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
1.3.1.98 UDP-N-acetylmuramate dehydrogenaseAdvanced search results
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Engineering
Engineering on EC 1.3.1.98 - UDP-N-acetylmuramate dehydrogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
S226A
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, no complementation of murB-deficient, temperature-sensitive Staphylcoccus aureus mutant strain TS2901
R176A
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, no complementation of murB-deficient, temperature-sensitive Staphylcoccus aureus mutant strain TS2901
R213A
site-directed mutagenesis, nearly inactive mutant, no complementation of murB-deficient, temperature-sensitive Staphylcoccus aureus mutant strain TS2901
R230A
site-directed mutagenesis, functional complementation of murB-deficient, temperature-sensitive Staphylcoccus aureus mutant strain TS2901
N71A
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, no complementation of murB-deficient, temperature-sensitive Staphylcoccus aureus mutant strain TS2901
S226A
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site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, no complementation of murB-deficient, temperature-sensitive Staphylcoccus aureus mutant strain TS2901
S243F
strong decrease in enzyme activity, thinner cell walls than wild type strain
S70A
site-directed mutagenesis, functional complementation of murB-deficient, temperature-sensitive Staphylcoccus aureus mutant strain TS2901
Y175F
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, poor functional complementation of murB-deficient, temperature-sensitive Staphylcoccus aureus mutant strain TS2901
N71A
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site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, no complementation of murB-deficient, temperature-sensitive Staphylcoccus aureus mutant strain TS2901
E275K
strong decrease in enzyme activity, thinner cell walls than wild type strain
H259A
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, no complementation of murB-deficient, temperature-sensitive Staphylcoccus aureus mutant strain TS2901
G78D
strong decrease in enzyme activity, thinner cell walls than wild type strain
G69A
site-directed mutagenesis, functional complementation of murB-deficient, temperature-sensitive Staphylcoccus aureus mutant strain TS2901
G67A
site-directed mutagenesis, functional complementation of murB-deficient, temperature-sensitive Staphylcoccus aureus mutant strain TS2901
G251D
strong decrease in enzyme activity, thinner cell walls than wild type strain
E296A
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme, no complementation of murB-deficient, temperature-sensitive Staphylcoccus aureus mutant strain TS2901
E275K
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strong decrease in enzyme activity, thinner cell walls than wild type strain
additional information
additional information
construction of a murB null mutant strain UHM350, introduction of PpetE-murB (pPJAV329) into the murB mutant in the presence of copper is sufficient for complete segregation of the murB insertion and created a viable strain UHM350, which displays a growth defect and spontaneously lyses if not passaged every 2 weeks once a sufficient density is reached during plate-based culture containing copper. The pattern of functional heterocysts and average filament lengths is altered and impaired compared to the wild-type
additional information
-
construction of a murB null mutant strain UHM350, introduction of PpetE-murB (pPJAV329) into the murB mutant in the presence of copper is sufficient for complete segregation of the murB insertion and created a viable strain UHM350, which displays a growth defect and spontaneously lyses if not passaged every 2 weeks once a sufficient density is reached during plate-based culture containing copper. The pattern of functional heterocysts and average filament lengths is altered and impaired compared to the wild-type
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