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2.4.1.129: peptidoglycan glycosyltransferase

This is an abbreviated version!
For detailed information about peptidoglycan glycosyltransferase, go to the full flat file.

Word Map on EC 2.4.1.129

Reaction

[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
=
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol
 +
undecaprenyl diphosphate

Synonyms

bacterial cell wall glycosyltransferase, bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase, bifunctional penicillin-binding protein, class A penicillin-binding protein, class B penicillin-binding protein, DD-transpeptidase, ftsI, glycosyltransferase, peptidoglycan, glycosyltransferase/acyltransferase penicillin-binding protein 4, GTase, MGT, monofunctional glycosyltransferase, mrcB, MtgA, murein synthase, PBP, PBP 1a, PBP 2b, PBP 2x, PBP 3, PBP-1A, PBP-1B, PBP-1C, PBP-2, PBP1, PBP1a, PBP1b, PBP1c, PBP2, PBP2A, PBP2b, PBP2c, PBP2d, PBP3, PBP4, PBP7, PBP8, PBPA, PenA, penicillin binding protein, penicillin binding protein 1b, penicillin-binding protein, penicillin-binding protein 1a, penicillin-binding protein 1B, penicillin-binding protein 2, penicillin-binding protein 3, peptidoglycan glycosyltransferase, peptidoglycan transglycosylase, PG-II, PGT, SgtB, SpoIID

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.129 peptidoglycan glycosyltransferase

Engineering

Engineering on EC 2.4.1.129 - peptidoglycan glycosyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E83A
mutant with undetectable activity
K124A
mutant shows 5fold reduced activity compared to the wild type enzyme
K137A
mutant with undetectable activity
Q121A
mutant with undetectable activity
R132A
mutant with barely detectable activity (about 3% of wild type)
S116A
mutant shows 10fold reduced activity compared to the wild type enzyme
E78A
-
the mutant shows 89% sporulation efficiency compared to the wild type enzyme
E88A
-
the mutant is severely impaired in sporulation efficiency (0.01% efficiency compared to the wild type enzyme)
E96A
-
the mutant shows wild type sporulation efficiency
H297A
-
the mutant is severely impaired in sporulation efficiency (0.02% efficiency compared to the wild type enzyme)
K99A
-
the mutant shows wild type sporulation efficiency
Q101A
-
the mutant shows 89% sporulation efficiency compared to the wild type enzyme
Q303A
-
the mutant shows 88% sporulation efficiency compared to the wild type enzyme
R106A
-
the mutant is severely impaired in sporulation efficiency (0.05% efficiency compared to the wild type enzyme)
R269A
-
the mutant shows 86% sporulation efficiency compared to the wild type enzyme
S276A
-
the mutant shows 93% sporulation efficiency compared to the wild type enzyme
T164A
-
the mutant shows 73% sporulation efficiency compared to the wild type enzyme
T188A
-
the mutant shows 33% sporulation efficiency compared to the wild type enzyme
Y171A
-
the mutant shows 71% sporulation efficiency compared to the wild type enzyme
Y201A
-
the mutant shows 87% sporulation efficiency compared to the wild type enzyme
Y323A
-
the mutant is severely impaired in sporulation efficiency (0.01% efficiency compared to the wild type enzyme)
Y324A
-
the mutant is severely impaired in sporulation efficiency (0.02% efficiency compared to the wild type enzyme)
Y80A
-
the mutant shows 70% sporulation efficiency compared to the wild type enzyme
D234N
-
the mutant shows 14% of wild type activity
E233Q
E290Q
-
the mutant shows 2% of wild type activity
F237A
G242A
-
the mutant shows 4% of wild type activity
G264L
-
no activity in vitro
H240A
-
mutant with completely abolished activity
H240Q
-
the mutant shows 7% of wild type activity
K274A
-
no activity in vitro
K287A
-
the mutant shows 63% of wild type activity
N312A
-
mutant with completely abolished activity
Q271A
-
no activity in vitro
R372A
-
the mutant shows 19% of wild type activity
S266A
-
the mutant displays 11% of wild type activity
T267A
-
no activity in vitro
Y310F
-
no activity in vitro
N526K
-
the mutant shows decreased susceptibility toward ampicillin and amoxicillin
E100Q
F104A
-
site-directed mutagenesis, the binding response for F104A is drastically decreased compared to the wild-type
F120S
-
site-directed mutagenesis, modification of the residue within the hydrophobic region of enzyme MtgA yields monodisperse forms of the protein with apparently no change in its secondary structure content, but at the expense of the enzyme function. Mutation F120S may affect the outer helix transition/conformational change during catalysis
F150S
-
site-directed mutagenesis, insoluble mutant
F158S
-
site-directed mutagenesis
L112N
-
site-directed mutagenesis
L119N
-
site-directed mutagenesis, modification of the residue within the hydrophobic region of enzyme MtgA yields monodisperse forms of the protein with apparently no change in its secondary structure content, but at the expense of the enzyme function. Mutation L119N may affect the outer helix transition/conformational change during catalysis
L119N/F120S/E100Q
-
structure of MtgA in complex with moenomycin A bound to the donor site, PDB 3HZS
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
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
V154S
-
site-directed mutagenesis
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
G494E
naturally occuring mutation, the mutant cannot be transformed with a DELTApbp2a deletion and shows the small-cell phenotype characteristic of DELTApbp1a mutants, reduced activity compared to wild-type
S89F
naturally occuring mutation, reduced activity compared to wild-type. The mutant can be transformed with a DELTApbp2a deletion. pbp1a(S89F) mutants shows an intermediate size
G494E
-
naturally occuring mutation, the mutant cannot be transformed with a DELTApbp2a deletion and shows the small-cell phenotype characteristic of DELTApbp1a mutants, reduced activity compared to wild-type
-
S89F
-
naturally occuring mutation, reduced activity compared to wild-type. The mutant can be transformed with a DELTApbp2a deletion. pbp1a(S89F) mutants shows an intermediate size
-
additional information