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Information on EC 2.4.1.227 - undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9HW01

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IUBMB Comments
The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, {iupac/misc/prenol#p6::click here}).
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This record set is specific for:
Pseudomonas aeruginosa
UNIPROT: Q9HW01
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
translocase ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-acetylmuramoylpentapeptide pyrophospholipid
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gene murG enzyme
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gene murG proteins
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Lipid I acetylglucosaminyltransferase
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MurG
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MurG glycosyltransferase
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MurG transferase
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proteins, gene murG
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UDP-acetylglucosamine-acetylmuramoylpentapeptide pyrophospholipid acetylglucosaminyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
transfer of alpha-N-acetylglucosamine
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:N-acetyl-alpha-D-muramyl(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol 4-beta-N-acetylglucosaminlytransferase
The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, {iupac/misc/prenol#p6::click here}).
CAS REGISTRY NUMBER
COMMENTARY hide
60976-26-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
structure comparison with the MurG enzyme from Escherichia coli, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complex of MurG with UDP-GlcNAc, X-ray diffraction structure determination and analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brown, K.; Vial, S.C.; Dedi, N.; Westcott, J.; Scally, S.; Bugg, T.D.; Charlton, P.A.; Cheetham, G.M.
Crystal structure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex
Protein Pept. Lett.
20
1002-1008
2013
Pseudomonas aeruginosa (Q9HW01)
Manually annotated by BRENDA team