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Information on EC 2.4.1.129 - peptidoglycan glycosyltransferase and Organism(s) Escherichia coli and UniProt Accession P02919
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2.4.1.129 peptidoglycan glycosyltransferaseIUBMB 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, click here). Involved in the synthesis of cell-wall peptidoglycan.
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Word Map
- 2.4.1.129
- staphylococcus
- aureus
- streptococcus
- pneumonia
- beta-lactams
-
methicillin-resistant
- cephalosporin
- methicillin
-
penicillin-resistant
- oxacillin
- ampicillin
-
pneumococci
- cefotaxime
-
penicillin-susceptible
- ceftriaxone
-
ceftaroline
-
methicillin-susceptible
- cefoxitin
-
ampicillin-resistant
- mecillinam
- meropenem
- imipenem
- carbapenems
-
muropeptide
- ceftazidime
- transpeptidases
-
penicillin-sensitive
- cefuroxime
-
e-test
- aztreonam
-
divisome
-
anti-mrsa
- cefixime
- piperacillin
-
sccmec
-
mic90s
-
blnar
- benzylpenicillin
- moenomycin
- cefaclor
- monobactams
- medicine
-
oxacillin-resistant
-
forespore
-
mid-cell
-
beta-lactam-resistant
-
beta-lactamase-negative
- cefsulodin
- drug development
-
cefotaxime-resistant
-
ca-mrsa
-
eucast
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
pbp2a, pbp2b, penicillin binding protein, gtase, penicillin-binding protein 3, penicillin-binding protein 2, pbp 2b, pbp 1a, pbp 2x, spoiid, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
penicillin-binding protein 1B
bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase
-
-
-
-
glycosyltransferase, peptidoglycan
-
-
-
-
PBP1a
PBP1b
PBP1c
penicillin-binding protein 1a
-
the enzyme has both transglycosylase and transpeptidase activity
penicillin-binding protein 1B
penicillin-binding protein 3
-
-
-
-
peptidoglycan transglycosylase
PG-II
-
-
-
-
PBP1b
-
-
-
-
penicillin-binding protein 1B
-
-
-
-
penicillin-binding protein 1B
-
the enzyme has both transglycosylase and transpeptidase activity
peptidoglycan transglycosylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -
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
79079-04-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
-
-
-
?
[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
-
-
-
?
[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
-
-
-
-
?
[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
-
-
-
-
?
[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
[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
-
i.e. lipid II
-
-
?
[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
-
-
-
-
?
[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
-
-
for isoform PBP1B, the limiting length of produced glycan chains is about 50 disaccharide units, whereas it is about 30 disaccharide units for isoform PBP1A
-
?
[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
-
peptidoglycan-synthetic enzyme activities of penicillin-binding protein 3 may by involved in the process of cell division
-
-
?
[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
-
enzyme is involved in synthesis of peptidoglycan
-
-
?
[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
-
PBP1a and PBP1b have both transglycosylase and transpeptidase activity
-
-
?
[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
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the enzyme catalyzes the assembly of lipid-transported N-acetylglucosaminyl-beta-1,4-N-acetylmuramoyl-L-Ala-gamma-D-Glu-meso-(diaminopimelic acid)-D-Ala-D-Ala units (lipid II) into linear peptidoglycan chains. These units are linked, at C1 of N-acetylmuramic acid, to a C55 undecaprenyl diphosphate. In an in vitro assay, lipid II functions both as a glycosyl donor and as a glycosyl acceptor substrate. Using substrate analogues, it is suggested that the specificity of the enzyme for the glycosyl donor substrate differs from that for the acceptor. The donor substrate requires the presence of both N-acetylglucosamine and MurNAc and a reactive group on C1 of the MurNAc and does not absolutely require the lipid chain which can be replaced by uridine. The enzyme appears to prefer an acceptor substrate containing a polyprenyl pyrophosphate on C1 of the MurNAc sugar
-
-
?
additional information
?
-
lipid II, i.e. undecaprenyl-diphosphoryl-MurNAc(pentapeptide)-GlcNAc, is polymerized by the glycosyltransferase reaction, under the release of undecaprenol diphosphate
-
-
?
additional information
?
-
fluorescence enzyme assay optimization and evaluation, detailed overview
-
-
-
additional information
?
-
-
the enzyme shows both transglycosylase and transpeptidase activities
-
-
?
additional information
?
-
-
overproduction of the inactive PBP1B variants causes lysis of wild-type cells
-
-
?
additional information
?
-
-
penicillin-binding protein 1b is the key enzyme responsible for the formation of the polysaccharide backbone of the peptidoglycan as well as for cross-linking of its peptide portion
-
-
?
additional information
?
-
-
dimerized enzyme synthesizes murein with long glycan strands of an average length of more than 25 disaccharide units with almost 50% of the peptides being part of cross-links. PBP1B is also capable of synthesizing trimeric muropeptide structures
-
-
?
additional information
?
-
-
penicillin binding protein 1b has transglycosylase and transpeptidase activity
-
-
?
additional information
?
-
-
the penicillin-binding protein 1B is a bifunctional murein synthase containing both a transpeptidase domain and a transglycosylasedomain, The protein is present in three forms: alpha, beta and gamma
-
-
?
additional information
?
-
-
utility of Lipid II and Lipid IV substrates to probe the mechanism of the enzyme
-
-
?
additional information
?
-
-
while isoform PBP1a is able to convert lipid IV (heptaprenyl-tetrasaccharide) to peptidoglycan in the absence of lipid II, isoform PBP1b does not use lipid IV as substrate unless lipid II is also present
-
-
?
additional information
?
-
-
NMR and mass spectrometric analysis of enzyme-substrate binding
-
-
?
additional information
?
-
-
PGT enzymes contain two substrate binding pockets flanking the enzymatic center. For a PGT enzyme in the process of extending the peptidoglycan chain, lipid II occupies the acceptor site, and the growing chain occupies the donor site and may extend through the enzyme's exit tunnel. Each round of catalysis results in the extension of the peptidoglycan chain by two saccharides and in the release of undecaprenyl diphosphate. Development of glycosyltransferase enzymatic activity and binding assays using the natural products moenomycin and vancomycin as model inhibitors
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
-
-
-
?
[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
[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
-
i.e. lipid II
-
-
?
[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
-
peptidoglycan-synthetic enzyme activities of penicillin-binding protein 3 may by involved in the process of cell division
-
-
?
[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
-
enzyme is involved in synthesis of peptidoglycan
-
-
?
additional information
?
-
lipid II, i.e. undecaprenyl-diphosphoryl-MurNAc(pentapeptide)-GlcNAc, is polymerized by the glycosyltransferase reaction, under the release of undecaprenol diphosphate
-
-
?
additional information
?
-
-
overproduction of the inactive PBP1B variants causes lysis of wild-type cells
-
-
?
additional information
?
-
-
penicillin-binding protein 1b is the key enzyme responsible for the formation of the polysaccharide backbone of the peptidoglycan as well as for cross-linking of its peptide portion
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(E)-2-(1-(2-isobutoxyphenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
-
(E)-2-(1-(4-(3-hydroxypropyl)phenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
-
(E)-2-(1-(4-(ethoxymethyl)phenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
-
(E)-2-(1-(4-(hydroxymethyl)phenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
-
(E)-2-(1-(4-(methoxymethoxy)phenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
-
(E)-2-(1-(4-(methoxymethyl)phenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
-
(E)-2-(1-(4-(sec-butyl)phenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
-
(E)-2-(1-(4-(tert-butoxymethyl)phenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
-
(E)-2-(1-(4-butylphenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
binding structure, modeling
(E)-2-(1-(4-ethoxyphenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
-
(E)-2-(1-(4-ethylphenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
-
(E)-2-(1-(4-hexylphenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
-
(E)-2-(1-(4-hydroxyphenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
-
(E)-2-(1-(4-octylphenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
-
(E)-2-(1-(naphthalen-1-yl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
-
(E)-2-(1-(naphthalen-2-yl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
-
(E)-2-(3-(2-carbamimidoylhydrazineylidene)-2-oxoindolin-1-yl)-N-(3-(trifluoromethyl)phenyl)acetamide
-
(E)-2-(3-(2-carbamimidoylhydrazineylidene)-2-oxoindolin-1-yl)-N-(3-ethylphenyl)acetamide
-
(E)-2-(3-(2-carbamimidoylhydrazineylidene)-2-oxoindolin-1-yl)-N-(naphthalen-2-yl)acetamide
-
(E)-2-(3-(2-carbamimidoylhydrazineylidene)-5-methyl-2-oxoindolin-1-yl)-N-(3-nitrophenyl)acetamide
-
(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-geranyl-3-methylbutenedioic acid dilithium salt
-
0.1 mM, 12% inhibition
(Z)-2-nerolyl-3-methylbutenedioic acid dilithium salt
-
0.1 mM, 17% inhibition
4-[(1E)-2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen-2-yl)prop-1-en-1-yl]benzoic acid
-
-
4-[3-amino-3-([1,1'-biphenyl]-4-yl)propanamido]-1,5-anhydro-2,4-dideoxy-3-O-[2-deoxy-2-({[3-(trifluoromethyl)phenyl]carbamoyl}amino)-beta-D-glucopyranosyl]-2-({[3-(trifluoromethyl)phenyl]carbamoyl}amino)-D-galactitol
-
-
EDTA
-
in the absence of detergents, stimulates in the presence of high concentrations of methanol and detergents
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
moenomycin A
-
moenomycins are phosphoglycolipid antibiotics that directly bind to PGT enzymes. Moenomycins are produced by certain Streptomyces species as a complex of related compounds in which moenomycin A is the major form
additional information
hydrophobic substituents on isatin derivatives enhance their inhibition against bacterial peptidoglycan glycosyltransferase activity. 20 amphiphilic compounds are systematically designed and the relationship between molecular hydrophobicity and the antibacterial activity by targeting at PGT is demonstrated, inhibitor synthesis, antimicrobial activity and MIC values, and structure-activity relationships, overview. Docking study and molecular modeling using the structure of Escherichia coli PBP1b, PBP ID 3VMA, as template. Diffusion to the PGT target is hindered by the inefficiency to pass through the periplasmic region of the Gram-negative bacteria
-
additional information
-
hydrophobic substituents on isatin derivatives enhance their inhibition against bacterial peptidoglycan glycosyltransferase activity. 20 amphiphilic compounds are systematically designed and the relationship between molecular hydrophobicity and the antibacterial activity by targeting at PGT is demonstrated, inhibitor synthesis, antimicrobial activity and MIC values, and structure-activity relationships, overview. Docking study and molecular modeling using the structure of Escherichia coli PBP1b, PBP ID 3VMA, as template. Diffusion to the PGT target is hindered by the inefficiency to pass through the periplasmic region of the Gram-negative bacteria
-
additional information
inhibitory effect of high detergent concentration on the enzyme activity. 25% Dimethylsulfoxide (DMSO) abrogates this detergent effect
-
additional information
-
molecular docking and modelling study using the structure of PBP1b, PDB ID 3VMA. NMR and mass spectrometric analysis of enzyme-inhibitor binding
-
additional information
-
PGT enzymes can be inhibited directly by compounds binding to the enzyme and indirectly by compounds binding to the lipid II substrate. Development of glycosyltransferase enzymatic activity and binding assays using the natural products moenomycin and vancomycin as model inhibitors. Design of a library of disaccharide compounds based on the minimum moenomycin fragment with peptidoglycan glycosyltransferase inhibitory activity and based on a more drug-like and synthetically versatile disaccharide building block. A subset of these disaccharide compounds bind and inhibit the glycosyltransferase enzyme. Inhibitor-enzyme binding structure analysis by 1H NMR spectral data and using crystal structure PDB ID 3VMA. MIC values with strain imp mutant BAS849
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DMSO
20% DMSO has a positive effect on the GTase rate of PBP1B, particularly at the higher Triton X-100 concentration of 0.2%. At higher Triton X-100 concentration in the presence of 20% DMSO the stimulation of PBP1B by LpoB is only 1.6fold
benzylpenicillin
-
stimulation, in the presence of 15% methanol, not at higher methanol concentrations or in the presence of 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
Sodium 1,2-cyclohexanediamine-N,N,N',N'-tetraacetic acid
-
stimulation in the presence of high concentrations of methanol and detergents
additional information
-
no activation by cephalexin, nocardicin A or mecillinam
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0183
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol
purified wild type enzyme
0.002
GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
lipid II, pH 7.5, 25°C
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
additional information
additional information
-
turnover-numbers of truncated variants
-
0.0004
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme E290Q
0.0011
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme R372A
0.0012
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme K287A
0.0012
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme N312A
0.0012
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme S266A
0.0016
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme G242A
0.00168
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme D234N
0.0018
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme H240Q
0.0018
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
wild type enzyme PBP1b
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.14
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol
purified wild type enzyme
1.44 - 70
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
additional information
additional information
-
turnover-numbers of truncated variants
-
1.44
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme E290Q
2.9
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme G242A
5.2
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme H240Q
7.6
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme S266A
9.4
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme D234N
11
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme N312A
13.4
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme R372A
44
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme K287A
70
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
wild type enzyme PBP1b
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
174
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol
purified wild type enzyme
1.8 - 39
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
1.8
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme G242A
3.6
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme E290Q
4.7
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme H240Q
5.6
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme D234N
6.3
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme S266A
9.2
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme N312A
12.2
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme R372A
36.5
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
mutant enzyme K287A
39
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol
-
wild type enzyme PBP1b
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.156
(E)-2-(1-(4-(methoxymethyl)phenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
Escherichia coli
pH and temperature not specified in the publication, recombinant enzyme
0.0828
(E)-2-(1-(4-butylphenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
Escherichia coli
pH and temperature not specified in the publication, recombinant enzyme
0.203
(E)-2-(1-(4-ethoxyphenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
Escherichia coli
pH and temperature not specified in the publication, recombinant enzyme
0.125
(E)-2-(1-(4-ethylphenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
Escherichia coli
pH and temperature not specified in the publication, recombinant enzyme
0.0124
(E)-2-(1-(4-octylphenyl)-2-oxoindolin-3-ylidene)hydrazine-1-carboximidamide
Escherichia coli
pH and temperature not specified in the publication, recombinant enzyme
0.00101
Vancomycin
Escherichia coli
pH and temperature not specified in the publication, recombinant enzyme
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
-
-
0.0497
4-[3-amino-3-([1,1'-biphenyl]-4-yl)propanamido]-1,5-anhydro-2,4-dideoxy-3-O-[2-deoxy-2-({[3-(trifluoromethyl)phenyl]carbamoyl}amino)-beta-D-glucopyranosyl]-2-({[3-(trifluoromethyl)phenyl]carbamoyl}amino)-D-galactitol
Escherichia coli
-
pH 7.5, 25°C, PBP1b
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 45
-
about 60% of maximal activity at 20°C and about half-maximal activity at 45°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the PGT domain of penicillin-binding protein is anchored on the outer surface of the bacterial cell membrane by a transmembrane helix
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
evolution
physiological function
physiological function
the enzyme is involved in synthesis of peptidoglycan, a key cell wall component in nearly all bacteria, protecting the cell from bursting by its internal turgor and maintaining cell shape. Peptidoglycan consists of glycan strands connected by short peptides and forms a continuous, mesh-like structure around the cytoplasmic membrane, called the sacculus. In Gram-negative species, such as Escherichia coli, the sacculus is made of a mainly single layer of peptidoglycan with a thickness of 3-6 nm. The glycan strands are made of alternating N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc) residues linked by beta-1,4 glyosidic bonds. The peptides contain L- and D-amino acids and are linked to MurNAc residues. The sequence is L-Ala-D-iGlu-m-Dap-D-Ala-D-Ala (m-Dap, meso-diaminopimelic acid). During cell growth and division, the surface of the sacculus is enlarged by the incorporation of new peptidoglycan material. In this process, the precursor lipid II (undecaprenyl-diphosphoryl-MurNAc(pentapeptide)-GlcNAc) is polymerized by the glycosyltransferase reaction of the GTase domain of enzyme PBP1B
physiological function
peptidoglycan glycosyltransferase (PGT) transfers the disaccharide-peptide of lipid II to the growing glycan chain in bacterial cell wall synthesis
physiological function
the majority of bacteria surround their cytoplasmic membrane with a peptidoglycan sacculus, a continuous layer that is required to maintain cell shape and osmotic stability. The basic chemical structure of peptidoglycan is well known, glycan strands consisting of alternating N -acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc) residues connected by short stem peptides protruding from MurNAc. Peptides of neighboring glycan strands may be connected (i.e. cross-linked) forming a net-like layer. Peptide cross-links are formed by DD-transpeptidases. DD-transpeptidases covalently bind beta-lactam antibiotics such as penicillin, and are hence named penicillin-binding proteins (PBPs). Most bacteria possess several peptidoglycan synthases capable of catalyzing the glycosyltransferase (GTase) and/or transpeptidase (TPase) reactions. The Gram negative model organism Escherichia coli has three enzymes capable of performing both reactions, so-called bifunctional synthases: PBP1A, PBP1B, and PBP1C, two monofunctional transpeptidases, PBP2 and PBP3, and the monofunctional glycosyltransferase MtgA. The main peptidoglycan synthesis activity in the cell is provided by the semi-redundant PBP1A and PBP1B in consort with the transpeptidases PBP2 and PBP3, latter have essential roles in cell elongation and division, respectively. PBP1C and MtgA are dispensable for growth
evolution
-
proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs
evolution
-
proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs. Both forms contain a single transmembrane span at the N-terminus followed by the glycosyltransferase domain. In the class A PBPs, the C-terminus contains the transpeptidase domain. Bacterial species typically have multiple forms of these enzymes. Escherichia coli has 3 class A PBPs (PBP1a, PBP1b, and PBP1c) and 2 MGT proteins
physiological function
-
isoform PBP3 is required for localization of MurG to division site
physiological function
-
MtgA localizes at the division site of Escherichia coli cells that are deficient in PBP1b and produce a thermosensitive PBP1a and is able to interact with three constituents of the divisome, PBP3, FtsW, and FtsN in peptidoglycan assembly during the cell cycle
physiological function
-
synthesis of bacterial cell wall requires the concerted action of peptidoglycan glycosyltransferases (PGT, also known as peptidoglycan transglycosylases) and transpeptidases. The PGT enzymes transfer the disaccharide-peptide from the lipid II substrate onto the growing glycan chain allowing TP enzymes to crosslink peptides from adjacent chains. The lipid II substrate is anchored into the cell membrane through an undecaprenyl (C55) tail. Each round of catalysis results in the extension of the peptidoglycan chain by two saccharides and in the release of undecaprenyl diphosphate (C55PP)
physiological function
-
the PGT enzymes transfer the disaccharide-peptide from the lipid II substrate onto the growing glycan chain allowing transpeptidase enzymes to crosslink peptides from adjacent chains. The lipid II substrate is anchored into the cell membrane through an undecaprenyl (C55) tail. The enzymatic reaction is thought to occur at the surface of the membrane
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90000
-
x * 90000, Escherichia coli penicillin binding protein 1B alpha, beta or gamma
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 90000, Escherichia coli penicillin binding protein 1B alpha, beta or gamma
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with moenomycin, sitting drop vapor diffusion method, using 1.2 M sodium formate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E233Q
F237A
additional information
-
ponA is synthesized with the addition of ribosome binding site (AGGAGGT) and linker (AAAACAT) upstream of the Met1 codon. This construct is inserted at the XbaI and HindIII sites of pACT3 (21), generating pMCC1, with PBP1a expression under control of the tac promoter. pMCC1 and pACT3 are transformed into hyperpermeable Escherichia coli isolate generating CBS-3546 and CBS-3567, respectively
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
organic solvent DMSO is a component of in vitro peptidoglycan synthesis assays making use of its ability to solubilize the lipid II substrate without denaturing enzymes. DMSO at high concentration can potentially affect protein stability and protein-protein interactions. The presence of 20% DMSO severely impairs the interaction of PBP1B with LpoB. In contrast, at lower concentration of Triton X-100 (between 0.02% and 0.08%) the activity of PBP1B can be robustly assayed and its interactions with LpoB, CpoB, TolA and FtsN are maintained. Inhibitory effect of high detergent concentration on the enzyme activity. 25% Dimethylsulfoxide (DMSO) abrogates this detergent effect
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene mrcB, recombinant His-tagged PBP1B from Escherichia coli strain BL21 pDML924 membrane fraction by ultracentrifugation, nickel affinity chromatography, dialysis, and tag cleavage by thrombin, followed by dialysis, cation exchange chromatography and again diaylsis, method overview
nickel chelation column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene mrcB, recombinant expression of His6-tagged PBP1b (residues 58-604) in Escherichia coli
overexpression of His-tagged enzyme in Escherichia coli strain BL21 pDML924
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
-
Escherichia coli structural gene mrcB, recloned from plasmid pLC19-19 to high copy number plasmid pBr322, yielding plasmid pTM13
-
overexpression and characterization of the glycosyltransferase module of PBP1b. The isolated module can be overexpressed at significantly higher levels than the full-length protein
-
wild type and mutant enzymes are expressed in Escherichia coli BL21(DE3) cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
peptidoglycan glycosyltransferase (PGT) is regarded as a potential drug target for development of antibiotics
medicine
-
PGT activity can be a useful target for antibiotic therapies because the enzymatic site of the enzyme is highly conserved and inhibition of PGT activity results in the inhibition of bacterial growth
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ishino, F.; Matsuhashi, M.
Peptidoglycan synthetic enzyme activities of highly purified penicillin-binding protein 3 in Escherichia coli: a septum-forming reaction sequence
Biochem. Biophys. Res. Commun.
101
905-911
1981
Escherichia coli
Nakagawa, J.; Tamaki, S.; Tomioka, S.; Matsuhashi, M.
Functional biosynthesis of cell wall peptidoglycan by polymorphic bifunctional polypeptides. Penicillin-binding protein 1Bs of Escherichia coli with activities of transglycosylase and transpeptidase
J. Biol. Chem.
259
13937-13946
1984
Escherichia coli, Escherichia coli JA200/pLC19-19
Park, W.; Seto, H.; Hakenbeck, R.; Matsuhashi, M.
Major peptidoglycan transglycosylase activity in Streptococcus pneumoniae that is not a penicillin-binding protein
FEMS Microbiol. Lett.
27
45-48
1985
Streptococcus pneumoniae, Escherichia coli, Streptococcus pneumoniae R6cwl
-
Van Heijenoort, J.
Formation of the glycan chains in the synthesis of bacterial peptidoglycan
Glycobiology
11
25R-36R
2001
Streptococcus pneumoniae, Escherichia coli
Chandrakala, B.; Shandil, R.K.; Mehra, U.; Ravishankar, S.; Kaur, P.; Usha, V.; Joe, B.; deSousa, S.M.
High-throughput screen for inhibitors of transglycosylase and/or transpeptidase activities of Escherichia coli penicillin binding protein 1b
Antimicrob. Agents Chemother.
48
30-40
2004
Escherichia coli
Barrett, D.S.; Chen, L.; Litterman, N.K.; Walker, S.
Expression and characterization of the isolated glycosyltransferase module of Escherichia coli PBP1b
Biochemistry
43
12375-12381
2004
Escherichia coli
Garneau, S.; Qiao, L.; Chen, L.; Walker, S.; Vederas, J.C.
Synthesis of mono- and disaccharide analogs of moenomycin and lipid II for inhibition of transglycosylase activity of penicillin-binding protein 1b
Bioorg. Med. Chem.
12
6473-6494
2004
Escherichia coli
Meisel, U.; Holtje, J.V.; Vollmer, W.
Overproduction of inactive variants of the murein synthase PBP1B causes lysis in Escherichia coli
J. Bacteriol.
185
5342-5348
2003
Escherichia coli
Bertsche, U.; Breukink, E.; Kast, T.; Vollmer, W.
In vitro murein (peptidoglycan) synthesis by dimers of the bifunctional transglycosylase-transpeptidase PBP1B from Escherichia coli
J. Biol. Chem.
280
38096-38101
2005
Escherichia coli
Terrak, M.; Ghosh, T.G.; van Heijenoort, J.; et al.
The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli
Mol. Microbiol.
34
350-364
1999
Escherichia coli
Ramachandran, V.; Chandrakala, B.; Kumar, V.P.; Usha, V.; Solapure, S.M.; de Sousa, S.M.
Screen for inhibitors of the coupled transglycosylase-transpeptidase of peptidoglycan biosynthesis in Escherichia coli
Antimicrob. Agents Chemother.
50
1425-1432
2006
Escherichia coli
Fraipont, C.; Sapunaric, F.; Zervosen, A.; Auger, G.; Devreese, B.; Lioux, T.; Blanot, D.; Mengin-Lecreulx, D.; Herdewijn, P.; van Beeumen, J.; Frere, J.M.; Nguyen-Disteche, M.
Glycosyl transferase activity of the Escherichia coli penicillin-binding protein 1b: specificity profile for the substrate
Biochemistry
45
4007-4013
2006
Escherichia coli
Zhang, Y.; Fechter, E.J.; Wang, T.A.; Barrett, D.; Walker, S.; Kahne, D.E.
Synthesis of heptaprenyl-lipid IV to analyze peptidoglycan glycosyltransferases
J. Am. Chem. Soc.
129
3080-3081
2007
Escherichia coli
Terrak, M.
Peptidoglycan glycosyltransferase inhibition: New perspectives for an old target
Anti-Infect. Agents Med. Chem.
7
180-192
2008
Aquifex aeolicus, Escherichia coli, Enterococcus faecalis, Helicobacter pylori, Staphylococcus aureus, Escherichia coli BAS849
-
Lovering, A.L.; Gretes, M.; Strynadka, N.C.
Structural details of the glycosyltransferase step of peptidoglycan assembly
Curr. Opin. Struct. Biol.
18
534-543
2008
Aquifex aeolicus, Bacillus subtilis, Caulobacter vibrioides, Escherichia coli, Staphylococcus aureus, Mycobacterium tuberculosis, Cereibacter sphaeroides
Wang, T.S.; Manning, S.A.; Walker, S.; Kahne, D.
Isolated peptidoglycan glycosyltransferases from different organisms produce different glycan chain lengths
J. Am. Chem. Soc.
130
14068-14069
2008
Escherichia coli, Enterococcus faecalis, Staphylococcus aureus
Derouaux, A.; Wolf, B.; Fraipont, C.; Breukink, E.; Nguyen-Disteche, M.; Terrak, M.
The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with penicillin-binding protein 3, FtsW, and FtsN
J. Bacteriol.
190
1831-1834
2008
Escherichia coli
Terrak, M.; Sauvage, E.; Derouaux, A.; Dehareng, D.; Bouhss, A.; Breukink, E.; Jeanjean, S.; Nguyen-Disteche, M.
Importance of the conserved residues in the peptidoglycan glycosyltransferase module of the class A penicillin-binding protein 1b of Escherichia coli
J. Biol. Chem.
283
28464-28470
2008
Escherichia coli
Sung, M.T.; Lai, Y.T.; Huang, C.Y.; Chou, L.Y.; Shih, H.W.; Cheng, W.C.; Wong, C.H.; Ma, C.
Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli
Proc. Natl. Acad. Sci. USA
106
8824-8829
2009
Escherichia coli (P02919)
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