2.4.1.227: undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase
This is an abbreviated version!
For detailed information about undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase, go to the full flat file.
Reaction
Synonyms
acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-acetylmuramoylpentapeptide pyrophospholipid, gene murG enzyme, gene murG proteins, HyMurG, Lipid I acetylglucosaminyltransferase, MsmegMurG, MurG, MurG glycosyltransferase, MurG transferase, peptidoglycan glycosyltransferase, proteins, gene murG, translocase II, UDP-acetylglucosamine-acetylmuramoylpentapeptide pyrophospholipid acetylglucosaminyltransferase
ECTree
2.4.1.227 undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferaseAdvanced search results
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General Information on EC 2.4.1.227 - undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
drug target
malfunction
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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
metabolism
physiological function
additional information
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
drug target
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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
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metabolism
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glycosyltransferase MurG catalyses the transfer of N-acetyl-D-glucosamine to lipid intermediate I on the bacterial peptidoglycan biosynthesis pathway
metabolism
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MurG is an essential N-acetylglucosaminyl transferase involved in catalyzing the final step of peptidoglycan subunit biosynthesis
metabolism
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the enzyme is an essential bacterial glycosyltransferase that catalyses the GlcNAc-transformation of lipid I to lipid II during peptidoglycan biosynthesis
metabolism
the enzyme is an essential bacterial glycosyltransferase that catalyses the GlcNAc-transformation of lipid I to lipid II during peptidoglycan biosynthesis
metabolism
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the enzyme is an essential bacterial glycosyltransferase that catalyses the GlcNAc-transformation of lipid I to lipid II during peptidoglycan biosynthesis
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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
physiological function
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MurG represents a temporary storage mechanism for excess protein that can later be remobilized into the active pool. Polar MurG can promote polar accumulation of anionic phospholipids
physiological function
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the biochemical production of lipid II requires four components, the lipid carrier undecaprenyl phosphate, UDP-MurNAc-pentapeptide, UDP-GlcNAc and the enzymes catalysing the formation of lipid II from these substrates, MraY and MurG
physiological function
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the biochemical production of lipid II requires four components, the lipid carrier undecaprenyl phosphate, UDP-MurNAc-pentapeptide, UDP-GlcNAc and the enzymes catalysing the formation of lipid II from these substrates, MraY and MurG
physiological function
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the glycosyltransferase MurG is necessary for cell wall synthesis at the spore during sporulation in the bacterium Bacillus subtilis. The enzyme localization is a critical factor in the regulation of proper enzyme function and catalysis
additional information
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docking of transition state analogues into MurG active site, overview
additional information
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
additional information
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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
additional information
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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
additional information
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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
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