EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.7.1.176 | ATP + UDP-alpha-D-glucose |
- |
Neisseria gonorrhoeae |
ADP + UDP-alpha-D-glucose 3'-phosphate |
- |
? |
2.7.1.176 | ATP + UDP-muramic acid |
ngzeta_1 phosphorylates UDP-muramic acid (UNAM) at the 4'-hydroxy group, binding structure analysis of substrate and product. The phosphate group on UNAM is attached to the C4'-OH and not to the C3'-OH group atom, different to what has been described for the hitherto characterized zeta UNAG kinases |
Neisseria gonorrhoeae |
ADP + UDP-muramic acid 4'-phosphate |
- |
? |
2.7.1.176 | ATP + UDP-N-acetyl-alpha-D-glucosamine |
- |
Streptococcus pneumoniae |
ADP + UDP-N-acetyl-alpha-D-glucosamine 3'-phosphate |
- |
? |
2.7.1.176 | ATP + UDP-N-acetyl-alpha-D-glucosamine |
- |
Neisseria gonorrhoeae |
ADP + UDP-N-acetyl-alpha-D-glucosamine 3'-phosphate |
- |
? |
2.7.1.176 | ATP + UDP-N-acetyl-D-glucosamine |
the kinase activity is responsible for the toxic function in vivo, because the phosphorylated product inhibits MurA, the enzyme responsible for the first step of peptidoglycan synthesis in bacteria, mechanism, overview |
Escherichia coli |
ADP + UDP-N-acetyl-D-glucosamine 3'-phosphate |
- |
? |
2.7.1.176 | ATP + UDP-N-acetyl-D-glucosamine |
the kinase activity is responsible for the toxic function in vivo, because the phosphorylated product inhibits MurA, the enzyme responsible for the first step of peptidoglycan synthesis in bacteria, mechanism, overview |
Streptococcus pyogenes |
ADP + UDP-N-acetyl-D-glucosamine 3'-phosphate |
- |
? |
2.7.1.176 | ATP + UDP-N-acetyl-D-glucosamine |
the kinase activity is responsible for the toxic function in vivo, because the phosphorylated product inhibits MurA, the enzyme responsible for the first step of peptidoglycan synthesis in bacteria, mechanism, overview |
Streptococcus pneumoniae |
ADP + UDP-N-acetyl-D-glucosamine 3'-phosphate |
- |
? |
2.7.1.176 | ATP + UDP-N-acetyl-D-glucosamine |
enzyme-substrate interaction analysis, overview. PezT activity is specific for the presence of the 2'-N-acetyl group on the sugar moiety and the stereoisomeric form of UDP-N-acetyl-D-glucosamine, selectivity for UDPglucose and UDP-N-acetylgalactosamine is dramatically reduced |
Escherichia coli |
ADP + UDP-N-acetyl-D-glucosamine 3'-phosphate |
- |
? |
2.7.1.176 | ATP + UDP-N-acetyl-D-glucosamine |
enzyme-substrate interaction analysis, overview. PezT activity is specific for the presence of the 2'-N-acetyl group on the sugar moiety and the stereoisomeric form of UDP-N-acetyl-D-glucosamine, selectivity for UDPglucose and UDP-N-acetylgalactosamine is dramatically reduced |
Streptococcus pneumoniae |
ADP + UDP-N-acetyl-D-glucosamine 3'-phosphate |
- |
? |
2.7.1.176 | ATP + UDP-N-acetyl-D-glucosamine |
enzyme-substrate interaction analysis, overview. PezT activity is specific for the presence of the 2'-N-acetyl group on the sugar moiety and the stereoisomeric form of UDP-N-acetyl-D-glucosamine, selectivity for UDPglucose and UDP-N-acetylgalactosamine is dramatically reduced. UDP-N-acetyl-D-glucosamine binds to a deep cleft at the molecular surface of the zeta toxin. The side chain group of Asp67 forms a hydrogen bond to the 3'-hydroxyl group of the amino sugar moiety of the substrate |
Streptococcus pyogenes |
ADP + UDP-N-acetyl-D-glucosamine 3'-phosphate |
UDP-N-acetyl-D-glucosamine 3'-phosphate enriches during PezT poisoning in vivo and inhibits peptidoglycan synthesis |
? |