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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General Information
General Information on EC 1.3.1.98 - UDP-N-acetylmuramate dehydrogenase
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evolution
malfunction
metabolism
physiological function
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Verrucomicrobium spinosum possesses a fusion open reading frame annotated by the locus tag (VspiD_010100018130). 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 complement Escherichia coli murB 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
evolution
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Verrucomicrobium spinosum possesses a fusion open reading frame annotated by the locus tag (VspiD_010100018130). 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 complement Escherichia coli murB 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
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cells depleted of either murC or murB expression fail to differentiate heterocysts under normally inducing conditions and display decreased filament integrity
malfunction
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cells depleted of either murC or murB expression fail to differentiate heterocysts under normally inducing conditions and display decreased filament integrity
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MurB is involved in cytoplasmic steps of peptidoglycan biosynthesis the peptidoglycan biosynthesis pathway, overview
metabolism
the enzyme catalyzes the final steps of the UDP-N-acetylmuramic acid formation in the peptidoglycan biosynthesis pathway
metabolism
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MurB is involved in cytoplasmic steps of peptidoglycan biosynthesis the peptidoglycan biosynthesis pathway, overview
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metabolism
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the enzyme catalyzes the final steps of the UDP-N-acetylmuramic acid formation in the peptidoglycan biosynthesis pathway
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the multicellular bacterium Anabaena, which differentiates a periodic pattern of specialized heterocyst cells, requires peptidoglycan synthesis by the murine ligase genes murC (alr5065) and murB (alr5066) for maintenance of patterned gene expression, filament integrity, and overall development. Recombinant expression of gene murB in an MurB enzyme-deficient Escherchia coli mutant can functionally complement the mutant strain. Gene murB depletion does not affect the pattern of patS expression
physiological function
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the multicellular bacterium Anabaena, which differentiates a periodic pattern of specialized heterocyst cells, requires peptidoglycan synthesis by the murine ligase genes murC (alr5065) and murB (alr5066) for maintenance of patterned gene expression, filament integrity, and overall development. Recombinant expression of gene murB in an MurB enzyme-deficient Escherchia coli mutant can functionally complement the mutant strain. Gene murB depletion does not affect the pattern of patS expression
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