Literature summary for 2.4.1.129 extracted from

Dahmane, I.; Montagner, C.; Matagne, A.; Dumbre, S.; Herdewijn, P.; Terrak, M.
Peptidoglycan glycosyltransferase-ligand binding assay based on tryptophan fluorescence quenching (2018), Biochimie, 152, 1-5 .

Search for more literature for 2.4.1.129

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of His-tagged wild-type MtgA and point mutants as well as MtgA (D68-R269) mutant lacking the transmembrane segment in Escherichia coli	Staphylococcus aureus

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of the MtgA (D68-R269) mutant lacking the transmembrane segment	Staphylococcus aureus
N224W	site-directed mutagenesis, the mutant shows the same stability and expression level as the wild-type, the catalytic activity of the mutant is reduced by 95%, the sensitivity to inhibitor moenomycin A is also reduced	Staphylococcus aureus
T244W	site-directed mutagenesis, the mutant shows the same stability and expression level as the wild-type, the catalytic activity of the mutant is reduced by 86%, the sensitivity to inhibitor moenomycin A is also reduced	Staphylococcus aureus
Y181W	site-directed mutagenesis, the mutant shows the same stability and expression level as the wild-type, while the catalytic activity of the mutant is reduced by 78%, the sensitivity to inhibitor moenomycin A is also reduced	Staphylococcus aureus

Inhibitors

Inhibitors	Comment	Organism	Structure
moenomycin A	binding structure, PDB 3HZS	Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol	Staphylococcus aureus	-	[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged wild-type MtgA and MtgA (D68-R269) mutant from Escherichia coli by nickel affinity chromatography in the presence of 0.7% CHAPS	Staphylococcus aureus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the GTase enzyme converts lipid II substrate into glycan chains	Staphylococcus aureus	?	-	-
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol	-	Staphylococcus aureus	[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate	-	?

Synonyms

Synonyms	Comment	Organism
GTase	-	Staphylococcus aureus
MtgA	-	Staphylococcus aureus
peptidoglycan glycosyltransferase	-	Staphylococcus aureus
SgtB	-	Staphylococcus aureus

IC50 Value

IC50 Value	IC50 Value Maximum	Comment	Organism	Inhibitor	Structure
0.000006	-	recombinant wild-type enzyme, pH and temperature not specified in the publication	Staphylococcus aureus	moenomycin A
0.000075	-	recombinant enzyme mutant Y181W, pH and temperature not specified in the publication	Staphylococcus aureus	moenomycin A

General Information

General Information	Comment	Organism
evolution	the enzyme belongs to the peptidoglycan glycosyltransferase family 51	Staphylococcus aureus
additional information	overall fold and active site of wild-type and mutant GTases	Staphylococcus aureus
physiological function	peptidoglycan glycosyltransferases (GTases) of family 51 are essential enzymes for the synthesis of the glycan chains of the bacterial cell wall. Enzyme MtgA converts lipid II substrate into glycan chains	Staphylococcus aureus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)