1.3.1.98: UDP-N-acetylmuramate dehydrogenase
This is an abbreviated version!
For detailed information about UDP-N-acetylmuramate dehydrogenase, go to the full flat file.
Word Map on EC 1.3.1.98
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1.3.1.98
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peptidoglycan
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aureus
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fad
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udp-n-acetylmuramic
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epidermidis
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medicine
- 1.3.1.98
- peptidoglycan
- aureus
- fad
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udp-n-acetylmuramic
- epidermidis
- medicine
Reaction
Synonyms
alr5066, EC 1.1.1.158, More, MurB, MurBAb, PA2977, PaMurB, reductase, uridine diphosphoacetylpyruvoylglucosamine, type I UNAGEP reductase, UDP-GlcNAc-enoylpyruvate reductase, UDP-N-acetylenolpyruvoylglucosamine reductase, UDP-N-acetylenolpyruvyl glucosamine reductase, UDP-N-acetylenolpyruvylglucosamine reductase, UDP-N-acetylglucosamine-enoylpyruvate reductase, UDP-N-acetylmuramate dehydrogenase, UNAGEP reductase, uridine diphospho-N-acetylglucosamine-enolpyruvate reductase, uridine-5'-diphospho-N-acetyl-2-amino-2-deoxy-3-O-lactylglucose:NADP-oxidoreductase, VspiD_010100018130
ECTree
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Metals Ions
Metals Ions on EC 1.3.1.98 - UDP-N-acetylmuramate dehydrogenase
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Cs+
K+
Na+
NH4+
Rb+
Tl+
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affinity about 8 times greater than K+, activation in decreasing order: Tl+, K+, NH4+, Rb+, Li+, Na+
additional information
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at saturating cation concentration maximal enzyme activity: 2 units/mg
K+
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at saturating cation concentration maximal enzyme activity: 50 units/mg
K+
PaMurB crystal structure contains a potassium ion in the active site. The potassium ion displays a pentagonal bipyramidal coordination geometry with two main chain oxygen atoms (Ala237, Ser239), one side chain carboxyl oxygen atom from Glu-335, one side chain oxygen atom of Asn-57 and the O7n oxygen atom of the nicotinamide ring as ligands. The potassium ion activates MurB by facilitating substrate orientation and binding
Na+
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at saturating cation concentration maximal enzyme activity: 5 units/mg
NH4+
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at saturating cation concentration maximal enzyme activity: 35 units/mg
Rb+
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at saturating cation concentration maximal enzyme activity: 33 units/mg