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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

UDP-N-acetyl-alpha-D-glucosamine
+
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
=
UDP
 +
beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol

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 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.227 undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase

Engineering

Engineering on EC 2.4.1.227 - undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F77E
-
site-directed mutagenesis, the mutant shows unaltered localization and cell growth comared to wild-type. Lipid II synthesis might be totally abrogated in mutant F77E explaining why the mutant is blocked in septation, cell wall synthesis is necessary for engulfment
S67E
-
site-directed mutagenesis, the mutant shows unaltered localization and cell growth comared to wild-type
V74E
-
site-directed mutagenesis, the mutant shows unaltered localization and cell growth comared to wild-type. Lipid II synthesis might be totally abrogated in mutant V74E explaining why the mutant is blocked in septation, cell wall synthesis is necessary for engulfment
V81E
-
site-directed mutagenesis, the mutant shows unaltered localization and cell growth comared to wild-type
E125A
amino acid substitution for evaluation of its role in the active site of MurG
E268A
H124A
amino acid substitution for evaluation of its role in the active site of MurG
H18A
amino acid substitution for evaluation of its role in the active site of MurG
L79E/F82E
-
site-directed mutagenesis, the mutant does not bind anionic phospholipids but can localize to the cell poles
N127A
amino acid substitution for evaluation of its role in the active site of MurG
N134A
amino acid substitution for evaluation of its role in the active site of MurG
N198A
amino acid substitution for evaluation of its role in the active site of MurG
N291A
amino acid substitution for evaluation of its role in the active site of MurG
Q288A
amino acid substitution for evaluation of its role in the active site of MurG
R260A
amino acid substitution for evaluation of its role in the active site of MurG
S191A
amino acid substitution for evaluation of its role in the active site of MurG
T15A
amino acid substitution for evaluation of its role in the active site of MurG
Y105A
amino acid substitution for evaluation of its role in the active site of MurG
additional information
-
none of the point mutations shows lethality and cells expressing MurG-GFP point mutants grow normally in absence of the wild-type murG allele