EC Number   |
General Information |
Reference |
|---|
    6.3.2.8 | evolution |
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 |
-, 744976 |
| 6.3.2.8 | 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 |
-, 745220 |
| 6.3.2.8 | malfunction |
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 |
744050 |
| 6.3.2.8 | metabolism |
enzyme MurC catalyzes the third step in peptidoglycan biosynthesis |
-, 745220 |
| 6.3.2.8 | metabolism |
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 |
-, 743924 |
| 6.3.2.8 | metabolism |
the enzyme MurB/CVs is involved in the cytoplasmic steps of peptidoglycan biosynthesis catalyzing the second and third step of the pathway, overview |
-, 744976 |
| 6.3.2.8 | more |
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 |
715975 |
| 6.3.2.8 | more |
protein-protein interaction network of MurC, D, E, and F synthetases, overview |
-, 728598 |
| 6.3.2.8 | physiological function |
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 |
-, 728598 |
| 6.3.2.8 | physiological function |
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 |
-, 743924 |
