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evolution
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the ORF with the locus tag VspiD_010100018130, encodes the enzymes UDP-N-acetylenolpyruvoylglucosamine reductase (MurB, EC 1.3.1.98) and UDP-N-acetylmuramate:L-alanine ligase (MurC), i.e. MurB/CVs, DNA and amino acid sequence determination and analysis, this fusion enzyme can only be identified in specific lineages within the Verrucomicrobia phylum. Unusual MurB and MurC composition is prevalent in currently sequenced members of Verrucomicrobia
evolution
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the ORF with the locus tag VspiD_010100018130, encodes the enzymes UDP-N-acetylenolpyruvoylglucosamine reductase (MurB, EC 1.3.1.98) and UDP-N-acetylmuramate:L-alanine ligase (MurC), i.e. MurB/CVs, DNA and amino acid sequence determination and analysis, this fusion enzyme can only be identified in specific lineages within the Verrucomicrobia phylum. Unusual MurB and MurC composition is prevalent in currently sequenced members of Verrucomicrobia
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malfunction
mutation of the gene murC impairs heterocyst differentiation in Nostoc sp. PCC 7120. Gene murC depletion leads to aberrant expression of patS in all cells of the filament
malfunction
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UDP-N-acetylmuramic acid L-alanine ligase (MurC) inhibition in a tolC mutant Escherichia coli strain leads to cell death. The mutant strain shows accumulation of the MurC substrate and a decrease in the level of product upon treatment with (2R)-2-((4-[(5-tert-butyl-1-methyl-1H-pyrazol-3-yl)amino]-1H-pyrazolo[3,4-d]pyrimidin-6-yl)amino)-3-cyclohexylpropan-1-ol, indicating inhibition of MurC enzyme in these cells. Overexpression of wild-type MurC in the Escherichia coli tolC mutant leads to an increase in the compound A MIC by over 16fold, establishing a correlation between MurC inhibition and cellular activity
malfunction
Nostoc sp. PCC 7120 = FACHB-418 SAG 25.82 / UTEX 2576
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mutation of the gene murC impairs heterocyst differentiation in Nostoc sp. PCC 7120. Gene murC depletion leads to aberrant expression of patS in all cells of the filament
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metabolism
enzyme MurC catalyzes the third step in peptidoglycan biosynthesis
metabolism
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the enzyme is essentially involved in the bacterial peptidoglycan biosynthesis pathway. MurC, the first of four Mur ligases, ligates L-alanine to UDP-N-acetylmuramic acid, initiating the synthesis of pentapeptide precursor
metabolism
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the enzyme is essentially involved in the bacterial peptidoglycan biosynthesis pathway. MurC, the first of four Mur ligases, ligates L-alanine to UDP-N-acetylmuramic acid, initiating the synthesis of pentapeptide precursor
metabolism
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the enzyme MurB/CVs is involved in the cytoplasmic steps of peptidoglycan biosynthesis catalyzing the second and third step of the pathway, overview
metabolism
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the enzyme MurB/CVs is involved in the cytoplasmic steps of peptidoglycan biosynthesis catalyzing the second and third step of the pathway, overview
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metabolism
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the enzyme is essentially involved in the bacterial peptidoglycan biosynthesis pathway. MurC, the first of four Mur ligases, ligates L-alanine to UDP-N-acetylmuramic acid, initiating the synthesis of pentapeptide precursor
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metabolism
Nostoc sp. PCC 7120 = FACHB-418 SAG 25.82 / UTEX 2576
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enzyme MurC catalyzes the third step in peptidoglycan biosynthesis
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physiological function
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ATP-dependent Mur ligases play essential roles in the biosynthesis of cell wall peptidoglycan as they catalyze the ligation of key amino acid residues to the stem peptide at the expense of ATP hydrolysis
physiological function
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the enzyme is essential for peptidoglycan biosynthesis. Peptidoglycan is an essential cell wall component of both gram-positive and gram-negative bacteria that protects the cytoplasmic membrane from osmotic stress
physiological function
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the enzyme is essential for peptidoglycan biosynthesis. Peptidoglycan is an essential cell wall component of both gram-positive and gram-negative bacteria that protects the cytoplasmic membrane from osmotic stress
physiological function
the enzyme is important in peptidoglycan biosynthesis. Heterocyst development has been shown to require proper peptidoglycan remodeling. Determination of a direct link between peptidoglycan synthesis and the maintenance of a biological pattern in a multicellular organism. Nostoc sp. PCC 7120 differentiates a periodic pattern of specialized heterocyst cells, requiring peptidoglycan synthesis by the murine ligase genes murC (alr5065) and murB (alr5066) for maintenance of patterned gene expression, filament integrity, and overall development, overview
physiological function
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the fusion gene encoding MurB/CVs is able to complement Escherichia coli murB and murC temperature-sensitive mutants
physiological function
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the fusion gene encoding MurB/CVs is able to complement Escherichia coli murB and murC temperature-sensitive mutants
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physiological function
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the enzyme is essential for peptidoglycan biosynthesis. Peptidoglycan is an essential cell wall component of both gram-positive and gram-negative bacteria that protects the cytoplasmic membrane from osmotic stress
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physiological function
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ATP-dependent Mur ligases play essential roles in the biosynthesis of cell wall peptidoglycan as they catalyze the ligation of key amino acid residues to the stem peptide at the expense of ATP hydrolysis
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physiological function
Nostoc sp. PCC 7120 = FACHB-418 SAG 25.82 / UTEX 2576
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the enzyme is important in peptidoglycan biosynthesis. Heterocyst development has been shown to require proper peptidoglycan remodeling. Determination of a direct link between peptidoglycan synthesis and the maintenance of a biological pattern in a multicellular organism. Nostoc sp. PCC 7120 differentiates a periodic pattern of specialized heterocyst cells, requiring peptidoglycan synthesis by the murine ligase genes murC (alr5065) and murB (alr5066) for maintenance of patterned gene expression, filament integrity, and overall development, overview
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additional information
MurC substrate binding site structures and three-dimensional structure modeling by homology modeling method, structure comparisons of Mur ligases, detailed overview. Identification of residues playing an important role in the catalytic activity of each of the Mur enzymes, docking of enzyme and substrate and ATP
additional information
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protein-protein interaction network of MurC, D, E, and F synthetases, overview
additional information
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protein-protein interaction network of MurC, D, E, and F synthetases, overview
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