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Information on EC 2.4.1.129 - peptidoglycan glycosyltransferase
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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
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methicillin-resistant
- methicillin
- cephalosporin
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penicillin-resistant
- oxacillin
- ampicillin
- cefotaxime
-
pneumococci
- ceftriaxone
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penicillin-susceptible
- cefoxitin
- imipenem
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ceftaroline
-
methicillin-susceptible
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ampicillin-resistant
- carbapenems
- meropenem
- mecillinam
- piperacillin
- transpeptidases
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e-test
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sccmec
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mic90s
-
divisome
-
blnar
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penicillin-sensitive
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anti-mrsa
- moenomycin
- cefixime
- aztreonam
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muropeptide
- cefuroxime
- benzylpenicillin
- ceftazidime
-
oxacillin-resistant
-
beta-lactamase-negative
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beta-lactam-resistant
- cefsulodin
- drug development
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eucast
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mid-cell
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ca-mrsa
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forespore
- cefaclor
- monobactams
- medicine
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cefotaxime-resistant
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bacterial cell wall glycosyltransferase
bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase
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bifunctional penicillin-binding protein
class A penicillin-binding protein
class B penicillin-binding protein
glycosyltransferase, peptidoglycan
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GTase
MGT
monofunctional glycosyltransferase
MtgA
PBP
PBP 3
PBP-1B
PBP1a
PBP1b
PBP1c
PBP2
PBP2A
PBP2b
PBP3
PBP4
PenA
penicillin-binding protein
penicillin-binding protein 1a
penicillin-binding protein 1B
penicillin-binding protein 2
penicillin-binding protein 3
peptidoglycan transglycosylase
PG-II
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PGT
SgtB
PBP1b
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penicillin-binding protein 1a
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the enzyme has both transglycosylase and transpeptidase activity
penicillin-binding protein 1B
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penicillin-binding protein 1B
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the enzyme has both transglycosylase and transpeptidase activity
penicillin-binding protein 2
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bifunctional peptidoglycan glycosyltransferase/transpeptidase
penicillin-binding protein 2
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bifunctional peptidoglycan glycosyltransferase/transpeptidase
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penicillin-binding protein 3
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peptidoglycan transglycosylase
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REACTION
REACTION DIAGRAM
COMMENTARY
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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.
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CAS REGISTRY NUMBER
COMMENTARY
79079-04-2
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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
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
?
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?
[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
[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
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?
[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
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?
[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
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?
[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
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?
[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
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?
[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
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?
[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
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?
[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
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?
[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
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?
[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
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?
[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
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?
[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
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?
[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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?
[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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?
[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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?
[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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?
[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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?
[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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for isoform PBP2A, the limiting length of produced glycan chains is about 15 disaccharide units
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?
[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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?
[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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?
[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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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
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?
[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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peptidoglycan-synthetic enzyme activities of penicillin-binding protein 3 may by involved in the process of cell division
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?
[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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enzyme is involved in synthesis of peptidoglycan
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?
[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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PBP1a and PBP1b have both transglycosylase and transpeptidase activity
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?
[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
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?
[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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?
[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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PBP4 is dispensable and that, as in other bacteria, its absence can be compensated for by the second class A PBP, PBP1
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-
?
[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
-
glycosyltransferase activity catalyzes glycan chain elongation from lipid II substrate undecaprenyl-pyrophosphoryl-N-acetylglucosamine-N-acetylmuramic acid-pentapeptide. PBP4 also catalyzes the aminolysis (D-Ala as acceptor) and hydrolysis of the thiolester donor substrate benzoyl-Gly-thioglycolate, indicating that PBP4 possesses both transpeptidase and carboxypeptidase activities
-
-
?
[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
-
gram-positive cocci have cell wall peptidoglycan which seems to be synthesized by penicillin-binding protein transpeptidases and a separate transglycosylase
-
-
?
[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
-
gram-positive cocci have cell wall peptidoglycan which seems to be synthesized by penicillin-binding protein transpeptidases and a separate transglycosylase
-
-
?
[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
-
enzyme synthesizes lysozyme-sensitive peptidoglycan from undecaprenyldiphosphoryl-disaccharide-pentapeptide
-
-
?
[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 synthesizes lysozyme-sensitive peptidoglycan from undecaprenyldiphosphoryl-disaccharide-pentapeptide
-
-
?
[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 PBP2, the limiting length of produced glycan chains is about 15 disaccharide units
-
?
[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
-
gram-positive cocci have cell wall peptidoglycan which seems to be synthesized by penicillin-binding protein transpeptidases and a separate transglycosylase
-
-
?
[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
-
gram-positive cocci have cell wall peptidoglycan which seems to be synthesized by penicillin-binding protein transpeptidases and a separate transglycosylase
-
-
?
[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
-
-
-
?
[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
-
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
-
-
-
?
[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
-
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
-
-
-
?
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
?
-
-
the enzyme is both an amidase and an endopeptidase. The enzyme is a lytic transglycosylase that degrades the glycan strands of the peptidoglycan into disaccharide units. The enzyme binds the cell wall, but only cleaves the glycan strands after the stem peptides have been removed. The enzyme alone is unable to cleave purified peptidoglycan but needs the presence of SpoIIP
-
-
?
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
?
-
-
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
?
-
lipid II, i.e. undecaprenyl-diphosphoryl-MurNAc(pentapeptide)-GlcNAc, is polymerized by the glycosyltransferase reaction, under the release of undecaprenol diphosphate
-
-
?
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
-
-
?
additional information
?
-
fluorescence enzyme assay optimization and evaluation, detailed overview
-
-
-
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
-
-
?
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
?
-
-
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
?
-
-
development of glycosyltransferase enzymatic activity and binding assays using the natural products moenomycin and vancomycin as model inhibitors
-
-
?
additional information
?
-
-
NMR and mass spectrometric analysis of enzyme-substrate binding
-
-
?
additional information
?
-
-
positive cooperativity between acceptor and donor sites of the peptidoglycan glycosyltransferase, mechanism of interaction with substrates, overview. At low concentrations the disaccharide compounds bind selectively to the acceptor site and increase the affinity of the donor site to moenomycin A by heteroallosteric activation leading to an increased MtgA binding response
-
-
?
additional information
?
-
-
the GTase enzyme converts lipid II substrate into glycan chains
-
-
-
additional information
?
-
-
development of glycosyltransferase enzymatic activity and binding assays using the natural products moenomycin and vancomycin as model inhibitors
-
-
?
additional information
?
-
-
NMR and mass spectrometric analysis of enzyme-substrate binding
-
-
?
additional information
?
-
-
the enzyme possesses peptidoglycan transglycosylase activity that lacks penicillin-binding activity
-
-
?
additional information
?
-
-
the enzyme possesses peptidoglycan transglycosylase activity that lacks penicillin-binding activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
-
?
[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
-
PBP4 is dispensable and that, as in other bacteria, its absence can be compensated for by the second class A PBP, PBP1
-
-
?
[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
-
gram-positive cocci have cell wall peptidoglycan which seems to be synthesized by penicillin-binding protein transpeptidases and a separate transglycosylase
-
-
?
[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
-
gram-positive cocci have cell wall peptidoglycan which seems to be synthesized by penicillin-binding protein transpeptidases and a separate transglycosylase
-
-
?
[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
-
gram-positive cocci have cell wall peptidoglycan which seems to be synthesized by penicillin-binding protein transpeptidases and a separate transglycosylase
-
-
?
[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
-
gram-positive cocci have cell wall peptidoglycan which seems to be synthesized by penicillin-binding protein transpeptidases and a separate transglycosylase
-
-
?
[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
-
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
-
-
-
?
[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
-
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
-
-
-
?
additional information
?
-
-
the enzyme is both an amidase and an endopeptidase. The enzyme is a lytic transglycosylase that degrades the glycan strands of the peptidoglycan into disaccharide units. The enzyme binds the cell wall, but only cleaves the glycan strands after the stem peptides have been removed. The enzyme alone is unable to cleave purified peptidoglycan but needs the presence of SpoIIP
-
-
?
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
?
-
lipid II, i.e. undecaprenyl-diphosphoryl-MurNAc(pentapeptide)-GlcNAc, is polymerized by the glycosyltransferase reaction, under the release of undecaprenol diphosphate
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
(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
-
(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
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
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
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
(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
-
-
(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
-
-
(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
-
-
(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
-
-
(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
-
-
(3Z)-5-(4-bromophenyl)-3-[(5-nitrofuran-2-yl)methylidene]furan-2(3H)-one
-
-
(3Z)-5-(4-bromophenyl)-3-[(5-nitrofuran-2-yl)methylidene]furan-2(3H)-one
-
-
(3Z)-5-(4-bromophenyl)-3-[(5-nitrofuran-2-yl)methylidene]furan-2(3H)-one
-
-
(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
-
-
(4Z)-2,5-diphenyl-4-[2-(1,3-thiazol-2-yl)hydrazinylidene]-2,4-dihydro-3H-pyrazol-3-one
-
-
(4Z)-2,5-diphenyl-4-[2-(1,3-thiazol-2-yl)hydrazinylidene]-2,4-dihydro-3H-pyrazol-3-one
-
-
(4Z)-2,5-diphenyl-4-[2-(1,3-thiazol-2-yl)hydrazinylidene]-2,4-dihydro-3H-pyrazol-3-one
-
-
(4Z)-2,5-diphenyl-4-[2-(1,3-thiazol-2-yl)hydrazinylidene]-2,4-dihydro-3H-pyrazol-3-one
-
-
2-(3-(2-carbamimidoylhydrazono)-2-oxoindolin-1-yl)-N-(3-nitrophenyl)acetamide
-
an isatin derivative, active against Gram-positive Bacillus subtilis and Staphylococcus aureus
2-(3-(2-carbamimidoylhydrazono)-2-oxoindolin-1-yl)-N-(3-nitrophenyl)acetamide
-
an isatin derivative, active against Gram-positive Bacillus subtilis and Staphylococcus aureus
2-(3-(2-carbamimidoylhydrazono)-2-oxoindolin-1-yl)-N-(m-tolyl)acetamide
-
an isatin derivative, active against Gram-positive Bacillus subtilis and Staphylococcus aureus with MIC values of 0.024 and 0.048 mg/ml, respectively
2-(3-(2-carbamimidoylhydrazono)-2-oxoindolin-1-yl)-N-(m-tolyl)acetamide
-
an isatin derivative, active against Gram-positive Bacillus subtilis and Staphylococcus aureus with MIC values of 0.024 and 0.048 mg/ml, respectively
4-[(1E)-2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen-2-yl)prop-1-en-1-yl]benzoic acid
-
-
4-[(1E)-2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen-2-yl)prop-1-en-1-yl]benzoic acid
-
-
4-[(1E)-2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen-2-yl)prop-1-en-1-yl]benzoic acid
-
-
4-[(1E)-2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen-2-yl)prop-1-en-1-yl]benzoic acid
-
-
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
-
-
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
Moenomycin
-
moenomycin A inhibits the transglycosylation step by binding to the donor site of the glycosyltransferase
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
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
-
synthesis of diverse isatin derivatives, MIC values for activity against Gram-positive Bacillus subtilis and Staphylococcus aureus, most compounds are poorly active, overview
-
additional information
-
molecular docking and modelling study using the structure of PBP1b, PDB ID 3VMA. NMR and mass spectrometric analysis of enzyme-inhibitor binding; 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
-
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, inhibtior 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, inhibtior 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
-
several analogues of the enzyme's lipid II substrate are synthesized previously and found to inhibit the enzyme activity in vitro and cause bacterial growth defect, overview
-
additional information
-
synthesis of diverse isatin derivatives, MIC values for activity against Gram-positive Bacillus subtilis and Staphylococcus aureus, most compounds are poorly active, overview
-
additional information
-
molecular docking and modelling study using the structure of MGT, PDB ID 3HZS. NMR and mass spectrometric analysis of enzyme-inhibitor binding. IC50 Inhibitory curves for MGT against moenomycin complex and vancomycin, overview; 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 3HZS. MIC values with strain ATCC 29213
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Abscess
PBP-2 Negative Methicillin Resistant Staphylococcus schleiferi Bacteremia from a Prostate Abscess: An Unusual Occurrence.
Adenocarcinoma
Gamma glutamyl transpeptidase in colon cancer induced by 1,2-dimethylhydrazine.
Arthritis
Tissue-specific galactosyltransferase abnormalities in an experimental model of rheumatoid arthritis.
Arthritis, Rheumatoid
Tissue-specific galactosyltransferase abnormalities in an experimental model of rheumatoid arthritis.
Bacteremia
Identification of a patient with Streptococcus pneumoniae bacteremia and meningitis by the polymerase chain reaction (PCR).
Bacteremia
PBP-2 Negative Methicillin Resistant Staphylococcus schleiferi Bacteremia from a Prostate Abscess: An Unusual Occurrence.
Blister
The gastroprotective potential of silibinin against Helicobacter pylori infection and gastric tumor cells.
Carcinogenesis
Glutathione and gamma glutamyl transpeptidase in rat liver during chemical carcinogenesis.
Carcinoma, Hepatocellular
Glutathione and gamma glutamyl transpeptidase in rat liver during chemical carcinogenesis.
Communicable Diseases
Alterations of pbp1a, pbp2b, and pbp2x in Streptococcus pneumoniae isolates from children with otolaryngological infectious disease in the Sapporo district of Japan.
Communicable Diseases
Computational studies of bacterial resistance to ?-lactam antibiotics: mechanism of covalent inhibition of the penicillin-binding protein 2a (PBP2a).
Cystic Fibrosis
Penicillin binding protein 3 is a common adaptive target among Pseudomonas aeruginosa isolates from adult cystic fibrosis patients treated with ?-lactams.
Cystitis
Morphological studies of Escherichia coli in the urine of patients with acute simple cystitis treated with aztreonam.
Dental Caries
Oral passive immunization against dental caries in rats by use of hen egg yolk antibodies specific for cell-associated glucosyltransferase of Streptococcus mutans.
Empyema
Identifying pneumococci in parapneumonic pleural effusion: Is there a role for culture-independent methods?
Gastritis, Atrophic
Prevalence of atrophic gastritis in southwest China and predictive strength of serum gastrin-17: A cross-sectional study (SIGES).
Hypersensitivity
The highly conserved serine threonine kinase StkP of Streptococcus pneumoniae contributes to penicillin susceptibility independently from genes encoding penicillin-binding proteins.
Infections
Bacteremia due to Staphylococcus aureus with reduced susceptibility to vancomycin.
Infections
Binding of ceftaroline to penicillin-binding proteins of Staphylococcus aureus and Streptococcus pneumoniae.
Infections
Clinical isolates of Staphylococcus intermedius masquerading as methicillin-resistant Staphylococcus aureus.
Infections
Computer aided screening and evaluation of herbal therapeutics against MRSA infections.
Infections
Crystal structures of penicillin-binding protein 2 from penicillin-susceptible and -resistant strains of Neisseria gonorrhoeae reveal an unexpectedly subtle mechanism for antibiotic resistance.
Infections
Determinants of plasma pepsinogen levels in a population at high risk for stomach cancer in Venezuela.
Infections
Expression of the Escherichia coli cell division gene sep cloned in a lambda Charon phage.
Infections
Identification of the Putative Specific Pathogenic Genes of Porphyromonas gingivalis with Type II Fimbriae.
Infections
Improved Performance of a Rapid Immunochromatographic Assay for the Detection of PBP2a in non-Staphylococcus aureus Staphylococcal Species.
Infections
Integrating a Rapid Diagnostic Test and Antimicrobial Stewardship: Optimizing Discharge Antibiotics in Skin and Soft Tissue Infections.
Infections
LB11058, a new cephalosporin with high penicillin-binding protein 2a affinity and activity in experimental endocarditis due to homogeneously methicillin-resistant Staphylococcus aureus.
Infections
Old Drugs To Treat Resistant Bugs: Methicillin-Resistant Staphylococcus aureus Isolates with mecC Are Susceptible to a Combination of Penicillin and Clavulanic Acid.
Infections
Pepsinogen-II 100Â bp ins/del gene polymorphism and its elevated circulating levels are associated with gastric cancer, particularly with Helicobacter pylori infection and intestinal metaplasia.
Infections
Quercetin 3-O-rutinoside mediated inhibition of PBP2a: computational and experimental evidence to its anti-MRSA activity.
Infections
Recombinant PBP2a as a vaccine candidate against methicillin-resistant Staphylococcus aureus: Immunogenicity and protectivity.
Infections
Relationship Between Different Resistance Mechanisms and Virulence in Acinetobacter baumannii.
Infections
Respiratory syncytial virus increases the virulence of Streptococcus pneumoniae by binding to penicillin binding protein 1a. A new paradigm in respiratory infection.
Infections
Single dose 1 g ceftriaxone for urogenital and pharyngeal infection caused by Neisseria gonorrhoeae.
Infections
Structural analysis of avibactam-mediated activation of the bla and mec divergons in methicillin-resistant Staphylococcus aureus.
Infections
The Molecular Epidemiology and Antimicrobial Resistance of Neisseria gonorrhoeae in Australia: A Nationwide Cross-Sectional Study, 2012.
Infections
The role of integrase/recombinase xerD and monofunctional biosynthesis peptidoglycan transglycosylase genes in the pathogenicity of Brucella abortus infection in vitro and in vivo.
Infections
Transcriptomic data for analyzing global gene expression patterns in Methicillin-resistance Staphylococcus aureus in response to spermine and oxacillin stress.
Meningitis
Identification of a patient with Streptococcus pneumoniae bacteremia and meningitis by the polymerase chain reaction (PCR).
Meningitis
Molecular epidemiology survey of penicillin-susceptible and -resistant Streptococcus pneumoniae recovered from patients with meningitis in France.
Neoplasms
Mechanisms of the Epithelial-Mesenchymal Transition and Tumor Microenvironment in Helicobacter pylori-Induced Gastric Cancer.
Neoplasms
Small molecule inhibitors of peptidoglycan synthesis targeting the lipid II precursor.
Otitis
[Molecular epidemiology of pneumococci with decreased susceptibility to penicillin isolated in a Parisian pediatric hospital]
Otitis Media
Antimicrobial resistance in Haemophilus influenzae isolated from the nasopharynx among Japanese children with acute otitis media.
Otitis Media
Antimicrobial resistance of Haemophilus influenzae isolated from the nasopharynx of Japanese children with acute otitis media.
Otitis Media
Diverse mutations in the ftsI gene in ampicillin-resistant Haemophilus influenzae isolates from pediatric patients with acute otitis media.
Otitis Media
High Prevalence of Streptococcus pneumoniae with Mutations in pbp1a, pbp2x, and pbp2b Genes of Penicillin-Binding Proteins in the Nasopharynx in Children in Japan.
Otitis Media
Nasopharyngeal carriage of drug-resistant Streptococcus pneumoniae in children with acute otitis media evaluated by polymerase chain reaction-based genotyping of penicillin-binding proteins.
Periodontal Diseases
Genetic variation of a fimbrial protein from Porphyromonas gingivalis and its distribution in patients with periodontal diseases.
Periodontal Diseases
Immunochemical characterisation and epitope mapping of a novel fimbrial protein (Pg-II fimbria) of Porphyromonas gingivalis.
Periodontitis
Differential virulence and innate immune interactions of type I and II fimbrial genotypes of Porphyromonas gingivalis.
Pneumonia
Molecular analysis of pbp2b in Streptococcus pneumonia isolated from clinical and normal flora samples.
Pneumonia
[Novel gene sequence variants of pbp2b in penicillin-nonsusceptible Streptococcus pneumonia isolates]
Pseudomonas Infections
Cloning, expression and purification of penicillin-binding protein 3 from Pseudomonas aeruginosa CMCC 10104.
Sepsis
Mode of bacterial killing affects the inflammatory response and associated organ dysfunctions in a porcine E. coli intensive care sepsis model.
Sepsis
Novel Immunoprotective Proteins of Streptococcus pneumoniae Identified by Opsonophagocytosis Killing Screen.
Sepsis
Passive immunization against methicillin resistant Staphylococcus aureus recombinant PBP2a in sepsis model of mice: Comparable results with antibiotic therapy.
Shock, Septic
Direct, Specific and Rapid Detection of Staphylococcal Proteins and Exotoxins Using a Multiplex Antibody Microarray.
Soft Tissue Infections
Integrating a Rapid Diagnostic Test and Antimicrobial Stewardship: Optimizing Discharge Antibiotics in Skin and Soft Tissue Infections.
Stomach Neoplasms
Prevalence of atrophic gastritis in southwest China and predictive strength of serum gastrin-17: A cross-sectional study (SIGES).
Tuberculosis
Characterization of a Mycobacterium smegmatis mutant lacking penicillin binding protein 1.
Tuberculosis
Loss of a Class A Penicillin-Binding Protein Alters ?-Lactam Susceptibilities in Mycobacterium tuberculosis.
Tuberculosis
Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis.
Tuberculosis
Structures of Mycobacterium tuberculosis Penicillin-Binding Protein 3 in Complex with Five ?-Lactam Antibiotics Reveal Mechanism of Inactivation.
Tuberculosis
The Role of the ?5-?11 Loop in the Active-Site Dynamics of Acylated Penicillin-Binding Protein A from Mycobacterium tuberculosis.
Urethritis
Single dose 1 g ceftriaxone for urogenital and pharyngeal infection caused by Neisseria gonorrhoeae.
Uterine Cervicitis
Single dose 1 g ceftriaxone for urogenital and pharyngeal infection caused by Neisseria gonorrhoeae.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
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
0.002
GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
lipid II, pH 8.0, 20°C
0.002
undecaprenyl-diphosphoryl-MurNAc-(L-Ala-gamma-D-Glu-meso-(diaminopimelic acid)-D-Ala-D-Ala)-GlcNAc
-
pH 7.5, 10 mM Mn2+
0.0028
undecaprenyl-diphosphoryl-MurNAc-(L-Ala-gamma-D-Glu-meso-(diaminopimelic acid)-D-Ala-D-Ala)-GlcNAc
-
pH 6.0, 10 mM Mn2+
0.0076
undecaprenyl-diphosphoryl-MurNAc-(L-Ala-gamma-D-Glu-meso-(diaminopimelic acid)-D-Ala-D-Ala)-GlcNAc
-
pH 7.5, 50 mM Mg2+
0.008
undecaprenyl-diphosphoryl-MurNAc-(L-Ala-gamma-D-Glu-meso-(diaminopimelic acid)-D-Ala-D-Ala)-GlcNAc
-
pH 7.5, 10 mM Mg2+
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
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
purified wild type enzyme
additional information
additional information
-
turnover-numbers of truncated variants
-
0.0063
undecaprenyl-diphosphoryl-MurNAc-(L-Ala-gamma-D-Glu-meso-(diaminopimelic acid)-D-Ala-D-Ala)-GlcNAc
-
pH 6.0, 10 mM Mn2+
0.0076
undecaprenyl-diphosphoryl-MurNAc-(L-Ala-gamma-D-Glu-meso-(diaminopimelic acid)-D-Ala-D-Ala)-GlcNAc
-
pH 7.5, 50 mM Mg2+
0.008
undecaprenyl-diphosphoryl-MurNAc-(L-Ala-gamma-D-Glu-meso-(diaminopimelic acid)-D-Ala-D-Ala)-GlcNAc
-
pH 7.5, 10 mM Mg2+
0.013
undecaprenyl-diphosphoryl-MurNAc-(L-Ala-gamma-D-Glu-meso-(diaminopimelic acid)-D-Ala-D-Ala)-GlcNAc
-
pH 7.5, 10 mM Mn2+
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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
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
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
[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
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
-
-
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
0.0093
4-[(1E)-2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen-2-yl)prop-1-en-1-yl]benzoic acid
Helicobacter pylori
-
-
0.0497 - 0.0732
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
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
0.0732
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
Staphylococcus aureus
-
pH 7.5, 25°C, MGT
0.000006
moenomycin A
Staphylococcus aureus
-
recombinant wild-type enzyme, pH and temperature not specified in the publication
0.000075
moenomycin A
Staphylococcus aureus
-
recombinant enzyme mutant Y181W, pH and temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 45
-
about 60% of maximal activity at 20°C and about half-maximal activity at 45°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC 49247 and beta-lactamase-negative ampicillin-resistant and beta-lactamase-positive amoxicillin-clavulanic acid-resistant strains
-
-
brenda
-
488534, 488535, 488536, 657556, 658267, 659032, 659500, 659960, 671367, 672145, 674207, 701718, 703349, 704163, 704438
-
-
brenda
clonal groups Poland23F-16 (strain ATCC BAA-343) and Poland6B-20 (strain ATCC BAA-612)
UniProt
brenda
clonal groups Poland23F-16 (strain ATCC BAA-343) and Poland6B-20 (strain ATCC BAA-612)
SwissProt
brenda
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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
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
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
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. Staphylococcus aureus has a single class A PBP (PBP2) and 2 MGT proteins (SgtA, SgtB/MGT)
evolution
-
the enzyme belongs to the glycosyltransferases of family 51 (GT51), the glycosyltransferases of family 51 are essential enzymes found in bacteria with peptidoglycan cell wall. They exist in two forms: as a monofunctional domain or linked to the N-terminal end of penicillin-binding (PB) domain in bifunctional PB proteins. Both forms catalyze the polymerization of lipid II (undecaprenyl pyrophosphate-MurNAc(pentapeptide)-GlcNAc) precursor to form linear glycan chains
evolution
Streptococcus pneumoniae contains three class A (PBP1a, PBP2a and PBP1b) and two class B (PBP2x and PBP2b) enzymes. PBP1a and PBP2a are not equivalent
evolution
-
the enzyme belongs to the peptidoglycan glycosyltransferase family 51
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
-
evolution
-
Streptococcus pneumoniae contains three class A (PBP1a, PBP2a and PBP1b) and two class B (PBP2x and PBP2b) enzymes. PBP1a and PBP2a are not equivalent
-
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. Staphylococcus aureus has a single class A PBP (PBP2) and 2 MGT proteins (SgtA, SgtB/MGT)
-
malfunction
-
inhibition of the enzyme blocks peptidoglycan synthesis and leads to bacterial lysis and death
malfunction
an Staphylococcus aureus sgtB transposon mutant, with the monofunctional peptidoglycan glycosyltransferase SgtB inactivated, display a 4fold increase in the MIC of oxacillin, suggesting that alterations in the peptidoglycan structure can help bacteria compensate for the lack of lipoteichoic acid (LTA). Muropeptide analysis of peptidoglycans isolated from a wild-type strain and sgtB mutant strain does not reveal any sizable alterations in the peptidoglycan structure. In contrast, the peptidoglycan isolated from an LTA-negative ltaS mutant strain shows a significant reduction in the fraction of highly cross-linked peptidoglycan, which is partially rescued in the sgtB ltaS double mutant suppressor strain. Introduction of SgtB or MazE in the respective suppressor strain results in growth arrest. Increased resistance of the sgtB mutant to oxacillin. The increase in peptidoglycan cross-linking potentially strengthens the cell wall to better sustain the high internal turgor pressure and might be at least partly responsible for the observed growth improvement
malfunction
DELTAmltG mutants in unencapsulated strains accumulate inactivation mutations of class A PBP1a. The reduction of cell width and size of DELTApbp1a mutants compared to those of wild-type parent cells. Mutations in pbp1a suppress the DELTAmltG mutations
malfunction
mutations that inactivate the pneumococcal YceG-domain protein, Spd_1346 (renamed MltG), remove the requirement for PBP2b. DELTAmltG mutants in unencapsulated strains accumulate inactivation mutations of class A PBP1a, which possesses TP and transglycosylase (TG) activities
malfunction
-
DELTAmltG mutants in unencapsulated strains accumulate inactivation mutations of class A PBP1a. The reduction of cell width and size of DELTApbp1a mutants compared to those of wild-type parent cells. Mutations in pbp1a suppress the DELTAmltG mutations
-
malfunction
-
mutations that inactivate the pneumococcal YceG-domain protein, Spd_1346 (renamed MltG), remove the requirement for PBP2b. DELTAmltG mutants in unencapsulated strains accumulate inactivation mutations of class A PBP1a, which possesses TP and transglycosylase (TG) activities
-
metabolism
-
the enzyme also functions as an activity enhancer of SpoIIP which generates its substrate
metabolism
the pneumococcal YceG-domain protein MltG releases anchored peptidoglycan (PG) glycan strands synthesized by PBP1a for crosslinking by a PBP2b:RodA complex in peripheral PG synthesis
metabolism
-
the pneumococcal YceG-domain protein MltG releases anchored peptidoglycan (PG) glycan strands synthesized by PBP1a for crosslinking by a PBP2b:RodA complex in peripheral PG synthesis
-
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
-
pbp-1C gene regulates in vitro growth and cell morphology, whereas pbp-1A, pbp-1B, and pbp-2 genes are essential for viability of Brucella melitensis
physiological function
-
PGT catalyzes the polymerization of lipid II to form the bacterial cell wall
physiological function
-
bifunctional penicillin-binding proteins (PBPs) proceed and catalyze the transglycosylation and transpeptidation. Bifunctional PBPs have both glycosyltransferase and transpeptidase catalytic sites that are located at N-terminus and C-terminus, respectively. In transglycosylation step, the glycosyltransferase polymerizes disaccharide phospholipid lipid II into polysaccharide strands. These oligosaccharide strands are cross-linked by transpeptidase to form peptidoglycans in the next transpeptidation step
physiological function
-
bifunctional penicillin-binding proteins (PBPs) proceed and catalyze the transglycosylation and transpeptidation. Bifunctional PBPs have both glycosyltransferase and transpeptidase catalytic sites that are located at N-terminus and C-terminus, respectively. In transglycosylation step, the glycosyltransferase polymerizes disaccharide phospholipid lipid II into polysaccharide strands. These oligosaccharide strands are cross-linked by transpeptidase to form peptidoglycans in the next transpeptidation step
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
-
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 enzyme catalyze the polymerization of lipid II to form linear glycan chains, which, after cross linking by the transpeptidases, form the net-like peptidoglycan macromolecule, which encases bacteria and protects them from rupture under their high cytoplasmic pressure
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
-
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
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
physiological function
peptidoglycan (PG) is composed of glycan chains of beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) sugars that are crosslinked by PG peptides. Pneumococcal PG provides the major scaffold for the covalent attachment of wall-teichoic acid (WTA), capsule and surface proteins linked by sortases, many of which are virulence factors. Class A PBP1a, which possesses TP and transglycosylase (TG) activities
physiological function
peptidoglycan (PG) is composed of glycan chains of beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) sugars that are crosslinked by PG peptides. Pneumococcal PG provides the major scaffold for the covalent attachment of wall-teichoic acid (WTA), capsule and surface proteins linked by sortases, many of which are virulence factors. In the pathogen Streptococcus pneumoniae (pneumococcus), side-wall (peripheral) peptidoglycan (PG) synthesis emanates from midcells and is catalyzed by the essential class B penicillin-binding protein PBP2b transpeptidase (TP). Class B PBP2x and PBP2b are essential for growth and required for septal and peripheral PG synthesis, respectively, in dividing Streptococcus pneumoniae cells. Pbp2b is essential in unencapsulated or encapsulated wild-type D39 strains
physiological function
peptidoglycan glycosyltransferase (PGT) transfers the disaccharide-peptide of lipid II to the growing glycan chain in bacterial cell wall synthesis
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
physiological function
Staphylococcus aureus has a typical Gram-positive cell envelope, which consists of a cytoplasmic membrane surrounded by a thick peptidoglycan layer. The peptidoglycan layer is a dynamic macromolecular structure that undergoes constant cycles of polymerization and hydrolysis to allow bacteria to grow and to divide. It is composed of glycan chains made of alternating N-acetylglucosamine and N-acetylmuramic acid residues connected by peptide bridges. This mesh-like sacculus is able to protect the cell from environmental threats while withstanding the high internal osmotic pressure. The final steps of peptidoglycan synthesis are catalyzed by enzymes termed penicillin binding proteins (PBPs) and coordinated actions of these enzymes are crucial for cell survival. PBPs with glycosyltransferase and transpeptidase activities polymerize the glycan chains and form peptide cross-bridges, while monofunctional transpeptidases, e.g. the monofunctional peptidoglycan glycosyltransferase SgtB in Staphylococcus aureus, have only the former activity. Important function of lipoteichoic acid (LTA) in cell wall integrity through its necessity for proper peptidoglycan assembly
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
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
-
physiological function
-
peptidoglycan (PG) is composed of glycan chains of beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) sugars that are crosslinked by PG peptides. Pneumococcal PG provides the major scaffold for the covalent attachment of wall-teichoic acid (WTA), capsule and surface proteins linked by sortases, many of which are virulence factors. Class A PBP1a, which possesses TP and transglycosylase (TG) activities
-
physiological function
-
peptidoglycan (PG) is composed of glycan chains of beta-1-4-linked N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) sugars that are crosslinked by PG peptides. Pneumococcal PG provides the major scaffold for the covalent attachment of wall-teichoic acid (WTA), capsule and surface proteins linked by sortases, many of which are virulence factors. In the pathogen Streptococcus pneumoniae (pneumococcus), side-wall (peripheral) peptidoglycan (PG) synthesis emanates from midcells and is catalyzed by the essential class B penicillin-binding protein PBP2b transpeptidase (TP). Class B PBP2x and PBP2b are essential for growth and required for septal and peripheral PG synthesis, respectively, in dividing Streptococcus pneumoniae cells. Pbp2b is essential in unencapsulated or encapsulated wild-type D39 strains
-
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
-
physiological function
-
bifunctional penicillin-binding proteins (PBPs) proceed and catalyze the transglycosylation and transpeptidation. Bifunctional PBPs have both glycosyltransferase and transpeptidase catalytic sites that are located at N-terminus and C-terminus, respectively. In transglycosylation step, the glycosyltransferase polymerizes disaccharide phospholipid lipid II into polysaccharide strands. These oligosaccharide strands are cross-linked by transpeptidase to form peptidoglycans in the next transpeptidation step
-
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
additional information
-
overall fold and active site of wild-type and mutant GTases
additional information
the single MltG(Y488D) change suppresses the requirement for PBP2b, MreCD, RodZ and RodA
additional information
the single MltG(Y488D) change suppresses the requirement for PBP2b, MreCD, RodZ and RodA
additional information
-
the single MltG(Y488D) change suppresses the requirement for PBP2b, MreCD, RodZ and RodA
additional information
-
the single MltG(Y488D) change suppresses the requirement for PBP2b, MreCD, RodZ and RodA
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90000
-
x * 90000, Escherichia coli penicillin binding protein 1B alpha, beta or gamma
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 90000, Escherichia coli penicillin binding protein 1B alpha, beta or gamma
?
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x * 90000, Escherichia coli penicillin binding protein 1B alpha, beta or gamma
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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
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K124A
mutant shows 5fold reduced activity compared to the wild type enzyme
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)
H297A
-
the mutant is severely impaired in sporulation efficiency (0.02% efficiency compared to the wild type enzyme)
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
E233Q
F237A
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
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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
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
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
E100Q
-
mutant of the soluble form of Staphylococcus aureus MGT devoid of its membrane anchor, called SauH6-MGT. glycosyltransferase activity of the mutant is reduced 500fold compared to the wild type
E100Q
-
site-directed mutagenesis, E100Q binds moenomycin A in the same order of magnitude as the wild-type
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
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
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additional information
-
construction of the MtgA (D68-R269) mutant lacking the transmembrane segment
additional information
introduction of wild-type and mutant SgtBs in a wild-type Staphylococcus aureus strain and in an ltaS mutant strain (ANG2135) deficient in lipoteichoic acid (LTA). Growth and cell morphology of wild-type and mutant strains. Introduction of SgtB or MazE in the respective suppressor strain results in growth arrest. Inactivation of MazE or SgtB is sufficient to allow Staphylococcus aureus to grow in the absence of LTA. Inactivation of SgtB leading to an increase in peptidoglycan cross-linking in an LTA-negative Staphylococcus aureus strain. Increased resistance of the sgtB mutant to oxacillin
additional information
-
introduction of wild-type and mutant SgtBs in a wild-type Staphylococcus aureus strain and in an ltaS mutant strain (ANG2135) deficient in lipoteichoic acid (LTA). Growth and cell morphology of wild-type and mutant strains. Introduction of SgtB or MazE in the respective suppressor strain results in growth arrest. Inactivation of MazE or SgtB is sufficient to allow Staphylococcus aureus to grow in the absence of LTA. Inactivation of SgtB leading to an increase in peptidoglycan cross-linking in an LTA-negative Staphylococcus aureus strain. Increased resistance of the sgtB mutant to oxacillin
additional information
construction of DELTA pbp2A deletion mutants. Domain architecture of PBP1a, TP active site motifs and mapped mutations in gene pbp1a in DELTAmltG suppressor strains. DELTApbp2A/DELTAmltG mutant phenotype, overview
additional information
construction of DELTA pbp2A deletion mutants. Domain architecture of PBP1a, TP active site motifs and mapped mutations in gene pbp1a in DELTAmltG suppressor strains. DELTApbp2A/DELTAmltG mutant phenotype, overview
additional information
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construction of DELTA pbp2A deletion mutants. Domain architecture of PBP1a, TP active site motifs and mapped mutations in gene pbp1a in DELTAmltG suppressor strains. DELTApbp2A/DELTAmltG mutant phenotype, overview
additional information
construction of DELTA pbp2B deletion mutants. Mutations in spd_1346 (mltG) suppress a DELTApbp2b deletion mutation. DELTApbp2B/DELTAmltG mutant phenotype, overview
additional information
construction of DELTA pbp2B deletion mutants. Mutations in spd_1346 (mltG) suppress a DELTApbp2b deletion mutation. DELTApbp2B/DELTAmltG mutant phenotype, overview
additional information
-
construction of DELTA pbp2B deletion mutants. Mutations in spd_1346 (mltG) suppress a DELTApbp2b deletion mutation. DELTApbp2B/DELTAmltG mutant phenotype, overview
additional information
-
construction of DELTA pbp2A deletion mutants. Domain architecture of PBP1a, TP active site motifs and mapped mutations in gene pbp1a in DELTAmltG suppressor strains. DELTApbp2A/DELTAmltG mutant phenotype, overview
-
additional information
-
construction of DELTA pbp2B deletion mutants. Mutations in spd_1346 (mltG) suppress a DELTApbp2b deletion mutation. DELTApbp2B/DELTAmltG mutant phenotype, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the soluble form of the glycosyltransferase domain of PBP1a in Escherichia coli
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
Ni2+-affinity column chromatography, gel filtration, and Mono Q ion-exchange chromatography
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nickel chelation column chromatography and Superdex 200 gel filtration
partial
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
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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
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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
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activity of PBP1a or PBP1b can be measured in membranes by cloning the PBP into an Escherichia coli ponB::Spcr strain
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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
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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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gene mrcB, recombinant expression of His6-tagged PBP1b (residues 58-604) in Escherichia coli
gene pbp2A, recombinant expression of FLAG-tagged wild-type and mutant enzymes in Streptococcus pneumoniae strain D39 DELTAcps/DELTAmltG obtained from strain IU7260
gene penA or pbp2B, genotyping, recombinant expression in Streptococcus pneumoniae strain IU1824, i.e. D39 DELTAcps
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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overexpression of His-tagged enzyme in Escherichia coli strain BL21 pDML924
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
-
wild type and mutant enzymes are expressed in Escherichia coli BL21(DE3) cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
medicine
drug development
-
the essential function of the enzyme makes it an attractive antimicrobial target
drug development
-
the essential function of the enzyme makes it an attractive antimicrobial target
drug development
peptidoglycan glycosyltransferase (PGT) is regarded as a potential drug target for development of antibiotics
drug development
-
the essential function of the enzyme makes it an attractive antimicrobial target
-
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
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Taku, A.; Stuckey, M.; Fan, D.P.
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J. Biol. Chem.
257
5018-5022
1982
Priestia megaterium, Priestia megaterium 899
brenda
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
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1981
Escherichia coli
brenda
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Staphylococcus aureus and Micrococcus luteus peptidoglycan transglycosylases that are not penicillin-binding proteins
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157
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1984
Micrococcus luteus, Staphylococcus aureus, Micrococcus luteus SM1, Staphylococcus aureus SAK 101
brenda
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259
13937-13946
1984
Escherichia coli, Escherichia coli JA200/pLC19-19
brenda
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
-
brenda
Van Heijenoort, J.
Formation of the glycan chains in the synthesis of bacterial peptidoglycan
Glycobiology
11
25R-36R
2001
Streptococcus pneumoniae, Escherichia coli
brenda
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
brenda
Stefanova, M.E.; Tomberg, J.; Olesky, M.; Holtje, J.V.; Gutheil, W.G.; Nicholas, R.A.
Neisseria gonorrhoeae penicillin-binding protein 3 exhibits exceptionally high carboxypeptidase and beta-lactam binding activities
Biochemistry
42
14614-14625
2003
Neisseria gonorrhoeae (O85665), Neisseria gonorrhoeae
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Offant, J.; Michoux, F.; Dermiaux, A.; Biton, J.; Bourne, Y.
Functional characterization of the glycosyltransferase domain of penicillin-binding protein 1a from Thermotoga maritima
Biochim. Biophys. Acta
1764
1036-1042
2006
Thermotoga maritima (Q9WZY8), Thermotoga maritima
brenda
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
brenda
Zawadzka-Skomial, J.; Markiewicz, Z.; Nguyen-Disteche, M.; Devreese, B.; Frere, J.M.; Terrak, M.
Characterization of the bifunctional glycosyltransferase/acyltransferase penicillin-binding protein 4 of Listeria monocytogenes
J. Bacteriol.
188
1875-1881
2006
Listeria monocytogenes
brenda
Terrak, M.; Nguyen-Disteche, M.
Kinetic characterization of the monofunctional glycosyltransferase from Staphylococcus aureus
J. Bacteriol.
188
2528-2532
2006
Staphylococcus aureus
brenda
Yuan, Y.; Barrett, D.; Zhang, Y.; Kahne, D.; Sliz, P.; Walker, S.
Crystal structure of a peptidoglycan glycos