EC Number   |
Natural Substrates |
|---|
    6.3.2.8 | ATP + UDP-N-acetyl-alpha-D-muramate + L-alanine |
- |
| 6.3.2.8 | ATP + UDP-N-acetylmuramate + L-Ala |
adds the first amino acid to the sugar moiety of the peptidoglycan precursor, catalyzing one essential step in cell wall biosynthesis |
| 6.3.2.8 | ATP + UDP-N-acetylmuramate + L-Ala |
formation of a acylphosphate intermediate |
| 6.3.2.8 | ATP + UDP-N-acetylmuramate + L-Ala |
enzyme activity is not in excess in the cell under normal growth conditions, but the amount is adjusted to the requirements of peptidoglycan synthesis |
| 6.3.2.8 | ATP + UDP-N-acetylmuramate + L-alanine |
- |
| 6.3.2.8 | ATP + UDP-N-acetylmuramate + L-alanine |
MurC is essential for peptidoglycan biosynthesis and is responsible of the addition of the first residue L-alanine onto the nucleotide precursor UDP-MurNAc. It is regulated by the serine/threonine protein kinase PknA, overview |
| 6.3.2.8 | more |
regulation by reversible phosphorylation, overview |
| 6.3.2.8 | more |
the Mur ligases constitute a series of four ATP-dependent enzymes, MurC to Mur, that are responsible for the stepwise addition of the pentapeptide side chain onto the D-lactoyl group of the uridine diphosphate-N-acetylmuramic acid initially formed via MurA and MurB, MurC catalyzes the additon of the first amino acid L-alanine. All of the Mur ligases catalyze the formation of an amide or peptide bond through the same reaction mechanism via a tetrahedral intermediate, overview |
