Information on EC 2.4.1.129 - peptidoglycan glycosyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.129
-
RECOMMENDED NAME
GeneOntology No.
peptidoglycan glycosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[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
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Peptidoglycan biosynthesis
-
-
peptidoglycan biosynthesis II (staphylococci)
-
-
peptidoglycan biosynthesis III (mycobacteria)
-
-
peptidoglycan biosynthesis IV (Enterococcus faecium)
-
-
peptidoglycan biosynthesis V (beta-lactam resistance)
-
-
peptidoglycan maturation (meso-diaminopimelate containing)
-
-
peptidoglycan biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
[poly-N-acetyl-D-glucosaminyl-(1->4)-(N-acetyl-D-muramoylpentapeptide)]-diphosphoundecaprenol:[N-acetyl-D-glucosaminyl-(1->4)-N-acetyl-D-muramoylpentapeptide]-diphosphoundecaprenol disaccharidetransferase
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, click here). Involved in the synthesis of cell-wall peptidoglycan.
CAS REGISTRY NUMBER
COMMENTARY hide
79079-04-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 899
-
-
Manually annotated by BRENDA team
strain 899
-
-
Manually annotated by BRENDA team
strains 16 M and 16 MDELTApbp1C
-
-
Manually annotated by BRENDA team
strain BAS849
-
-
Manually annotated by BRENDA team
strain JA200/pLC19-19
-
-
Manually annotated by BRENDA team
strain ATCC 49247 and beta-lactamase-negative ampicillin-resistant and beta-lactamase-positive amoxicillin-clavulanic acid-resistant strains
-
-
Manually annotated by BRENDA team
strain SM1, synonym M. lysodeikticus
-
-
Manually annotated by BRENDA team
strain SM1, synonym M. lysodeikticus
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
strain NCTC 8325
-
-
Manually annotated by BRENDA team
strain SAK 101
-
-
Manually annotated by BRENDA team
strain R6cwl
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
-
inhibition of the enzyme blocks peptidoglycan synthesis and leads to bacterial lysis and death
metabolism
-
the enzyme also functions as an activity enhancer of SpoIIP which generates its substrate
physiological function
additional information
-
the enzyme contain a conserved hydrophobic surface that mediates its interaction with the cytoplasmic membrane and renders the purified protein polydisperse. Quantitative binding study of the MtgA by surface plasmon resonance
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
undecaprenyl-diphosphoryl-MurNAc-(L-Ala-gamma-D-Glu-meso-(diaminopimelic acid)-D-Ala-D-Ala)-GlcNAc + undecaprenyl-diphosphoryl-MurNAc-(L-Ala-gamma-D-Glu-meso-(diaminopimelic acid)-D-Ala-D-Ala)-GlcNAc
?
show the reaction diagram
-
-
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
show the reaction diagram
[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)-meso-diaminopimelic acid-(L)-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
show the reaction diagram
[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
show the reaction diagram
[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
show the reaction diagram
[phenyl-4(n)-3H]benzylpenicillin
?
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[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
show the reaction diagram
[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
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no divalent cation requirement
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2R)-2-[[(2S)-2-([[(2R,3R,4R,5S,6R)-5-[[(2S,3R,4R,5S,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy]-4-[(1S)-1-carboxyethoxy]-2-[[(hexadecyloxy)(hydroxy)phosphoryl]oxy]-6-(hydroxymethyl)oxan-3-yl]carbamoyl]amino)propanoyl]amino]pentanedioic acid
-
-
-
(2R)-2-[[(2S)-2-[[(2S)-2-[[(2R,3R,4R,5S,6R)-3-acetamido-2-([[(2R)-2-carboxy-2-(hexadecyloxy)ethoxy](hydroxy)phosphoryl]oxy)-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxy]propanoyl]amino]propanoyl]amino]pentanedioic acid
-
-
-
(2R)-2-[[(2S)-2-[[(2S)-2-[[(2R,3R,4R,5S,6R)-3-acetamido-2-[[(hexadecyloxy)(hydroxy)phosphoryl]oxy]-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxy]propanoyl]amino]propanoyl]amino]pentanedioic acid
-
-
-
(2R)-2-[[(2S)-2-[[(2S)-2-[[(2R,3S,4R,5R,6R)-3-[[(2S,3R,4R,5S,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy]-5-(2-carboxyethyl)-6-([[(2R)-2-carboxy-2-(pentadecyloxy)ethoxy](hydroxy)phosphoryl]oxy)-2-(hydroxymethyl)oxan-4-yl]oxy]propanoyl]amino]propanoyl]amino]pentanedioic acid
-
-
-
(2R,3'R)-3-(3-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)propylphosphinato)-2-(3',7'-dimethyloctyloxy)propanoic acid
-
0.1 mM, 25% inhibition, 0.2 mM, 37% inhibition
(2R,3'R)-3-[3-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)propylphosphinato]-2-(3',7'-dimethyloctyloxy)propanoic acid
-
0.1 mM., 25% inhibition, 0.2 mM, 61% inhibition
(3E,7E,14E)-4,9,9,15,19-pentamethyl-12-methylideneicosa-3,7,14,18-tetraen-1-yl (2R)-3-[[[[(2R,3R,4S,5S,6S)-6-carbamoyl-3-[[(2S,3R,4R,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-([[3-(trifluoromethyl)phenyl]carbonyl]amino)tetrahydro-2H-pyran-2-yl]oxy]-5-hydroxy-4-([[4-(trifluoromethoxy)-3-(trifluoromethyl)phenyl]carbamoyl]amino)tetrahydro-2H-pyran-2-yl]oxy](hydroxy)phosphoryl]oxy]-2-hydroxypropanoate
(3Z)-5-(4-bromophenyl)-3-[(5-nitrofuran-2-yl)methylidene]furan-2(3H)-one
(4Z)-2,5-diphenyl-4-[2-(1,3-thiazol-2-yl)hydrazinylidene]-2,4-dihydro-3H-pyrazol-3-one
(R)-3-((2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl)methylphosphinato)-2-octyloxypropanoic acid
-
0.1 mM, 17% inhibition
(R)-3-[3-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl)propylphosphinato]-2-octyloxypropanoic acid
-
0.1 mM, 10% inhibition
(Z)-2-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)oxymethyl-3-tetradecylbutenedioic acid dilithium salt
-
0.1 mM, 28% inhibition
(Z)-2-farnesyl-3-methylbutenedioic acid dilithium salt
-
weak inhibition
(Z)-2-geranyl-3-methylbutenedioic acid dilithium salt
-
0.1 mM, 12% inhibition
(Z)-2-nerolyl-3-methylbutenedioic acid dilithium salt
-
0.1 mM, 17% inhibition
2-(3-(2-carbamimidoylhydrazono)-2-oxoindolin-1-yl)-N-(3-nitrophenyl)acetamide
-
2-(3-(2-carbamimidoylhydrazono)-2-oxoindolin-1-yl)-N-(m-tolyl)acetamide
-
2-acetamido-3-O-[(1S)-1-carboxyethyl]-1-O-[[(2R)-2-carboxy-2-(hexadecyloxy)ethoxy](hydroxy)phosphoryl]-2-deoxy-alpha-D-glucopyranose
-
-
-
2-acetamido-4-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-3-O-[(1S)-1-carboxyethyl]-2-deoxy-1-O-[(hexadecyloxy)(hydroxy)phosphoryl]-alpha-D-glucopyranose
-
-
-
4-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-2-(carboxyamino)-3-O-[(1S)-1-carboxyethyl]-1-O-[[(2R)-2-carboxy-2-(pentadecyloxy)ethoxy](hydroxy)phosphoryl]-2-deoxy-alpha-D-glucopyranose
-
-
-
4-[(1E)-2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen-2-yl)prop-1-en-1-yl]benzoic acid
AC326-alpha
ACL19098
ACL19109
-
ACL19110
ACL19243
ACL19273
ACL19336
ACL19423
-
chaetomellic acid A dilithium salt
-
weak inhibition
chlorobiphenyl desleucyl vancomycin
chlorobiphenyl disaccharide
chlorobiphenyl vancomycin
Dimethylsulfoxide
-
in the presence of 0.05% N-lauroylsarcosine
enramycin
-
-
-
Garneau-5
Macarbomycin
-
mersacidin
-
Moenomycin
moenomycin A
moenomycin disaccharide
moenomycin trisaccharide
neryl-moenomycin A
active site inhibitor
penicillin
Ristocetin
-
-
Sodium 1,2-cyclohexanediamine-N,N,N',N'-tetraacetic acid
-
in the absence of detergents, stimulates in the presence of high concentrations of methanol and detergents
Sodium deoxycholate
-
in the presence of methanol, inhibits at 0.5%
Triton X-100
TS30153
tunicamycin
-
-
Vancomycin
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
benzylpenicillin
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stimulation, in the presence of 15% methanol, not at higher methanol concentrations or in the presence of deoxycholate
deoxycholate
-
-
Dimethylsulfoxide
-
activation, in the absence of methanol, inhibits in the presence of 0.05% sarkosyl
EDTA
-
stimulation in the presence of high concentrations of methanol and detergents
Imipenem
-
stimulation, in the presence of 15% methanol, not at higher methanol concentrations or in the presence of deoxycholate
RodA
-
RodA is required for isoform PBP2 activity
-
Sarkosyl
-
activation
Sodium 1,2-cyclohexanediamine-N,N,N',N'-tetraacetic acid
-
stimulation in the presence of high concentrations of methanol and detergents
Sodium deoxycholate
-
0.05-0.1%, activation
Triton X-100
additional information
-
no activation by cephalexin, nocardicin A or mecillinam
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002
GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
0.002 - 0.008
undecaprenyl-diphosphoryl-MurNAc-(L-Ala-gamma-D-Glu-meso-(diaminopimelic acid)-D-Ala-D-Ala)-GlcNAc
0.0004 - 0.0018
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
0.0183
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
purified wild type enzyme
additional information
additional information
-
turnover-numbers of truncated variants
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0063 - 0.013
undecaprenyl-diphosphoryl-MurNAc-(L-Ala-gamma-D-Glu-meso-(diaminopimelic acid)-D-Ala-D-Ala)-GlcNAc
1.44 - 70
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
3.14
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol
Escherichia coli
-
purified wild type enzyme
additional information
additional information
Escherichia coli
-
turnover-numbers of truncated variants
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.8 - 39
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
3949
174
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol
Escherichia coli
-
purified wild type enzyme
21920
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0098
(3E,7E,14E)-4,9,9,15,19-pentamethyl-12-methylideneicosa-3,7,14,18-tetraen-1-yl (2R)-3-[[[[(2R,3R,4S,5S,6S)-6-carbamoyl-3-[[(2S,3R,4R,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-([[3-(trifluoromethyl)phenyl]carbonyl]amino)tetrahydro-2H-pyran-2-yl]oxy]-5-hydroxy-4-([[4-(trifluoromethoxy)-3-(trifluoromethyl)phenyl]carbamoyl]amino)tetrahydro-2H-pyran-2-yl]oxy](hydroxy)phosphoryl]oxy]-2-hydroxypropanoate
Escherichia coli
-
-
0.034
(3Z)-5-(4-bromophenyl)-3-[(5-nitrofuran-2-yl)methylidene]furan-2(3H)-one
Helicobacter pylori
-
-
0.0037
(4Z)-2,5-diphenyl-4-[2-(1,3-thiazol-2-yl)hydrazinylidene]-2,4-dihydro-3H-pyrazol-3-one
Helicobacter pylori
-
-
0.0093
4-[(1E)-2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen-2-yl)prop-1-en-1-yl]benzoic acid
Helicobacter pylori
-
-
0.0062 - 0.0073
ACL19098
0.0346 - 0.0382
ACL19109
-
0.0365 - 0.0905
ACL19110
0.0497 - 0.0732
ACL19243
0.04 - 0.05
ACL19273
0.0362 - 0.075
ACL19336
0.0497 - 0.0732
ACL19423
-
0.00388
chlorobiphenyl desleucyl vancomycin
0.0015
chlorobiphenyl vancomycin
0.000006 - 0.019
moenomycin A
0.000033
moenomycin disaccharide
0.000016
moenomycin trisaccharide
0.00038 - 0.000685
Vancomycin
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
broad, in the presence of 0.1% deoxycholate
8.5
-
Tris-HCl buffer without deoxycholate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 45
-
about 60% of maximal activity at 20°C and about half-maximal activity at 45°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.6
calculated from amino acid sequence
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isoforms PBP-1A, PBP-1B, and PBP-2
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Atopobium parvulum (strain ATCC 33793 / DSM 20469 / JCM 10300 / VPI 0546)
Atopobium parvulum (strain ATCC 33793 / DSM 20469 / JCM 10300 / VPI 0546)
Atopobium parvulum (strain ATCC 33793 / DSM 20469 / JCM 10300 / VPI 0546)
Atopobium parvulum (strain ATCC 33793 / DSM 20469 / JCM 10300 / VPI 0546)
Atopobium parvulum (strain ATCC 33793 / DSM 20469 / JCM 10300 / VPI 0546)
Atopobium parvulum (strain ATCC 33793 / DSM 20469 / JCM 10300 / VPI 0546)
Atopobium parvulum (strain ATCC 33793 / DSM 20469 / JCM 10300 / VPI 0546)
Atopobium parvulum (strain ATCC 33793 / DSM 20469 / JCM 10300 / VPI 0546)
Atopobium parvulum (strain ATCC 33793 / DSM 20469 / JCM 10300 / VPI 0546)
Burkholderia ambifaria (strain MC40-6)
Eggerthella lenta (strain ATCC 25559 / DSM 2243 / JCM 9979 / NCTC 11813 / VPI 0255)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
-
x * 60000, SDS-PAGE
61000
-
gel filtration
62200
x * 62200, His-tagged enzyme, SDS-PAGE
62856
x * 62856, calculated from amino acid sequence
90000
-
x * 90000, Escherichia coli penicillin binding protein 1B alpha, beta or gamma
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme is prersent as a monomer and as a dimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complex of neryl-moenomycin A bound to the peptidoglycan glycosyltransferase domain of PBP1A
hanging-drop vapor-diffusion method. 2.1 A crystal structure of the peptidoglycan glycosyltransferase domain of PBP1A along with biochemical studies suggest a model for processive glycosyltransfer
-
in complex with moenomycin, sitting drop vapor diffusion method, using 1.2 M sodium formate
-
sitting drop vapor diffusion method, using 100 mM HEPES, pH 7.5, 2 M ammonium sulfate, 20% (v/v) ethylene glycol and 0.28 mM lauryldimethylamine oxide
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 42
-
wild type PBP1b is expressed in stable form at 37°C and 42°C
60
-
up to 87% loss of activity within 10 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, in concentrated PEG 6000 solution, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 isozymes
-
expression of the soluble form of the glycosyltransferase domain of PBP1a in Escherichia coli
Ni2+-affinity column chromatography, gel filtration, and Mono Q ion-exchange chromatography
-
Ni2+-agarose column chromatography
-
Ni2+-NTA agarose column chromatography
Ni2+-Sepharose column chromatography
-
nickel chelation column chromatography and Superdex 200 gel filtration
-
partial
penicillin-binding protein 3
-
recombinant enzyme
recombinant wild-type and mutant enzymes including gel filtration
-
soluble form of Staphylococcus aureus MGT devoid of its membrane anchor, called SauH6-MGT (D68-R268), is expressed in the cytoplasm of Escherichia coli C41 (DE3) strain
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a soluble form of Staphylococcus aureus MGT devoid of its membrane anchor, called SauH6-MGT (D68-R268), is expressed in the cytoplasm of Escherichia coli C41 (DE3) strain
-
activity of PBP1a or PBP1b can be measured in membranes by cloning the PBP into an Escherichia coli ponB::Spcr strain
-
construction of expression plasmids allowing the production of native PBP1B or PBP1B variants with an inactive transpeptidase or transglycosylase domain or both. Overproduction of the inactive PBP1B variants, but not of the active proteins, causes lysis of wild-type cells. Cells became tolerant to lysis by inactive PBP1B at a pH of 5.0
-
enzyme overexpression in Escherichia coli imp mutant strain
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Escherichia coli structural gene mrcB, recloned from plasmid pLC19-19 to high copy number plasmid pBr322, yielding plasmid pTM13
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(lambdaDE3)-RIL cells
expressed in Escherichia coli Rosetta lambdaDE3 cells
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expressed in Escherichia coli Top10 cells
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expression in Escherichia coli
gene mtgA, recombinant expression of wild-type and mutant enzymes
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overexpression and characterization of the glycosyltransferase module of PBP1b. The isolated module can be overexpressed at significantly higher levels than the full-length protein
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PBP4 was not functional in Escherichia coli
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wild type and mutant enzymes are expressed in Escherichia coli BL21(DE3) cells
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ENGINEERING
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
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the mutant shows 89% sporulation efficiency compared to the wild type enzyme
E88A
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the mutant is severely impaired in sporulation efficiency (0.01% efficiency compared to the wild type enzyme)
E96A
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the mutant shows wild type sporulation efficiency
H297A
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the mutant is severely impaired in sporulation efficiency (0.02% efficiency compared to the wild type enzyme)
K99A
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the mutant shows wild type sporulation efficiency
Q101A
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the mutant shows 89% sporulation efficiency compared to the wild type enzyme
Q303A
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the mutant shows 88% sporulation efficiency compared to the wild type enzyme
R106A
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the mutant is severely impaired in sporulation efficiency (0.05% efficiency compared to the wild type enzyme)
R269A
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the mutant shows 86% sporulation efficiency compared to the wild type enzyme
S276A
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the mutant shows 93% sporulation efficiency compared to the wild type enzyme
T164A
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the mutant shows 73% sporulation efficiency compared to the wild type enzyme
T188A
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the mutant shows 33% sporulation efficiency compared to the wild type enzyme
Y171A
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the mutant shows 71% sporulation efficiency compared to the wild type enzyme
Y201A
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the mutant shows 87% sporulation efficiency compared to the wild type enzyme
Y323A
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the mutant is severely impaired in sporulation efficiency (0.01% efficiency compared to the wild type enzyme)
Y324A
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the mutant is severely impaired in sporulation efficiency (0.02% efficiency compared to the wild type enzyme)
Y80A
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the mutant shows 70% sporulation efficiency compared to the wild type enzyme
D234N
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the mutant shows 14% of wild type activity
E290Q
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the mutant shows 2% of wild type activity
F237A
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mutant with completely abolished activity; no activity in vitro
G242A
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the mutant shows 4% of wild type activity
G264L
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no activity in vitro
H240A
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mutant with completely abolished activity
H240Q
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the mutant shows 7% of wild type activity
K274A
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no activity in vitro
K287A
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the mutant shows 63% of wild type activity
N312A
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mutant with completely abolished activity
Q271A
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no activity in vitro
R372A
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the mutant shows 19% of wild type activity
S266A
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the mutant displays 11% of wild type activity
T267A
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no activity in vitro
Y310F
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no activity in vitro
N526K
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the mutant shows decreased susceptibility toward ampicillin and amoxicillin
F104A
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site-directed mutagenesis, the binding response for F104A is drastically decreased compared to the wild-type
F120S
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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
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site-directed mutagenesis, insoluble mutant
F158S
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site-directed mutagenesis
L112N
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site-directed mutagenesis
L119N
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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
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structure of MtgA in complex with moenomycin A bound to the donor site, PDB 3HZS
V154S
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site-directed mutagenesis
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
medicine
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