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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Cloned
Cloned on EC 1.3.1.98 - UDP-N-acetylmuramate dehydrogenase
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gene murB or alr5066, construction of plasmid pPJAV308 and recombinant expression of the enzyme in Escherichia coli, functional complementation of a MurB enzyme-deficient Escherchia coli mutant
gene murB, overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), functional complementation of murB-deficient, temperature-sensitive Staphylcoccus aureus mutant strain TS2901 by the wild-type enzyme, and enzyme mutants G67A, S70A, G69A, and R230A
gene murB, recombinant expression of N-terminally His6-tagged enzyme, harboring a TEV protease cleavage site, in Escherichia coli strain BL21(DE3)
gene murB, Verrucomicrobium spinosum possesses a fusion open reading frame annotated by the locus tag (VspiD_010100018130). Recombinant expression in Escherichia coli strain Rosetta (DE3) pLysS. The ORF, which is predicted to encode the enzymes UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) and UDP-N-acetylmuramate:L-alanine ligase (MurC) is cloned. In vivo analyses using functional complementation shows that the fusion gene is able to functionally complement Escherichia coli murB (mutant ST5 strain) and murC temperature sensitive mutants. The purified recombinant fusion enzyme (MurB/CVs) is endowed with UDP-N-acetylmuramate:L-alanine ligase activity. All attempts to demonstrate an in vitro UDP-N-acetylenolpyruvoylglucosamine reductase (MurB) activity are unsuccessful. Phylogenetic analysis reveals that this fusion enzyme can only be identified in specific lineages within the Verrucomicrobia phylum. The fusion gene is able to functionally complement two Escherichia coli strains that harbor mutations in the murB and murC genes
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