EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
   2.7.8.33 | more |
no activity with farnesyl phosphate and geranylgeranyl phosphate. Heptaprenyl phosphate shows 3% of the activity compared to ditrans,polycis-undecaprenyl phosphate |
Thermotoga maritima |
? |
- |
? |
| 2.7.8.33 | more |
wecAHP complementes O antigen synthesis in the Escherichia coli wecA mutant |
Helicobacter pylori |
? |
- |
? |
| 2.7.8.33 | more |
the enzyme does not display any diphosphatase activity on the nucleotide substrate. Enzyme catalytic mechanism and substrate specificity, overview. The minimal length of the carbon chain of the lipid substrate for an efficient catalysis is 35. The essential aspartate residue, that is invariant in the superfamily, is Asp72 in Thermotoga maritima WecA, the residue is involved in the deprotonation of the lipid substrate during the catalytic process. No activity by the enzyme with UDP-galactose, UDP-GalNAc, GDP-glucose, ADP-ribose, UDP-glucuronic acid, GDP-D-mannose, and UDP-hexanolamine |
Thermotoga maritima |
? |
- |
? |
| 2.7.8.33 | more |
the enzyme does not display any diphosphatase activity on the nucleotide substrate. Enzyme catalytic mechanism and substrate specificity, overview. The minimal length of the carbon chain of the lipid substrate for an efficient catalysis is 35. The essential aspartate residue, that is invariant in the superfamily, is Asp72 in Thermotoga maritima WecA, the residue is involved in the deprotonation of the lipid substrate during the catalytic process. No activity by the enzyme with UDP-galactose, UDP-GalNAc, GDP-glucose, ADP-ribose, UDP-glucuronic acid, GDP-D-mannose, and UDP-hexanolamine |
Thermotoga maritima ATCC 43589 |
? |
- |
? |
| 2.7.8.33 | more |
no activity with farnesyl phosphate and geranylgeranyl phosphate. Heptaprenyl phosphate shows 3% of the activity compared to ditrans,polycis-undecaprenyl phosphate |
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589 |
? |
- |
? |
| 2.7.8.33 | UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate |
- |
Bacillus subtilis |
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol |
- |
? |
| 2.7.8.33 | UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate |
the enzyme is highly specific for UDP-GlcNAc, its physiological substrate |
Thermotoga maritima |
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol |
- |
r |
| 2.7.8.33 | UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate |
the forward and reverse exchange reactions required the presence of the second substrate, undecaprenyl phosphate and UMP, respectively. The nucleotide substrate UDPMurNAc-pentapeptide, as well as the nucleotide product UMP, can bind to MraY in the absence of lipid ligands. The enzyme is highly specific for UDP-GlcNAc, its physiological substrate |
Thermotoga maritima |
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol |
- |
r |
| 2.7.8.33 | UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate |
- |
Bacillus subtilis 168 |
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol |
- |
? |
| 2.7.8.33 | UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate |
the enzyme is highly specific for UDP-GlcNAc, its physiological substrate |
Thermotoga maritima ATCC 43589 |
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol |
- |
r |
