EC Number   |
Natural Substrates |
|---|
    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-glucosamine 1-phosphate |
- |
| 2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine |
amino sugar metabolism |
| 2.7.7.23 | UTP + N-acetyl-alpha-D-glucosamine 1-phosphate |
because the multifunctional ST0452 protein is capable of catalyzing the last two reactions (Ec 2.3.1.157 and EC 2.7.7.23 (UDP-N-acetylglucosamine diphosphorylase)) of the bacteria-type four-step biosynthesis pathway of UDP-GlcNAc from fructose 6-phosphate, the ST0452 protein plays an important role for the bacteria-type UDP-GlcNAc biosynthesis pathway in this archaeon |
| 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 |
| 2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine |
deficiency mutant fully swollen and some are lysed |
| 2.7.7.23 | diphosphate + UDP-N-acetyl-D-glucosamine |
enzyme of the Leloir pathway |
| 2.7.7.23 | more |
glycosylation pathway |
