EC Number   |
General Information |
Reference |
|---|
   2.4.1.227 | drug target |
the enzyme is an important and unique drug target in Acinetobacter baumannii since it plays a key role during the synthesis of peptidoglycan and it is not found in Homo sapiens |
-, 759512 |
| 2.4.1.227 | malfunction |
point mutations in a MurG helical causes severe sporulation defects, but does not affect localization nor cause detectable defects during exponential growth. In strains in which the cardiolipin-synthesizing genes are deleted, MurG levels are diminished at the forespore, but MurG localization during sporulation is rescued by external addition of purified cardiolipin. During sporulation, lack of MurG localization heavily affects engulfment dynamics and sporulation efficiency, indicating a defect in MurG enzymatic activity linked to its diffuse localization |
735983 |
| 2.4.1.227 | metabolism |
glycosyltransferase MurG catalyses the transfer of N-acetyl-D-glucosamine to lipid intermediate I on the bacterial peptidoglycan biosynthesis pathway |
721824 |
| 2.4.1.227 | metabolism |
MurG is an essential N-acetylglucosaminyl transferase involved in catalyzing the final step of peptidoglycan subunit biosynthesis |
722525 |
| 2.4.1.227 | metabolism |
the enzyme is an essential bacterial glycosyltransferase that catalyses the GlcNAc-transformation of lipid I to lipid II during peptidoglycan biosynthesis |
-, 758570 |
| 2.4.1.227 | more |
docking of transition state analogues into MurG active site, overview |
721824 |
| 2.4.1.227 | more |
large-scale conformational change in the relative orientations of the N- and C-terminal domains, which has the effect of widening the cofactor binding site and displacing the UDP-GlcNAc donor |
723716 |
| 2.4.1.227 | more |
MurG becomes polarly localized when expressed at high cellular concentrations, only at levels that saturate MurGs cellular requirement for growth, the polar MurG is not active and polar MurG is dynamic. It can be remobilized when MurG levels drop |
722525 |
| 2.4.1.227 | more |
the active site residue Gln298 plays a critical role in ligand-target interactions, other active site residues like Arg168, Ser198, Arg202, Ser269, and His297 also play roles in binding interactions, docking study, and molecular modeling and structure validation, overview |
-, 723086 |
| 2.4.1.227 | physiological function |
MurG is an essential bacterial glycosyltransferase enzyme in Pseudomonas aeruginosa performing one of the key membrane steps of peptidoglycan synthesis catalyzing the transfer of N-acetyl glucosamine (GlcNAc) from its donor substrate, UDP-GlcNAc, to the acceptor substrate Lipid I |
723716 |
