EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.7.7.23 | more |
GlcNAc-1-P displays hydrogen bond interactions with residues Q110, R113, K120, D209, S215, and A217. the loops moved close to UTP and narrowed the entrance. Other residues that are surrounding the UTP include L106, G108, G109, K120, P218, D219, G220, N325, I326, C327, K374, and F378, which form hydrophobic, electrostatic, and van der Waals interactions, thus increasing the stability of this complex. In UTP-bound form, the residues present in the nucleotide-binding loop of UAP does not have a major role in binding to uridine. Docking analysis of substrates and products, overview |
Bombyx mori |
? |
- |
- |
2.7.7.23 | CTP + N-acetyl-alpha-D-glucosamine 1-phosphate |
- |
Escherichia coli |
diphosphate + CDP-N-acetyl-alpha-D-glucosamine |
- |
? |
2.7.7.23 | diphosphate + UDP-glucose |
- |
Giardia intestinalis |
UTP + D-glucose 1-phosphate |
- |
? |
2.7.7.23 | diphosphate + UDP-glucose |
30% of the activity with UDP-N-acetylglucosamine |
Bos taurus |
UTP + D-glucose 1-phosphate |
- |
? |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-galactosamine |
- |
Giardia intestinalis |
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate |
- |
? |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-galactosamine |
2.8% of the activity with UDP-N-acetylglucosamine |
Staphylococcus aureus |
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate |
- |
? |
2.7.7.23 | diphosphate + UDP-N-acetyl-D-galactosamine |
2-3 times more active with N-acetyl-D-galactosamine 1-phosphate than with N-acetyl-D-glucosamine 1-phosphate, AGX2 8 times less active with N-acetyl-D-galactosamine 1-phosphate than with N-acetyl-D-glucosamine 1-phosphate |
Homo sapiens |
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate |
- |
? |
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 |
? |
- |
? |