidopsis thaliana |
? |
- |
? |
| 2.7.7.23 | more |
no substrates: CTP, GTP, ITP or ATP, glucose 1-phosphate, glucosamine 1-phosphate, xylose 1-phosphate, galactose 1-phosphate, galactosamin 1-phosphate, fucose 1-phosphate, mannose 1-phosphate, galactosamine 1-phosphate, fructose 1-phosphate, or glucose 6-phosphate |
Arabidopsis thaliana |
? |
- |
? |
| 2.7.7.23 | more |
the human and trypanosome enzymes both display a strictly ordered bi-bi mechanism, but with the order of substrate binding reversed. Human UAP does not bind UTP alone, and although it does show significant binding to GlcNAc-1-P, it is not possible to calculate an affinity due to complex binding kinetics |
Homo sapiens |
? |
- |
? |
| 2.7.7.23 | more |
the human and trypanosome enzymes both display a strictly ordered bi-bi mechanism, but with the order of substrate binding reversed. Trypanosoma brucei UAP binds UTP alone with a KD of 83.1 microM, but does not bind GlcNAc-1-P alone |
Trypanosoma brucei brucei |
? |
- |
? |
| 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 |
Mycobacterium tuberculosis |
? |
- |
? |
| 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 |
Mycobacterium tuberculosis |
? |
- |
? |
| 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 |
Mycobacterium tuberculosis |
? |
- |
? |
