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Information on EC 5.1.1.3 - glutamate racemase
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5.1.1.3 glutamate racemaseIUBMB Comments
A pyridoxal-phosphate protein.
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Word Map
- 5.1.1.3
- peptidoglycan
- drug development
-
cofactor-independent
- pediococcus
- pentosaceus
-
poly-gamma-glutamate
- pyrophilus
- fermenti
- medicine
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
BAS0806, BAS4379, BcGR, BsGR, BsRacE, D-glutamate racemase, DapF, FnGR, GBAA_0847, GBAA_4717, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BAS0806
BAS4379
GBAA_0847
GBAA_4717
glutamate racemase
glutamic acid racemases
MurI
RACE
RacE1
RacE2
Racemase, glutamate
-
-
-
-
Rv1338
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-glutamate = D-glutamate
-
-
-
-
L-glutamate = D-glutamate
the enzyme uses a two-base mechanism in which two Cys thiolates serve as the general base/acid catalysts. An initial deprotonation event produces a resonance-stabilized carbanionic intermediate that is subsequently protonated on the opposite face to generate the enantiomeric product
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L-glutamate = D-glutamate
two base mechanism, removal of alpha-hydrogen is the rate determining step
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L-glutamate = D-glutamate
deprotonation/protonation mechanism for racemization in which the breaking of the carbon-hydrogen bond at C-2 is partially rate-determining
-
L-glutamate = D-glutamate
deprotonation/protonation mechanism. Two-base mechanism in which one enzymic base deprotonates the substrate, and the conjugate acid of a second enzymic base protonates the resulting intermediate from the opposite face
-
L-glutamate = D-glutamate
initial step is the proton abstraction from the substrate alpha-carbon atom, which is mediated by an amino acid residue in the enzyme protein
-
L-glutamate = D-glutamate
the enzyme uses a two-base mechanism involving a deprotonation of the substrate at the alpha-position to form an anionic intermediate, followed by a reprotonation in the opposite stereochemical sense. Cys73 is responsible for the deprotonation of D-glutamate and Cys184 is responsible for the deprotonation of L-glutamate
-
L-glutamate = D-glutamate
molecular dynamics simulations, mechanism by which binding mismatches are propagated into an opening of the active site
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L-glutamate = D-glutamate
glutamate racemase faces the difficult task of deprotonating a relatively low acidicity proton, the amino acid’s R-hydrogen, with a relatively poor base, a cysteine. The titration curves and the pK1/2 values of all of the ionizable residues for different structures leading from reactants to products are analyzed. From these results a concerted mechanism is proposed in which the Cys70 residue deprotonates the R-hydrogen of the substrate while, at the same time, being deprotonated by the Asp7 residue
-
L-glutamate = D-glutamate
the molecular mechanism involves deprotonation of the glutamate alpha-proton, followed by substrate reprotonation on the opposite stereochemical face
-
L-glutamate = D-glutamate
MurI is a member of the two-base mechanism (dual-cysteine) racemase family, where two essential active-site cysteine residues act as catalytic base and acid to stereospecifically de- and reprotonate, respectively, the alpha position of glutamate in order to enact substrate racemization. C185 of BsMurI corresponds to the essential catalytic cysteine residue that deprotonates an incoming L-glutamate substrate (or reprotonates a carbanionic intermediate to form the D-stereoconfiguration)
-
L-glutamate = D-glutamate
MurI is a member of the two-base mechanism (dual-cysteine) racemase family, where two essential active-site cysteine residues act as catalytic base and acid to stereospecifically de- and reprotonate, respectively, the alpha position of glutamate in order to enact substrate racemization
-
L-glutamate = D-glutamate
MurI is a member of the two-base mechanism (dual-cysteine) racemase family, where two essential active-site cysteine residues act as catalytic base and acid to stereospecifically de- and reprotonate, respectively, the alpha position of glutamate in order to enact substrate racemization. C185 of BsMurI corresponds to the essential catalytic cysteine residue that deprotonates an incoming L-glutamate substrate (or reprotonates a carbanionic intermediate to form the D-stereoconfiguration)
-
-
L-glutamate = D-glutamate
MurI is a member of the two-base mechanism (dual-cysteine) racemase family, where two essential active-site cysteine residues act as catalytic base and acid to stereospecifically de- and reprotonate, respectively, the alpha position of glutamate in order to enact substrate racemization
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
racemization
racemization
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
glutamate racemase
A pyridoxal-phosphate protein.
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CAS REGISTRY NUMBER
COMMENTARY
9024-08-2
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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
D-glutamate
L-glutamate
-
catalytic action of glutamate racemase is driven by its own substrate, D-glutamate
-
-
r
D-glutamate
L-glutamate
enzyme catalyzes the formation of D-glutamate from L-glutamate through a 1,1-proton transfer mechanism which reversibly inverts the stereochemistry at the alpha-carbon of glutamate
-
-
r
D-glutamate
L-glutamate
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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D-Glu binding structure, overview
-
-
r
D-glutamate
L-glutamate
D-Glu binding structure, overview
-
-
r
D-glutamate
L-glutamate
Mycolicibacterium smegmatis ATCC 700084 / mc(2)155
D-Glu binding structure, overview
-
-
r
L-2-aminoadipic acid
D-2-aminoadipic acid
-
-
-
-
L-Glu
?
glutamate racemase is mainly concerned in D-Glu synthesis for poly-gamma-glutamate production
-
-
-
L-Glu
?
-
glutamate racemase is mainly concerned in D-Glu synthesis for poly-gamma-glutamate production
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-
-
L-Glu
?
-
the biosynthesis of D-Glu, one of the essential components of bacterial cell-wall peptidoglycan, is catalyzed by glutamate racemase
-
-
-
L-Glu
?
Lactic acid bacteria
-
the biosynthesis of D-Glu, one of the essential components of bacterial cell-wall peptidoglycan, is catalyzed by glutamate racemase
-
-
-
L-glutamate
D-glutamate
the enzyme is responsible for the synthesis of D-glutamate, an essential building block of the peptidoglycan layer in bacterial cell walls
-
?
L-glutamate
D-glutamate
enzyme catalyzes the formation of D-glutamate from L-glutamate through a 1,1-proton transfer mechanism which reversibly inverts the stereochemistry at the alpha-carbon of glutamate
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-
r
L-glutamate
D-glutamate
-
MurI enzymes from the Gram-positive species Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium share similar biophysical and biochemical characteristics that are distinct from Escherichia coli and Helicobacter pylori MurI
-
-
r
L-glutamate
D-glutamate
-
MurI enzymes from the Gram-positive species Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium share similar biophysical and biochemical characteristics that are distinct from Escherichia coli and Helicobacter pylori MurI
-
-
r
L-glutamate
D-glutamate
enzyme catalyzes the formation of D-glutamate from L-glutamate through a 1,1-proton transfer mechanism which reversibly inverts the stereochemistry at the alpha-carbon of glutamate
-
-
r
L-glutamate
D-glutamate
-
the enzyme provides bacteria with a source of D-glutamate for use in peptidoglycan biosynthesis
-
?
L-glutamate
D-glutamate
-
MurI enzymes from the Gram-positive species Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium share similar biophysical and biochemical characteristics that are distinct from Escherichia coli and Helicobacter pylori MurI
-
-
r
L-Homocysteinesulfinate
D-Homocysteinesulfinate
-
slightly serves as substrate
-
-
additional information
?
-
-
Chlamydia trachomatis dapF encodes a bifunctional enzyme capable of both D-glutamate racemase and diaminopimelate epimerase, EC 5.1.1.7, activities. Diaminopimelate and glutamate appear to be competitive substrates, indicating that they share an active site despite the racemase reaction requiring the PLP cofactor
-
-
-
additional information
?
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-
the enzyme is an endogenous DNA gyrase inhibitor
-
?
additional information
?
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-
the enzyme uses a two-base mechanism involving a deprotonation of the substrate at the alpha-position to form an anionic intermediate, followed by a reprotonation in the opposite stereochemical sense. Cys73 is responsible for the deprotonation of D-glutamate and Cys184 is responsible for the deprotonation of L-glutamate
-
?
additional information
?
-
-
enzyme does not catalyze the exchange between 2-oxolutarate and DL-Glu
-
-
-
additional information
?
-
-
enzyme does not catalyze the exchange between 2-oxolutarate and DL-Glu
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-
-
additional information
?
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-
enzyme exhibits both racemization activity and DNA gyrase inhibition. The two activities are unlinked and independent of each other. Enzyme-DNA gyrase interaction influences gyrase activity but has no effect on the racemization activity
-
-
-
additional information
?
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-
in addition to racemization activity, enzyme exhibits DNA gyrase activity by preventing DNA binding of gyrase. Sequestration of gyrase results in inhibition of all reactions catalyzed by DNA gyrase. Overexpression additiionally provides protection against ciprofloxacin
-
-
-
additional information
?
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-
in addition to racemization activity, enzyme exhibits DNA gyrase activity by preventing DNA binding of gyrase. Sequestration of gyrase results in inhibition of all reactions catalyzed by DNA gyrase. Overexpression additionally provides protection against ciprofloxacin
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-
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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
D-glutamate
L-glutamate
-
catalytic action of glutamate racemase is driven by its own substrate, D-glutamate
-
-
r
D-glutamate
L-glutamate
Q8REE6
enzyme catalyzes the formation of D-glutamate from L-glutamate through a 1,1-proton transfer mechanism which reversibly inverts the stereochemistry at the alpha-carbon of glutamate
-
-
r
L-2-aminoadipic acid
D-2-aminoadipic acid
Q8REE6
-
-
-
-
L-Glu
?
P94556
glutamate racemase is mainly concerned in D-Glu synthesis for poly-gamma-glutamate production
-
-
-
L-Glu
?
-
glutamate racemase is mainly concerned in D-Glu synthesis for poly-gamma-glutamate production
-
-
-
L-Glu
?
-
the biosynthesis of D-Glu, one of the essential components of bacterial cell-wall peptidoglycan, is catalyzed by glutamate racemase
-
-
-
L-Glu
?
Lactic acid bacteria
-
the biosynthesis of D-Glu, one of the essential components of bacterial cell-wall peptidoglycan, is catalyzed by glutamate racemase
-
-
-
L-glutamate
D-glutamate
P56868
the enzyme is responsible for the synthesis of D-glutamate, an essential building block of the peptidoglycan layer in bacterial cell walls
-
?
L-glutamate
D-glutamate
P94556
enzyme catalyzes the formation of D-glutamate from L-glutamate through a 1,1-proton transfer mechanism which reversibly inverts the stereochemistry at the alpha-carbon of glutamate
-
-
r
L-glutamate
D-glutamate
Q8REE6
enzyme catalyzes the formation of D-glutamate from L-glutamate through a 1,1-proton transfer mechanism which reversibly inverts the stereochemistry at the alpha-carbon of glutamate
-
-
r
additional information
?
-
-
Chlamydia trachomatis dapF encodes a bifunctional enzyme capable of both D-glutamate racemase and diaminopimelate epimerase, EC 5.1.1.7, activities. Diaminopimelate and glutamate appear to be competitive substrates, indicating that they share an active site despite the racemase reaction requiring the PLP cofactor
-
-
-
additional information
?
-
-
the enzyme is an endogenous DNA gyrase inhibitor
-
?
additional information
?
-
-
enzyme exhibits both racemization activity and DNA gyrase inhibition. The two activities are unlinked and independent of each other. Enzyme-DNA gyrase interaction influences gyrase activity but has no effect on the racemization activity
-
-
-
additional information
?
-
-
in addition to racemization activity, enzyme exhibits DNA gyrase activity by preventing DNA binding of gyrase. Sequestration of gyrase results in inhibition of all reactions catalyzed by DNA gyrase. Overexpression additiionally provides protection against ciprofloxacin
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
the glutamate racemase activity is dependent on the cofactor pyridoxal phosphate
additional information
-
glutamate racemase (MurI) is a pyridoxal 5'-phosphate-independent racemase
-
additional information
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glutamate racemase (MurI) is a pyridoxal 5'-phosphate-independent racemase
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no effects on activity by Mg2+, Fe2+, and Ni2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,4R)-2-amino-4-(2-benzo[b]furyl)methyl pentanedioic acid
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IC50: 0.1 mg/l, minimum inhibitor concentration: 0.24 mg/l
(2R,4R)-2-amino-4-(2-benzo[b]thiazolyl)methyl pentanedioic acid
-
IC50: 0.38 mg/l, minimum inhibitor concentration: 0.24 mg/l
(2R,4R)-2-amino-4-(2-benzo[b]thienyl)methyl pentanedioic acid
-
IC50: 0.036 mg/l, minimum inhibitor concentration: 0.24 mg/l
(2R,4R)-2-amino-4-(2-indolyl)methyl pentanedioic acid
-
IC50: 9.8 mg/l, minimum inhibitor concentration: 62.5 mg/l
(2R,4R)-2-amino-4-(2-thienyl)methyl pentanedioic acid
-
IC50: 0.1 mg/l, minimum inhibitor concentration: above 1.0 mg/l
(2R,4R)-2-amino-4-[(3-chloro)-2-benzo[b]thienyl]methyl pentanedioic acid
-
IC50: 0.01 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(2-bromo)benzyl pentanedioic acid
-
IC50: 6.3 mg/l, minimum inhibitor concentration: 31.3 mg/l
(2R,4S)-2-amino-4-(2-chloro)benzyl pentanedioic acid
-
IC50: 7.1 mg/l, minimum inhibitor concentration: 3.9 mg/l
(2R,4S)-2-amino-4-(3,4,5-trimethoxy)benzyl pentanedioic acid
-
IC50: 81 mg/l, minimum inhibitor concentration: above 250 mg/l
(2R,4S)-2-amino-4-(3,5-dichloro)benzyl pentanedioic acid
-
IC50: 3.0 mg/l, minimum inhibitor concentration: 3.9 mg/l
(2R,4S)-2-amino-4-(3-benzo[b]thienyl)methyl pentanedioic acid
-
IC50: 1.7 mg/l, minimum inhibitor concentration: 7.8 mg/l
(2R,4S)-2-amino-4-(3-bromo)benzyl pentanedioic acid
-
IC50: 0.13 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(3-chloro)benzyl pentanedioic acid
-
IC50: 3.4 mg/l, minimum inhibitor concentration: 1.0 mg/l
(2R,4S)-2-amino-4-(3-cyclohexyl)propyl pentanedioic acid
-
IC50: 0.6 mg/l, MIC: 2.0 mg/l
(2R,4S)-2-amino-4-(3-methoxy)benzyl pentanedioic acid
-
IC50: 0.2 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(3-nitro)benzyl pentanedioic acid
-
IC50: 5.2 mg/l, minimum inhibitor concentration: 2.0 mg/l
(2R,4S)-2-amino-4-(3-phenyl)benzyl pentanedioic acid
-
IC50: 0.7 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(3-phenyl)propargyl pentanedioic acid
-
IC50: 0.37 mg/l, minimum inhibitor concentration: 2.0 mg/l
(2R,4S)-2-amino-4-(3-phenyl)propyl pentanedioic acid
-
IC50: 0.5 mg/l, minimum inhibitor concentration: 3.9 mg/l
(2R,4S)-2-amino-4-(3-trifluoromethyl)benzyl pentanedioic acid
-
IC50: 0.8 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(4-chloro)benzyl pentanedioic acid
-
IC50: 0.3 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(4-methoxy)benzyl pentanedioic acid
-
IC50: 0.1 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(4-nitro)benzyl pentanedioic acid
-
IC50: 5.2 mg/l, minimum inhibitor concentration: 2.0 mg/l
(2R,4S)-2-amino-4-(4-phenyl)benzyl pentanedioic acid
-
IC50: 0.078 mg/l, minimum inhibitor concentration: 1.0 mg/l
(2R,4S)-2-amino-4-(4-tert-butyl)benzyl pentanedioic acid
-
IC50: 0.6 mg/l, minimum inhibitor concentration: 1.0 mg/l
(2R,4S)-2-amino-4-(4-trifluoromethyl)benzyl pentanedioic acid
-
IC50: 0.8 mg/l, minimum inhibitor concentration: 7.8 mg/l
(2R,4S)-2-amino-4-(5-phenyl-2E,4E-pentadienyl)pentanedioic acid
-
IC50: 9.1 mg/l, minimum inhibitor concentration: 3.9 mg/l
(2R,4S)-2-amino-4-(prop-2-ynyl) pentanedioic acid
-
IC50: 5.5 mg/l, MIC: 31.3 mg/l
(2R,4S)-2-amino-4-[3-(2-benzo[b]thienyl)]benzyl pentanedioic acid
-
IC50: 0.3 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-[3-(2-furyl)]benzyl pentanedioic acid
-
IC50: 0.5 mg/l, minimum inhibitor concentration: 0.24 mg/l
(2R,4S)-2-amino-4-[4-(2-benzo[b]thienyl)]benzyl pentanedioic acid
-
IC50: 0.65 mg/l, minimum inhibitor concentration: 3.9 mg/l
(2R,4S)-2-amino-4-[4-(2-naphthyl)]benzyl pentanedioic acid
-
IC50: 0.42 mg/l, minimum inhibitor concentration: 7.8 mg/l
(2R,4S)-2-amino-4-[4-(3-thienyl)]benzyl pentanedioic acid
-
IC50: 0.32 mg/l, minimum inhibitor concentration: 0.24 mg/l
(2R,4S)-2-amino-4-[4-(n-benzenesulfonylamino)]benzyl pentanedioic acid
-
IC50: 10.2 mg/l, minimum inhibitor concentration: above 250 mg/l
(2R,4S)-2-amino-4-[4-(N-phenylaminocarbonyl)amino]-benzyl pentanedioic acid
-
IC50: 0.49 mg/l, minimum inhibitor concentration: 15.6 mg/l
(2R,4S,E)-2-amino-4-(3-phenylprop-2-enyl) pentanedioic acid
-
IC50: 0.1 mg/l, minimum inhibitor concentration: 0.4 mg/l
(2R,4S,E)-2-amino-4-(3-phenylprop-2-enyl)pentanedioic acid
-
D-glutamate analog, good competitive inhibitor for RacE1; D-glutamate analog, only weak inhibitor of RacE2, but a potent competitive inhibitor for mutant V149A
(2R,4S,E)-2-amino-4-[3-(2-naphthyl)prop-2-enyl]pentanedioic acid
-
IC50: 0.5 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2S,4R)-2-amino-4-benzyl pentanedioic acid
-
IC50: 0.3 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2S,4S)-2-amino-4-(1-naphthyl)methyl pentanedioic acid
-
IC50: 5.6 mg/l, minimum inhibitor concentration: 3.9 mg/l
(4R,2S)-2-cinnamyl-4-amino-5-hydroxypentanoic acid
-
D-glutamate analog, good competitive inhibitor for RacE1; D-glutamate analog, only weak inhibitor of RacE2, but a potent competitive inhibitor for mutant V149A
1-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)-3-(4-nitrophenyl)thiourea
-
-
1-(4-chlorophenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)thiourea
-
Binding pose and the interaction pattern of the compound, non-competitive inhibition
1-(4-chlorophenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)urea
-
-
1-(4-fluorophenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)thiourea
-
-
1-(4-fluorophenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)urea
-
-
1-(4-methoxyphenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)urea
-
-
2-(2-Carboxyethyl)aziridine-2-carboxylic acid
-
i.e. aziridino-glutamate, inactivates glutamate racemase by alkylating an active site Cys residue
2-[(5-chloro-1-methyl-1H-indol-3-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-[1-methyl-4-(methylsulfonyl)-1H-pyrrol-2-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
analysis of mouse and human internal clearance
2-[(6-chloroquinolin-4-yl)methyl]-5,7-bis(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-5-cyclopropyl-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-5-methyl-3-(1-methyl-1H-imidazol-5-yl)-7-(2-methylpropyl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-5-methyl-7-(2-methylpropyl)-3-(1-methyl-1H-pyrrol-2-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-(pent-4-yn-2-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-(prop-2-en-1-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-(prop-2-yn-1-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-(propan-2-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-[4-(morpholin-4-yl)but-2-yn-1-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-(3-hydroxyprop-2-yn-1-yl)-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-ethyl-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(1-methyl-1H-1,2,4-triazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(4-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(4-methyl-1H-pyrazol-3-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(4-methyl-4H-1,2,4-triazol-3-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-[1-methyl-4-(methylsulfonyl)-1H-pyrrol-2-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
2-[2-[(6-chloroquinolin-4-yl)methyl]-5,7-bis(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
-
-
2-[2-[(6-chloroquinolin-4-yl)methyl]-5-cyclopropyl-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
-
-
2-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(prop-2-en-1-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
-
-
2-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(prop-2-yn-1-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
-
-
2-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-ethyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
-
-
2-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
-
-
3-(2-amino-4-methyl-1,3-thiazol-5-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
3-(2-amino-5-methyl-1,3-thiazol-4-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
3-(3-chlorothiophen-2-yl)-5-(furan-2-yl)-N-methyl-3H-pyrido[2,3-e][1,4]diazepin-2-amine
-
uncompetitive, inhibitor with improved solubility and reduced plasma protein binding, binds at the enzyme dimer interface
3-(4-acetyl-1-methyl-1H-pyrrol-2-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
4-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-5-methylfuran-2-carbonitrile
-
-
5-(but-2-yn-1-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
5-(furan-2-yl)-N-methyl-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
-
uncompetitive, inhibitor with improved solubility and reduced plasma protein binding, binds at the enzyme dimer interface
5-methyl-7-(2-methylpropyl)-2-(naphthalen-1-ylmethyl)-3-(pyridin-4-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
5-methyl-7-(2-methylpropyl)-2-(naphthalen-1-ylmethyl)-3-pyridin-4-yl-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
5-[2-[(6-chloro-1,2-dihydroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
pyrazolopyrimidinedione inhibits growth of Helicobacter pylori specifically, inhibition of enzyme results in inhibition of peptidoglycan biosynthesis, minimum inhibitory concentration in wild-type strains SS1 and ARHp80 is 1 and 0.5 microg/ml
5-[2-[(6-chloroquinolin-4-yl)methyl]-5,7-bis(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-5-(cyanomethyl)-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-5-cyclopropyl-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-5-methyl-7-(2-methylpropyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(prop-2-en-1-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(prop-2-yn-1-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(propan-2-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-[2-(1H-1,2,3-triazol-1-yl)ethyl]-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-[2-(1H-pyrazol-1-yl)ethyl]-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-[4-(1H-1,2,4-triazol-1-yl)but-2-yn-1-yl]-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-[4-(1H-pyrazol-1-yl)but-2-yn-1-yl]-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-(2-hydroxyethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-(4-hydroxybut-2-yn-1-yl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-ethyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-4-methylfuran-2-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-[4-(1H-imidazol-1-yl)but-2-yn-1-yl]-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-[4-(morpholin-4-yl)but-2-yn-1-yl]-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-[5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl]-1H-pyrrole-3-sulfonamide
-
analysis of mouse and human internal clearance
5-[5-(but-2-yn-1-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[5-(but-3-yn-2-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
-
-
5-[7-(cyclopropylmethyl)-5-methyl-2-[(5-methyl-1H-indol-3-yl)methyl]-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-N-methoxy-1-methyl-1H-pyrrole-3-carboxamide
-
pyrazolopyrimidinedione inhibits growth of Helicobacter pylori specifically, inhibition of enzyme results in inhibition of peptidoglycan biosynthesis, minimum inhibitory concentration in wild-type strains SS1 and ARHp80 is 16 microg/ml
6-chloro-4-([7-(cyclopropylmethyl)-5-methyl-3-[1-methyl-4-(methylsulfinyl)-1H-pyrrol-2-yl]-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl]methyl)isoquinoline-3-carbonitrile
-
pyrazolopyrimidinedione inhibits growth of Helicobacter pylori specifically, inhibition of enzyme results in inhibition of peptidoglycan biosynthesis, minimum inhibitory concentration in wild-type strains SS1 and ARHp80 is 16 and 8 microg/ml
6-chloro-4-[[3-(4-cyano-1-methyl-1H-pyrrol-2-yl)-7-(cyclopropylmethyl)-4,6-dioxo-5-prop-2-yn-1-yl-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-2-yl]methyl]isoquinoline-3-carbonitrile
-
pyrazolopyrimidinedione inhibits growth of Helicobacter pylori specifically, inhibition of enzyme results in inhibition of peptidoglycan biosynthesis, minimum inhibitory concentration in wild-type strains SS1 and ARHp80 is 2 and 1 microg/ml
9-(2,6-difluoro-3-methylbenzyl)-2-[(1,1,1,2,2-pentafluoropentan-3-yl)oxy]-9H-purin-6-amine
beta-chloro-L-alanine
-
BCLA, modifies BsMurI predominantly at C74, the cysteine residue responsible for deprotonation of an incoming D-Glu substrate
bis(2,4-bis (trichloromethyl)-1,3,5-triazapentadienato)-Zn(II) complex
-
binding structure, overview
-
D-glutamate
-
MurI of Helicobacter pylori is strongly inhibited by D-glutamate
D-N-Hydroxyglutamate
-
the compound acts as alternate substrate and is converted into 2-oxoglutarate and NH4+. Km: 0.057 mM, turnover number: 1080 min-1. An imine intermediate is likely the species causing the inhibition
exiguaquinol
-
pentacyclic hydroquinone from Neopetrosia exigua, protein-ligand modeling
gamma-2-naphthylmethyl-D-glutamate
potent competitive inhibitor that induces a disorder in one of the loops near the active site
L-serine-O-sulfate
-
suicide substrate. The glutamate racemase catalyzes alpha,beta-elimination of L-serine O-sulfate to produce a pyruvate concomitantly with an irreversible inactivation of the enzyme
N,8-dimethyl-5-phenyl-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
-
uncompetitive, inhibitor with improved solubility and reduced plasma protein binding, binds at the enzyme dimer interface
N-methyl-3,5-di(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
-
uncompetitive, inhibitor with improved solubility and reduced plasma protein binding, binds at the enzyme dimer interface
N-methyl-5-(1H-pyrrol-3-yl)-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
-
uncompetitive, inhibitor with improved solubility and reduced plasma protein binding, binds at the enzyme dimer interface
N-methyl-5-phenyl-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
-
uncompetitive, inhibitor with improved solubility and reduced plasma protein binding, binds at the enzyme dimer interface
tetracycline
-
inhibition of enzyme results in inhibition of peptidoglycan biosynthesis, minimum inhibitory concentration in wild-type strains SS1 and ARHp80 is 0.25 and 0.13 microg/ml
tris(2,4-bis(trichloromethyl)-1,3,5-triazapentadienate)-Mn(III) complex
-
binding structure, overview
[2-[(6-chloro-1,2-dihydroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-4,6-dioxo-2,4,6,7-tetrahydro-5H-pyrazolo[3,4-d]pyrimidin-5-yl]acetonitrile
-
pyrazolopyrimidinedione inhibits growth of Helicobacter pylori specifically, inhibition of enzyme results in inhibition of peptidoglycan biosynthesis, minimum inhibitory concentration in wild-type strains SS1 and ARHp80 is 2 and 1 microg/ml
(2R,4S)-2-amino-4-(2-naphthyl)methyl pentanedioic acid
-
D-glutamate analog, good competitive inhibitor for RacE1; D-glutamate analog, only weak inhibitor of RacE2, but a potent competitive inhibitor for mutant V149A
(2R,4S)-2-amino-4-(2-naphthyl)methyl pentanedioic acid
-
IC50: 0.1 mg/l, minimum inhibitor concentration: 0.25 mg/l
2-(butylsulfanyl)-8-(4-fluorobenzyl)-4-(methylamino)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Staphylococcus aureus
2-(butylsulfanyl)-8-(4-fluorobenzyl)-4-(methylamino)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Enterococcus faecalis
2-(butylsulfanyl)-9-(2-methoxy-5-nitrobenzyl)-9H-purin-6-amine
comparison with effect on Enterococcus faecium and Staphylococcus aureus
2-(butylsulfanyl)-9-(2-methoxy-5-nitrobenzyl)-9H-purin-6-amine
comparison with effect on Enterococcus faecalis and Staphylococcus aureus
2-(butylsulfanyl)-9-(2-methoxy-5-nitrobenzyl)-9H-purin-6-amine
-
analysis of mouse and human internal clearance
2-(butylsulfanyl)-9-(3-chloro-2,6-difluorobenzyl)-9H-purin-6-amine
comparison with effect on Enterococcus faecium and Staphylococcus aureus
2-(butylsulfanyl)-9-(3-chloro-2,6-difluorobenzyl)-9H-purin-6-amine
comparison with effect on Enterococcus faecalis and Staphylococcus aureus
2-(butylsulfanyl)-9-(4-nitrophenyl)-9H-purin-6-amine
-
comparison with effect on enzyme from Staphylococcus aureus
2-(butylsulfanyl)-9-(4-nitrophenyl)-9H-purin-6-amine
-
comparison with effect on enzyme from Enterococcus faecalis and Staphylococcus aureus
2-(butylsulfanyl)-9-(4-nitrophenyl)-9H-purin-6-amine
-
comparison with effect on enzyme from Enterococcus faecalis
2-butoxy-9-(3-chloro-2,6-difluorobenzyl)-N-(pyridin-3-ylmethyl)-9H-purin-6-amine
comparison with effect on Enterococcus faecium and Staphylococcus aureus
2-butoxy-9-(3-chloro-2,6-difluorobenzyl)-N-(pyridin-3-ylmethyl)-9H-purin-6-amine
comparison with effect on Enterococcus faecalis and Staphylococcus aureus
2-butoxy-9-(3-chloro-2,6-difluorobenzyl)-N-(pyridin-3-ylmethyl)-9H-purin-6-amine
-
-
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-[1-methyl-4-(methylsulfonyl)-1H-pyrrol-2-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
analysis of mouse and human internal clearance
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-[1-methyl-4-(methylsulfonyl)-1H-pyrrol-2-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
-
4-amino-2-(butylsulfanyl)-8-(2,6-difluorobenzyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Staphylococcus aureus
4-amino-2-(butylsulfanyl)-8-(2,6-difluorobenzyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Enterococcus faecalis
4-amino-2-(butylsulfanyl)-8-(3,4-dichlorobenzyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Staphylococcus aureus
4-amino-2-(butylsulfanyl)-8-(3,4-dichlorobenzyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Enterococcus faecalis
4-amino-2-(butylsulfanyl)-8-(4-fluorobenzyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Staphylococcus aureus
4-amino-2-(butylsulfanyl)-8-(4-fluorobenzyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Enterococcus faecalis
4-amino-8-benzyl-2-(benzylsulfanyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Staphylococcus aureus
4-amino-8-benzyl-2-(benzylsulfanyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Enterococcus faecalis
4-amino-8-benzyl-2-(butylsulfanyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Staphylococcus aureus
4-amino-8-benzyl-2-(butylsulfanyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Enterococcus faecalis
4-amino-8-benzyl-2-(cyclopentylsulfanyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Staphylococcus aureus
4-amino-8-benzyl-2-(cyclopentylsulfanyl)-5,8-dihydropteridine-6,7-dione
-
comparison with effect on enzyme from Enterococcus faecalis
5-methyl-7-(2-methylpropyl)-2-(naphthalen-1-ylmethyl)-3-pyridin-4-yl-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
a pyrazolopyrimidinedione analogue identified by a high-throughput screen demonstrates inhibition with excellent selectivity for MurI of Helicobacter pylori, it is time-independent, fully-reversible and insensitive to changes in enzyme or detergent concentration
5-methyl-7-(2-methylpropyl)-2-(naphthalen-1-ylmethyl)-3-pyridin-4-yl-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
-
pyrazolopyrimidinedione inhibits growth of Helicobacter pylori specifically, inhibition of enzyme results in inhibition of peptidoglycan biosynthesis, minimum inhibitory concentration in wild-type strains SS1 and ARHp80 is 4 microg/ml
9-(2,6-difluoro-3-methylbenzyl)-2-[(1,1,1,2,2-pentafluoropentan-3-yl)oxy]-9H-purin-6-amine
comparison with effect on Enterococcus faecium and Staphylococcus aureus
9-(2,6-difluoro-3-methylbenzyl)-2-[(1,1,1,2,2-pentafluoropentan-3-yl)oxy]-9H-purin-6-amine
comparison with effect on Enterococcus faecalis and Staphylococcus aureus
beta-Chloro-D-alanine
-
BCDA, its primary target is glutamate racemase, poor activity oagainst alanine racemase activity, potent antituberculosis activity. BCDA does not inhibit the D-alanine pathway in intact cells, consistent with its poor in vitro activity, it is instead an irreversible mechanism-based inactivator of glutamate racemase (MurI), an upstream enzyme in the same early stage of peptidoglycan biosynthesis. Inhibition kinetics, overview. BCDA-treated BsMurI has a single cysteine residue, C185, that is the sole site of modification in over 95% of the inactivated protein. BCDA inhibition of MurI is mechanism-based as opposed to arising from nonspecific interaction with suitably configured cysteine thiols
beta-Chloro-D-alanine
-
BCDA, its primary target is glutamate racemase, poor activity oagainst alanine racemase activity, potent antituberculosis activity. BCDA does not inhibit the D-alanine pathway in intact cells, consistent with its poor in vitro activity, it is instead an irreversible mechanism-based inactivator of glutamate racemase (MurI), an upstream enzyme in the same early stage of peptidoglycan biosynthesis. Inhibition kinetics, overview. BCDA modifies MtMurI in vitro and in vivo
dipicolinic acid
-
allosteric inhibitor of both Bacillus anthracis glutamate racemase isozymes which exhibits low micromolar inhibition with clear noncompetitive behavior
hydroxylamine
-
different experimentators found inhibition or no inhibition
additional information
-
the pressure does not affect catalysis after substrate binding
-
additional information
-
no inhibition by beta-fluoroalanine (BFA, racemic mixture) and O-acetyl-D-serine (OADS)
-
additional information
-
library screening for inhibitory compounds, two Zn (II) and Mn (III) 1,3,5-triazapentadienate complexes are found to efficiently inhibit the glutamate racemase activity. The metal complexes affect the enzyme activity by binding to the enzyme-substrate complex and promoting the formation of an inhibited dimeric form of the enzyme. Evaluation of a series of compounds, including 1H-benzimidazole-2-sulfonic acid, dipicolinic acid, 4-hydroxybenzene-1,3-disulfonate, and (2R)-2-amino-4-benzylpentanedioic acid, which are already known inhibitors of different bacterial glutamate racemases, for inhibitory activity on the enzyme, inhibition mechanism of BcGR by metal complexes, overview
-
additional information
-
in contrast to MurI of Helicobacter pylori no inhibition by D-glutamate
-
additional information
-
substrate-product analogue inhibitor synthesis and evaluation, overview
-
additional information
-
in contrast to MurI of Helicobacter pylori no inhibition by D-glutamate
-
additional information
-
in contrast to MurI of Helicobacter pylori no inhibition by D-glutamate
-
additional information
although Tris-HCl isthe buffer most commonly employed when assaying glutamate racemases from various microbial sources, FnGR is slightly inhibited in this buffer, kcat values are reduced 14% and 25% in the L-D and D-L reaction directions at pH 8.0, respectively relative to the corresponding values observed using the phosphate assay buffer
-
additional information
-
design of inhibitors of glutamate racemase as selective antibacterial agents, incorporation of imidazoles onto a core pyrazolopyrimidinedione scaffold to improve bioavailabilty, structure-activity relationships, MIC values with wild-type Helicobacter pylori strain 055 and mutant strain hefC-, overview. Substituents on the inhibitor scaffold are varied to optimize target potency, antibacterial activity, and in vivo pharmacokinetic stability
-
additional information
-
insensitive to carbonyl reagents such as hydroxylamine, phenylhydrazine, or NaBH4
-
additional information
-
no inhibition by beta-fluoroalanine (BFA, racemic mixture) and O-acetyl-D-serine (OADS). MtMurI adopts a unique oligomeric configuration and contains distinct active-site architectural differences from other MurI orthologues and that dimer interface mutations are required to introduce catalytic capability. Conventional MurI inhibitors are inactive against this recombinant form of mycobacterial MurI, the selective inhibitory activity of BCDA against MtMurI may arise from unique protein-ligand interactions unseen in orthologous MurIs. MsMurI results demonstrate these same structural features and yet BCDA does not appear to act via MurI in this bacterium
-
additional information
-
inhibitor screening, compounds designed to target other glutamate racemases have been screened but do not inhibit mycobacterial MurI, suggesting that a different drug design effort will be needed to develop inhibitors. A distinct type of MurI dimer arrangement is observed in both structures, and this arrangement becomes the third biological dimer geometry for MurI found
-
additional information
-
development of a class of Mycobacterium tuberculosis (Mtb) inhibitors by exploring the pharmaceutically underexploited enzyme targets which are majorly involved in cell wall biosynthesis of mycobacteria, compoud library screening using a thermal shift assay. Identification of two lead compounds, optimization and expansion result in twenty four compounds. Molecular docking and dynamic studies using the D-glutamate bound glutamate racemase structures of Mycobacterium tuberculosis (PDB ID 5HJ7) and Bacillus subtilis (PDB ID 1ZUW), simulations and modeling, overview. The compounds are also tested on their cytotoxicity and in a Myconacterium tuberculosis biofilm assay, activity profile of compounds in nutrient starved stress model, overview
-
additional information
-
inhibitor screening, compounds designed to target other glutamate racemases have been screened but do not inhibit mycobacterial MurI, suggesting that a different drug design effort will be needed to develop inhibitors. A distinct type of MurI dimer arrangement is observed in both structures, and this arrangement becomes the third biological dimer geometry for MurI found
-
additional information
-
no inactivation by carbonyl reagents such as hydroxylamine and NaBH4
-
additional information
-
in contrast to MurI of Helicobacter pylori no inhibition by D-glutamate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
UDP-MurNAc-Ala
-
strong activation by UDP-MurNAc-Ala, the product of the preceding enzyme in the peptidoglycan biosynthetic pathway
additional information
-
the pressure does not affect catalysis after substrate binding
-
additional information
-
in contrast to Escherichia coli no activation by UDP-MurNAc-Ala, the product of the preceding enzyme in the peptidoglycan biosynthetic pathway
-
additional information
-
in contrast to Escherichia coli no activation by UDP-MurNAc-Ala, the product of the preceding enzyme in the peptidoglycan biosynthetic pathway
-
additional information
-
in contrast to Escherichia coli no activation by UDP-MurNAc-Ala, the product of the preceding enzyme in the peptidoglycan biosynthetic pathway
-
additional information
-
not stimulated by the addition of pyridoxal 5'-phosphate
-
additional information
-
pyridoxal phosphate-independent enzyme
-
additional information
-
in contrast to Escherichia coli no activation by UDP-MurNAc-Ala, the product of the preceding enzyme in the peptidoglycan biosynthetic pathway
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
26
L-2-aminoadipic acid
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
4.2
D-Glu
-
in presence of 0.0065 mM of the activator UDP-N-acetylmuramyl-L-Ala
0.07
D-glutamate
-
recombinant wild type enzyme, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/mL diaphorase, and 0.05 mM D-glutamate
0.1
D-glutamate
-
mutant Q86A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.13
D-glutamate
-
mutant Y221A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.14
D-glutamate
-
mutant R25A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.16
D-glutamate
-
mutant R214A/K106A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.17
D-glutamate
-
mutant P99A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.25
D-glutamate
-
mutant K29A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.25
D-glutamate
wild type enzyme, at 25 °C in 50 mM Tris-HCl (pH 8.0), 5 mM NAD+, 0.5 mM iodonitrotetrazolium chloride, 2.5 mM ADP, 20 units of L-glutamate dehydrogenase, 2 units of diaphorase and D-glutamate
0.3
D-glutamate
-
mutant R214A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.42
D-glutamate
-
mutant K106A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
1.5
D-glutamate
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
1.7
D-glutamate
-
His-tagged recombinant BsGR, in potassium phosphate buffer (10 mM, pH 8.0)
1.7
D-glutamate
recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
8.6
D-glutamate
mutant T76A, at 25 °C in 50 mM Tris-HCl, pH 8.0, 5 mM NAD+, 0.5 mM iodonitrotetrazolium chloride, 2.5 mM ADP, 20 units of L-glutamate dehydrogenase, 2 units of diaphorase and D-glutamate
10
D-glutamate
-
His-tagged recombinant BsGR mutant V149A, in potassium phosphate buffer (10 mM, pH 8.0)
0.25
L-glutamate
-
wild-type enzyme, pH and temperature not specified in the publication
0.74
L-glutamate
-
demonstrates a high degree of asymmetry in substrate processing with the Michaelis constant for D-glutamate approximately tenfold lower than for L-glutamate
0.9
L-glutamate
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
1.04
L-glutamate
recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
4.1
L-glutamate
-
mutant P99A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
5.8
L-glutamate
-
mutant R25A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
6.1
L-glutamate
-
recombinant RacE2 wild type enzyme, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
7.2
L-glutamate
-
mutant K29A, in 10 mM potassium phosphate (pH 8.2)and 0.2 mM dithiothreitol
8.8
L-glutamate
-
mutant Q86A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
9.9
L-glutamate
-
mutant Y221A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
10.1
L-glutamate
-
mutant R214A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
10.8
L-glutamate
-
mutant K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
11
L-glutamate
-
mutant R214A/K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
14
L-glutamate
-
His-tagged recombinant BsGR, in potassium phosphate buffer (10 mM, pH 8.0)
14
L-glutamate
wild type enzyme, 50 mM boric acid, 100 mM KCl, 0.2 mM dithiothreitol, pH 8.0 at 25°C in the presence of 0.22 microM glutamate racemase
47
L-glutamate
-
His-tagged recombinant BsGR mutant V149A, in potassium phosphate buffer (10 mM, pH 8.0)
additional information
additional information
-
mutant V149A has a Km value for L-glutamate similar to that of RacE2 (4.6 mM versus 3.7 mM). In the reverse reaction, the Km of V149A for D-glutamate is the same as that of RacE2 (0.2 mM)
-
additional information
additional information
-
recombinant enzyme, steady state kinetic analysis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.4
L-2-aminoadipic acid
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
additional information
additional information
-
mutant V149A has about a 2fold higher kcat than wild-type RacE2 (67/sec versus 38/sec). In the reverse reaction, V149A has a higher kcat than RacE2 (4.9/sec versus 1.6/sec, respectively)
-
0.43
D-glutamate
mutant T76A, at 25°C in 50 mM Tris-HCl (pH 8.0), 5 mM NAD+, 0.5 mM iodonitrotetrazolium chloride, 2.5 mM ADP, 20 units of L-glutamate dehydrogenase, 2 units of diaphorase and D-glutamate
1.3
D-glutamate
wild type enzyme, at 25°C in 50 mM Tris-HCl, pH 8.0, 5 mM NAD+, 0.5 mM iodonitrotetrazolium chloride, 2.5 mM ADP, 20 units of L-glutamate dehydrogenase, 2 units of diaphorase and D-glutamate
8.3
D-glutamate
-
His-tagged recombinant BsGR, in potassium phosphate buffer (10 mM, pH 8.0)
15
D-glutamate
-
His-tagged recombinant BsGR mutant V149A, in potassium phosphate buffer (10 mM, pH 8.0)
22
D-glutamate
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
26
D-glutamate
recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
780
D-glutamate
-
recombinant wild type enzyme, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
2160
D-glutamate
-
mutant Q86A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
2760
D-glutamate
-
mutant Y221A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
5220
D-glutamate
-
mutant K106A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
6660
D-glutamate
-
mutant R214A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
7440
D-glutamate
-
mutant K29A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
7560
D-glutamate
-
mutant R25A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
7680
D-glutamate
-
mutant P99A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
7980
D-glutamate
-
mutant R214A/K106A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
1.3
L-glutamate
-
wild-type enzyme, pH and temperature not specified in the publication
13.8
L-glutamate
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
17.4
L-glutamate
recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
63
L-glutamate
-
His-tagged recombinant BsGR, in potassium phosphate buffer (10 mM, pH 8.0)
76
L-glutamate
-
His-tagged recombinant BsGR mutant V149A, in potassium phosphate buffer (10 mM, pH 8.0)
87
L-glutamate
wild type enzyme, 50 mM boric acid, 100 mM KCl, 0.2 mM dithiothreitol, pH 8.0, at 25°C in the presence of 0.22 microM glutamate racemase
116600
L-glutamate
-
recombinant wild type enzyme, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
144000
L-glutamate
-
mutant Q86A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
164400
L-glutamate
-
mutant P99A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
219600
L-glutamate
-
mutant K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
252000
L-glutamate
-
mutant Y221A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
278400
L-glutamate
-
mutant R214A/K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
294000
L-glutamate
-
mutant R25A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
306000
L-glutamate
-
mutant K29A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
355200
L-glutamate
-
mutant R214A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.09
L-2-aminoadipic acid
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
0.0031
D-glutamate
-
recombinant wild type enzyme, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.0035
D-glutamate
-
mutant K106A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.0059
D-glutamate
-
mutant Y221A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.006
D-glutamate
-
mutant Q86A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.0062
D-glutamate
-
mutant R214A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.0083
D-glutamate
-
mutant K29A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.0125
D-glutamate
-
mutant P99A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.0139
D-glutamate
-
mutant R214A/K106A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
0.015
D-glutamate
-
mutant R25A, reactions are conducted at 25°C in the assay mixture that contains 5 mM NAD+, 2.5 mM ADP, 50 mM CHES buffer (pH 9.2), 0.65 mM iodonitrotetrazolium chloride, 37.5 units/ml L-glutamate dehydrogenase, 2 units/ml diaphorase, and 0.05 mM D-glutamate
1.5
D-glutamate
-
His-tagged recombinant BsGR mutant V149A, in potassium phosphate buffer (10 mM, pH 8.0)
4
D-glutamate
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
5
D-glutamate
-
His-tagged recombinant BsGR, in potassium phosphate buffer (10 mM, pH 8.0)
15
D-glutamate
recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
0.0045
L-glutamate
-
mutant Q86A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
0.0053
L-glutamate
-
recombinant wild type enzyme, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
0.0056
L-glutamate
-
mutant K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
0.007
L-glutamate
-
mutant R214A/K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
0.0071
L-glutamate
-
mutant Y221A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
0.0098
L-glutamate
-
mutant R214A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
0.0111
L-glutamate
-
mutant P99A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
0.0118
L-glutamate
-
mutant K29A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
0.014
L-glutamate
-
mutant R25A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
1.8
L-glutamate
-
His-tagged recombinant BsGR mutant V149A, in potassium phosphate buffer (10 mM, pH 8.0)
4.6
L-glutamate
-
His-tagged recombinant BsGR, in potassium phosphate buffer (10 mM, pH 8.0)
15
L-glutamate
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
17
L-glutamate
recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.1
(R,S)-1-hydroxy-1-oxo-4-amino-4-carboxyphosphorinane
-
pH and temperature not specified in the publication
18.4
1,1-dioxo-tetrahydrothiopyran-4-one
-
pH and temperature not specified in the publication
0.042
2-hydroxy-3,4,5-trioxocyclopent-1-en-1-olate
-
pH and temperature not specified in the publication
0.059
benzene-1,3-disulfonate
-
pH and temperature not specified in the publication
0.0003
(2R,4S)-2-amino-4-(2-naphthyl)methyl pentanedioic acid
-
potent competitive inhibitor for RacE2 mutant V149A
0.0046
(2R,4S)-2-amino-4-(2-naphthyl)methyl pentanedioic acid
-
D-glutamate analog, good competitive inhibitor for RacE1
0.289
(2R,4S)-2-amino-4-(2-naphthyl)methyl pentanedioic acid
-
D-glutamate analog, only weak inhibitor of RacE2
0.0002
(2R,4S,E)-2-amino-4-(3-phenylprop-2-enyl)pentanedioic acid
-
potent competitive inhibitor for RacE2 mutant V149A
0.0035
(2R,4S,E)-2-amino-4-(3-phenylprop-2-enyl)pentanedioic acid
-
D-glutamate analog, good competitive inhibitor for RacE1
0.064
(2R,4S,E)-2-amino-4-(3-phenylprop-2-enyl)pentanedioic acid
-
D-glutamate analog, only weak inhibitor of RacE2
0.0002
(4R,2S)-2-cinnamyl-4-amino-5-hydroxypentanoic acid
-
potent competitive inhibitor for RacE2 mutant V149A
0.0015
(4R,2S)-2-cinnamyl-4-amino-5-hydroxypentanoic acid
-
D-glutamate analog, good competitive inhibitor for RacE1
0.073
(4R,2S)-2-cinnamyl-4-amino-5-hydroxypentanoic acid
-
D-glutamate analog, only weak inhibitor of RacE2
0.075
dipicolinic acid
-
isozyme RacE1, pH and temperature not specified in the publication
0.092
dipicolinic acid
-
isozyme RacE2, pH and temperature not specified in the publication
1.236
dipicolinic acid
-
RacE2 mutant enzyme S207A, pH and temperature not specified in the publication
2.342
dipicolinic acid
-
RacE2 mutant enzyme K106A, pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
24.1
(R,S)-1-hydroxy-1-oxo-4-amino-4-carboxyphosphorinane
Enterococcus faecalis
-
pH and temperature not specified in the publication
215
(R,S)-4-amino-4-carboxy-1,1-dioxotetrahydro-thiopyran
Enterococcus faecalis
-
pH and temperature not specified in the publication
21.2
1,1-dioxo-tetrahydrothiopyran-4-one
Enterococcus faecalis
-
pH and temperature not specified in the publication
0.0068
1-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)-3-(4-nitrophenyl)thiourea
Mycobacterium tuberculosis
-
pH 8.0, 37°C, recombinant enzyme
0.025
1-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)-3-(p-tolyl)thiourea
Mycobacterium tuberculosis
-
above, pH 8.0, 37°C, recombinant enzyme
0.0088
1-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)-3-phenylthiourea
Mycobacterium tuberculosis
-
pH 8.0, 37°C, recombinant enzyme
0.025
1-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)-3-phenylurea
Mycobacterium tuberculosis
-
above, pH 8.0, 37°C, recombinant enzyme
0.025
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-chlorophenyl)thiourea
Mycobacterium tuberculosis
-
above, pH 8.0, 37°C, recombinant enzyme
0.0115
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-chlorophenyl)urea
Mycobacterium tuberculosis
-
pH 8.0, 37°C, recombinant enzyme
0.0011
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-fluorophenyl)thiourea
Mycobacterium tuberculosis
-
pH 8.0, 37°C, recombinant enzyme
0.00182
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-fluorophenyl)urea
Mycobacterium tuberculosis
-
pH 8.0, 37°C, recombinant enzyme
0.025
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-methoxyphenyl)urea
Mycobacterium tuberculosis
-
above, pH 8.0, 37°C, recombinant enzyme
0.0044
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-nitrophenyl)thiourea
Mycobacterium tuberculosis
-
pH 8.0, 37°C, recombinant enzyme
0.025
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(4-nitrophenyl)urea
Mycobacterium tuberculosis
-
above, pH 8.0, 37°C, recombinant enzyme
0.025
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(p-tolyl)thiourea
Mycobacterium tuberculosis
-
above, pH 8.0, 37°C, recombinant enzyme
0.00835
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-(p-tolyl)urea
Mycobacterium tuberculosis
-
pH 8.0, 37°C, recombinant enzyme
0.0013
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-benzylthiourea
Mycobacterium tuberculosis
-
pH 8.0, 37°C, recombinant enzyme
0.025
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-benzylurea
Mycobacterium tuberculosis
-
above, pH 8.0, 37°C, recombinant enzyme
0.00712
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-isopropylurea
Mycobacterium tuberculosis
-
pH 8.0, 37°C, recombinant enzyme
0.025
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-phenylthiourea
Mycobacterium tuberculosis
-
above, pH 8.0, 37°C, recombinant enzyme
0.025
1-(3-(benzo[d]oxazol-2-yl)phenyl)-3-phenylurea
Mycobacterium tuberculosis
-
above, pH 8.0, 37°C, recombinant enzyme
0.025
1-(4-chlorophenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)thiourea
Mycobacterium tuberculosis
-
above, pH 8.0, 37°C, recombinant enzyme
0.025
1-(4-chlorophenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)urea
Mycobacterium tuberculosis
-
above, pH 8.0, 37°C, recombinant enzyme
0.0228
1-(4-fluorophenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)thiourea
Mycobacterium tuberculosis
-
pH 8.0, 37°C, recombinant enzyme
0.0085
1-(4-fluorophenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)urea
Mycobacterium tuberculosis
-
pH 8.0, 37°C, recombinant enzyme
0.025
1-(4-methoxyphenyl)-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)urea
Mycobacterium tuberculosis
-
above, pH 8.0, 37°C, recombinant enzyme
0.025
1-benzyl-3-(3-(5-methylbenzo[d]oxazol-2-yl)phenyl)thiourea
Mycobacterium tuberculosis
-
above, pH 8.0, 37°C, recombinant enzyme
47.7
1-hydroxyphosphinan-4-one 1-oxide
Enterococcus faecalis
-
pH and temperature not specified in the publication
0.0009 - 0.0038
2-(butylsulfanyl)-8-(4-fluorobenzyl)-4-(methylamino)-5,8-dihydropteridine-6,7-dione
105
2-amino-4-phosphonobutanoic acid
Enterococcus faecalis
-
pH and temperature not specified in the publication
0.000026 - 0.0027
2-butoxy-9-(3-chloro-2,6-difluorobenzyl)-N-(pyridin-3-ylmethyl)-9H-purin-6-amine
0.000033
2-[(5-chloro-1-methyl-1H-indol-3-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-[1-methyl-4-(methylsulfonyl)-1H-pyrrol-2-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
-
0.000069
2-[(6-chloroquinolin-4-yl)methyl]-5,7-bis(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000079
2-[(6-chloroquinolin-4-yl)methyl]-5-cyclopropyl-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00017
2-[(6-chloroquinolin-4-yl)methyl]-5-methyl-3-(1-methyl-1H-imidazol-5-yl)-7-(2-methylpropyl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00026
2-[(6-chloroquinolin-4-yl)methyl]-5-methyl-7-(2-methylpropyl)-3-(1-methyl-1H-pyrrol-2-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00046
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-(pent-4-yn-2-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000056
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-(prop-2-en-1-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000024
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-(prop-2-yn-1-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00022
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-(propan-2-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00017
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-5-[4-(morpholin-4-yl)but-2-yn-1-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000054
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-(3-hydroxyprop-2-yn-1-yl)-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000072
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-ethyl-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00081
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(1-methyl-1H-1,2,4-triazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000041
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.0009
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(4-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00022
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(4-methyl-1H-pyrazol-3-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00023
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-(4-methyl-4H-1,2,4-triazol-3-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000034
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-[1-methyl-4-(methylsulfonyl)-1H-pyrrol-2-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
0.00015
2-[2-[(6-chloroquinolin-4-yl)methyl]-5,7-bis(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00025
2-[2-[(6-chloroquinolin-4-yl)methyl]-5-cyclopropyl-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00025
2-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(prop-2-en-1-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000089
2-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(prop-2-yn-1-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00018
2-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-ethyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000087
2-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-imidazole-4-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00074
3-(2-amino-4-methyl-1,3-thiazol-5-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00028
3-(2-amino-5-methyl-1,3-thiazol-4-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.0028
3-(3-chlorothiophen-2-yl)-5-(furan-2-yl)-N-methyl-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Helicobacter pylori
-
-
0.000039
3-(4-acetyl-1-methyl-1H-pyrrol-2-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.007
3-(5-methylbenzo[d]oxazol-2-yl)aniline
Mycobacterium tuberculosis
-
pH 8.0, 37°C, recombinant enzyme
-
0.025
3-(benzo[d]oxazol-2-yl)aniline
Mycobacterium tuberculosis
-
above, pH 8.0, 37°C, recombinant enzyme
-
0.0015 - 0.0031
4-amino-2-(butylsulfanyl)-8-(2,6-difluorobenzyl)-5,8-dihydropteridine-6,7-dione
0.00065 - 0.0015
4-amino-2-(butylsulfanyl)-8-(3,4-dichlorobenzyl)-5,8-dihydropteridine-6,7-dione
0.0011 - 0.0035
4-amino-2-(butylsulfanyl)-8-(4-fluorobenzyl)-5,8-dihydropteridine-6,7-dione
0.00022
4-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-5-methylfuran-2-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000063
5-(but-2-yn-1-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-3-(1-methyl-1H-imidazol-5-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.002
5-(furan-2-yl)-N-methyl-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Helicobacter pylori
-
-
0.0014
5-methyl-7-(2-methylpropyl)-2-(naphthalen-1-ylmethyl)-3-(pyridin-4-yl)-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000062
5-[2-[(6-chloroquinolin-4-yl)methyl]-5,7-bis(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000055
5-[2-[(6-chloroquinolin-4-yl)methyl]-5-(cyanomethyl)-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00008
5-[2-[(6-chloroquinolin-4-yl)methyl]-5-cyclopropyl-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000086
5-[2-[(6-chloroquinolin-4-yl)methyl]-5-methyl-7-(2-methylpropyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00007
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(prop-2-en-1-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000028
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(prop-2-yn-1-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00024
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-(propan-2-yl)-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00067
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-[2-(1H-1,2,3-triazol-1-yl)ethyl]-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00047
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-[2-(1H-pyrazol-1-yl)ethyl]-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000013
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-[4-(1H-1,2,4-triazol-1-yl)but-2-yn-1-yl]-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00012
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-5-[4-(1H-pyrazol-1-yl)but-2-yn-1-yl]-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000088
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-(2-hydroxyethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000057
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-(4-hydroxybut-2-yn-1-yl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00007
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-ethyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000026
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00006
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-4-methylfuran-2-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00026
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-[4-(1H-imidazol-1-yl)but-2-yn-1-yl]-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000051
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-[4-(morpholin-4-yl)but-2-yn-1-yl]-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.000016
5-[2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-[5-methyl-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl]-1H-pyrrole-3-sulfonamide
Helicobacter pylori
-
-
0.000074
5-[5-(but-2-yn-1-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.00016
5-[5-(but-3-yn-2-yl)-2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-4,6-dioxo-4,5,6,7-tetrahydro-2H-pyrazolo[3,4-d]pyrimidin-3-yl]-1-methyl-1H-pyrrole-3-carbonitrile
Helicobacter pylori
-
pH and temperature not specified in the publication
0.0043 - 0.0044
9-(2,6-difluoro-3-methylbenzyl)-2-[(1,1,1,2,2-pentafluoropentan-3-yl)oxy]-9H-purin-6-amine
0.0353
bis(2,4-bis (trichloromethyl)-1,3,5-triazapentadienato)-Zn(II) complex
Burkholderia cenocepacia
-
recombinant enzyme, pH 8.0, 37°C
-
60.4
bis(2-carboxyethyl)-phosphinic acid
Enterococcus faecalis
-
pH and temperature not specified in the publication
0.0017
N,8-dimethyl-5-phenyl-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Helicobacter pylori
-
-
0.00625
N-benzyl-N'-[3-(5-methyl-1,3-benzoxazol-2-yl)phenyl]urea
Mycobacterium tuberculosis
-
pH 8.0, 37°C, recombinant enzyme
0.0007
N-methyl-3,5-di(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Helicobacter pylori
-
-
0.0006
N-methyl-5-(1H-pyrrol-3-yl)-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Helicobacter pylori
-
-
0.0022
N-methyl-5-phenyl-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Helicobacter pylori
-
-
0.01
tris(2,4-bis(trichloromethyl)-1,3,5-triazapentadienate)-Mn(III) complex
Burkholderia cenocepacia
-
recombinant enzyme, pH 8.0, 37°C
0.0009
2-(butylsulfanyl)-8-(4-fluorobenzyl)-4-(methylamino)-5,8-dihydropteridine-6,7-dione
Enterococcus faecalis
-
-
0.0038
2-(butylsulfanyl)-8-(4-fluorobenzyl)-4-(methylamino)-5,8-dihydropteridine-6,7-dione
Staphylococcus aureus
-
-
0.0014
2-(butylsulfanyl)-9-(2-methoxy-5-nitrobenzyl)-9H-purin-6-amine
Enterococcus faecalis
Q836J0
-
0.0025
2-(butylsulfanyl)-9-(2-methoxy-5-nitrobenzyl)-9H-purin-6-amine
Enterococcus faecium
Q836J0
-
0.0022
2-(butylsulfanyl)-9-(3-chloro-2,6-difluorobenzyl)-9H-purin-6-amine
Enterococcus faecalis
Q836J0
-
0.0026
2-(butylsulfanyl)-9-(3-chloro-2,6-difluorobenzyl)-9H-purin-6-amine
Enterococcus faecium
Q836J0
-
0.000026
2-butoxy-9-(3-chloro-2,6-difluorobenzyl)-N-(pyridin-3-ylmethyl)-9H-purin-6-amine
Helicobacter pylori
-
-
0.002
2-butoxy-9-(3-chloro-2,6-difluorobenzyl)-N-(pyridin-3-ylmethyl)-9H-purin-6-amine
Enterococcus faecalis
Q836J0
-
0.0027
2-butoxy-9-(3-chloro-2,6-difluorobenzyl)-N-(pyridin-3-ylmethyl)-9H-purin-6-amine
Enterococcus faecium
Q836J0
-
0.000034
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-[1-methyl-4-(methylsulfonyl)-1H-pyrrol-2-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
-
0.000034
2-[(6-chloroquinolin-4-yl)methyl]-7-(cyclopropylmethyl)-5-methyl-3-[1-methyl-4-(methylsulfonyl)-1H-pyrrol-2-yl]-2H-pyrazolo[3,4-d]pyrimidine-4,6(5H,7H)-dione
Helicobacter pylori
-
pH and temperature not specified in the publication
0.0015
4-amino-2-(butylsulfanyl)-8-(2,6-difluorobenzyl)-5,8-dihydropteridine-6,7-dione
Enterococcus faecalis
-
-
0.0031
4-amino-2-(butylsulfanyl)-8-(2,6-difluorobenzyl)-5,8-dihydropteridine-6,7-dione
Staphylococcus aureus
-
-
0.00065
4-amino-2-(butylsulfanyl)-8-(3,4-dichlorobenzyl)-5,8-dihydropteridine-6,7-dione
Enterococcus faecalis
-
-
0.0015
4-amino-2-(butylsulfanyl)-8-(3,4-dichlorobenzyl)-5,8-dihydropteridine-6,7-dione
Staphylococcus aureus
-
-
0.0011
4-amino-2-(butylsulfanyl)-8-(4-fluorobenzyl)-5,8-dihydropteridine-6,7-dione
Staphylococcus aureus
-
-
0.0035
4-amino-2-(butylsulfanyl)-8-(4-fluorobenzyl)-5,8-dihydropteridine-6,7-dione
Enterococcus faecalis
-
-
0.0076
4-amino-8-benzyl-2-(benzylsulfanyl)-5,8-dihydropteridine-6,7-dione
Staphylococcus aureus
-
-
0.021
4-amino-8-benzyl-2-(benzylsulfanyl)-5,8-dihydropteridine-6,7-dione
Enterococcus faecalis
-
-
0.0024
4-amino-8-benzyl-2-(butylsulfanyl)-5,8-dihydropteridine-6,7-dione
Enterococcus faecalis
-
-
0.0064
4-amino-8-benzyl-2-(butylsulfanyl)-5,8-dihydropteridine-6,7-dione
Staphylococcus aureus
-
-
0.0019
4-amino-8-benzyl-2-(cyclopentylsulfanyl)-5,8-dihydropteridine-6,7-dione
Enterococcus faecalis
-
-
0.052
4-amino-8-benzyl-2-(cyclopentylsulfanyl)-5,8-dihydropteridine-6,7-dione
Staphylococcus aureus
-
-
0.0043
9-(2,6-difluoro-3-methylbenzyl)-2-[(1,1,1,2,2-pentafluoropentan-3-yl)oxy]-9H-purin-6-amine
Enterococcus faecalis
Q836J0
-
0.0044
9-(2,6-difluoro-3-methylbenzyl)-2-[(1,1,1,2,2-pentafluoropentan-3-yl)oxy]-9H-purin-6-amine
Enterococcus faecium
Q836J0
-
0.0014
pyrazolopyrimidinedione analogue
Helicobacter pylori
-
a pyrazolopyrimidinedione analogue (compound A) identified by a high-throughput screen demonstrates inhibition with excellent selectivity for MurI of Helicobacter pylori, it is time-independent, fully-reversible and insensitive to changes in enzyme or detergent concentration
-
0.4
pyrazolopyrimidinedione analogue
Escherichia coli
-
value above 0.4, a pyrazolopyrimidinedione analogue (compound A) identified by a high-throughput screen demonstrates inhibition with excellent selectivity for MurI of Helicobacter pylori but not for MurI of Escherichia coli
-
0.4
pyrazolopyrimidinedione analogue
Staphylococcus aureus
-
value above 0.4, a pyrazolopyrimidinedione analogue (compound A) identified by a high-throughput screen demonstrates inhibition with excellent selectivity for MurI of Helicobacter pylori but not for MurI of Staphylococcus aureus
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
computer simulations on a QM/MM (quantum mechanics/molecular mechanics) potential energy surface are carried out to gain insights into the catalytic mechanism of glutamate racemase (MurI). Results suggest at least two possible roles for MurI as a catalyst: (1) to activate the bound substrate by donating a proton to its carboxylate main chain in a step prior to the racemization process and (2) to optimize the differential stabilization of the intermediate relative to the reactant via an intermolecular effect that comes, partly, from a desolvation effect on the reactant in going from water to the enzyme environment and, partly, from a stabilization effect on the intermediate by the enzymatic residues. Thus, the catalytic effect of glutamate racemase is achieved without resorting to covalent bond formation between the enzyme or cofactor and the transition state.
additional information
-
in Bacillus anthracis glutamate racemase is encoded by two genes racE1 and racE2, both enzymes are different in quaternary structure and catalyze the reversible stereoisomerization with similar but not identical kinetic properties; in Bacillus anthracis glutamate racemase is encoded by two genes racE1 and racE2, both enzymes are different in quaternary structure and catalyze the reversible stereoisomerization with similar but not identical kinetic properties
additional information
-
Escherichia coli MurI is monomeric in solution and shows extremely low intrinsic activity in either direction (symmetrical kinetic profile), but catalytic turnover is upregulated over 1000fold by UDP-MurNAc-Ala, the product of the preceding enzyme in the peptidoglycan biosynthetic pathway
additional information
polarimetric assay method, protocol for measurement of enzyme activity in 96-well microtiter plates
additional information
-
it is demonstrated that mycobacterial MurI inhibits DNA gyrase activity. Inhibition is not species-specific as Escherichia coli gyrase is also inhibited but is enzyme-specific as topoisomerase I activity remains unaltered. MurI binds to GyrA subunit of the enzyme leading to a decrease in DNA-binding of the holoenzyme. The sequestration of the gyrase by MurI results in inhibition of all reactions catalysed by DNA gyrase. MurI is thus not a typical potent inhibitor of DNA gyrase and instead its role could be in modulation of the gyrase activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.6
8.2
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 10
-
pH 2.0: about 40% of maximal activity of soluble enzyme, about 60% of maximal activity of immobilized enzyme, pH 10.0: about 80% of maximal activity of immobilized enzyme, about 40% of maximal activity of soluble enzyme
6 - 10
-
enzyme exhibits a preference for high pH values, showing an optimal activity at pH 8.0-9.0, with about 70% of maximal activity at pH 9.5, and less than 50% activity below pH 7.0
6.5 - 8.5
-
6.5: 90% of the activity at pH 7.5, routinely assayed at pH 7.5, 8.5: 70% of the activity at pH 7.5
7 - 10
8 - 8.5
FnGR is active over a broad pH range, with the maximum of activity between pH 8.0 and 8.5 for the reaction in the L-D direction
8.5 - 9
FnGR is active over a broad pH range, with the maximum of activity between pH 8.0 and 8.5 for the reaction in the D-L direction
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 70
-
20°C: about 65% of maximal activity, 70°C: about 30% of maximal activity, soluble enzyme; more than 80% of maximal activity is observed between 20°C and 70°C, immobilized enzyme
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
JM109/pGR3, overproducer of glutamate racemase and WM335 mutant defective in the gene of glutamate racemase
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
highest activity in the early stationary phase of growth
brenda
-
highest activity in the early stationary phase of growth
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the overexpression results in the formation of inclusion bodies, little activity is found in the soluble fraction
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
a large number of Chlamydia species (as well as members of the Planctomycetes-Verrucomicrobiae-Chlamydiae superphylum) possess DapF but lack homologues of MurI. It is likely that DapF is a primordial isomerase that functions as both racemase and epimerase in these organisms, suggesting that specialized D-glutamate racemase enzymes never evolved in these microbes. DapFCT possesses an additional cysteine (C86) that is not highly conserved in other bacterial species
malfunction
metabolism
physiological function
additional information
malfunction
-
the racE1 deletion does not affect growth rates, whereas racE2 deletion delays the vegetative growth of Bacillus anthracis following spore germination, producing aberrant cell shapes that can only partially be suppressed with exogenous D-glutamate. Deletion of racE1 or racE2 does not affect the synthesis or stereochemical composition of Bacillus anthracis poly-gamma-D-glutamic acid (PDGA) capsule, and mutants with a deletion of both genes, racE1 and racE2, are not viable; the racE1 deletion does not affect growth rates, whereas racE2 deletion delays the vegetative growth of Bacillus anthracis following spore germination, producing aberrant cell shapes that can only partially be suppressed with exogenous D-glutamate. Deletion of racE1 or racE2 does not affect the synthesis or stereochemical composition of Bacillus anthracis poly-gamma-D-glutamic acid (PDGA) capsule, and mutants with a deletion of both genes, racE1 and racE2, are not viable
malfunction
inactivation of glutamate racemase eliminates the virulence in Streptococcus mutans, a stable mutant of Streptococcus mutans deficient in glutamate racemase, strain FW1718, is constructed to investigate the impact of murI inactivation on cariogenic virulence in wild-type strain UA159. The murI mutant exhibits an enlarged cell size, longer cell chains, diminished cell-cell aggregation, and altered cell surface ultrastructure compared with the wild-type. Gene murI deficiency weakens acidogenicity, aciduricity, and biofilm formation ability of Streptococcus mutans. The deletion of murI reduces the expression of the acidogenesis-related gene ldh by 44fold. The expression levels of the gene coding for surface protein antigen P (spaP) and the acid-tolerance related gene (atpD) are downregulated by 99%. Expression of comE, comD, gtfB and gtfC genes, related to biofilm formation, are downregulated 8, 43, 85, and 298fold in the murI mutant compared with the wild-type, respectively
malfunction
-
the racE1 deletion does not affect growth rates, whereas racE2 deletion delays the vegetative growth of Bacillus anthracis following spore germination, producing aberrant cell shapes that can only partially be suppressed with exogenous D-glutamate. Deletion of racE1 or racE2 does not affect the synthesis or stereochemical composition of Bacillus anthracis poly-gamma-D-glutamic acid (PDGA) capsule, and mutants with a deletion of both genes, racE1 and racE2, are not viable; the racE1 deletion does not affect growth rates, whereas racE2 deletion delays the vegetative growth of Bacillus anthracis following spore germination, producing aberrant cell shapes that can only partially be suppressed with exogenous D-glutamate. Deletion of racE1 or racE2 does not affect the synthesis or stereochemical composition of Bacillus anthracis poly-gamma-D-glutamic acid (PDGA) capsule, and mutants with a deletion of both genes, racE1 and racE2, are not viable
-
malfunction
Streptococcus mutans serotype c ATCC 700610 / UA159
-
inactivation of glutamate racemase eliminates the virulence in Streptococcus mutans, a stable mutant of Streptococcus mutans deficient in glutamate racemase, strain FW1718, is constructed to investigate the impact of murI inactivation on cariogenic virulence in wild-type strain UA159. The murI mutant exhibits an enlarged cell size, longer cell chains, diminished cell-cell aggregation, and altered cell surface ultrastructure compared with the wild-type. Gene murI deficiency weakens acidogenicity, aciduricity, and biofilm formation ability of Streptococcus mutans. The deletion of murI reduces the expression of the acidogenesis-related gene ldh by 44fold. The expression levels of the gene coding for surface protein antigen P (spaP) and the acid-tolerance related gene (atpD) are downregulated by 99%. Expression of comE, comD, gtfB and gtfC genes, related to biofilm formation, are downregulated 8, 43, 85, and 298fold in the murI mutant compared with the wild-type, respectively
-
metabolism
-
glutamate racemase racemizes D-glutamate from L-glutamate, a key step in peptidoglycan synthesis
metabolism
-
D-glutamate is generated via the racemization of L-glutamate by glutamate racemase (MurI). Chlamydia lacks homologues of MurI. The bifunctional diaminopimelate epimerase (DapF) also synthesizes D-glutamate, EC 5.1.1.3, and catalyzes the final step in the synthesis of meso-diaminopimelate, an amino acid unique to peptidoglycan, EC 5.1.1.7
metabolism
Mycobacterium tuberculosis ATCC 25618 / H37Rv
-
glutamate racemase racemizes D-glutamate from L-glutamate, a key step in peptidoglycan synthesis
-
physiological function
peptidoglycan synthesis
physiological function
-
glutamate racemase catalyzes stereoinversion at the Calpha of glutamate and is a source of D-glutamate in bacteria, an essential component of the peptidoglycan layer of the bacterial cell walls
physiological function
-
overexpression of the glutamate racemase gene not only increases the production of poly-gamma-glutamic acid by 22.5% but also increases the proportion of D-glutamate in poly-gamma-glutamic acid from 77 to 85%
physiological function
-
glutamate racemase provides D-glutamate for the construction of N-acetylglucosamine-N-acetylmuramic acid peptidoglycan subunits assimilated into the bacterial cell wall
physiological function
-
D-glutamate is an essential biosynthetic building block of the peptidoglycans that encapsulate the bacterial cell wall
physiological function
-
glutamate racemase (GR) catalyzes the cofactor independent stereoinversion of L- to D-glutamate for biosynthesis of bacterial cell walls. Glutamate racemase is a flexible enzyme capable of binding a variety of small molecules both in the active site and at allosteric binding pockets
physiological function
-
glutamate racemase (MurI) is responsible for providing D-glutamate for peptidoglycan biosynthesis in bacteria
physiological function
-
glutamate racemase (MurI) is responsible for providing D-glutamate for peptidoglycan biosynthesis in bacteria
physiological function
-
glutamate racemase racemizes D-glutamate from L-glutamate, a key step in peptidoglycan synthesis
physiological function
-
enzyme MurI function is essential for the growth of Mycobacterium tuberculosis cells
physiological function
-
MurI is essential for growth, and glutamate racemase is the only source of D-glutamate for peptidoglycan synthesis in Mycobacterium smegmatis
physiological function
-
genes racE1 and racE2, encoding two glutamate racemases, are not essential for growth of Bacillus anthracis noncapsulating vaccine strain Sterne and fully virulent, capsulating strain Ames, even in the absence of exogenous D-glutamate. Modeling of Bacillus anthracis, similar to Bacillus subtilis, utilizing two functionally redundant racemase enzymes to synthesize D-glutamic acid for peptidoglycan synthesis; genes racE1 and racE2, encoding two glutamate racemases,are not essential for growth of Bacillus anthracis noncapsulating vaccine strain Sterne and fully virulent, capsulating strain Ames, even in the absence of exogenous D-glutamate. Modeling of Bacillus anthracis, similar to Bacillus subtilis, utilizing two functionally redundant racemase enzymes to synthesize D-glutamic acid for peptidoglycan synthesis
physiological function
-
DapF is a primordial isomerase that functions as both racemase and epimerase in the organism. genetic complementation of an Escherichia coli murI mutant demonstrating that Chlamydia DapF can generate D-glutamate. D-Glu racemase activity is required for synthesizing D-Glu-containing peptidoglycan, DapFCT is also capable of racemizing D-Glu to L-Glu
physiological function
glutamate racemase (MurI) is an essential enzyme in peptidoglycan biosynthesis
physiological function
-
glutamate racemase is an essential enzyme for the biosynthesis of the bacterial cell wall
physiological function
-
genes racE1 and racE2, encoding two glutamate racemases, are not essential for growth of Bacillus anthracis noncapsulating vaccine strain Sterne and fully virulent, capsulating strain Ames, even in the absence of exogenous D-glutamate. Modeling of Bacillus anthracis, similar to Bacillus subtilis, utilizing two functionally redundant racemase enzymes to synthesize D-glutamic acid for peptidoglycan synthesis; genes racE1 and racE2, encoding two glutamate racemases,are not essential for growth of Bacillus anthracis noncapsulating vaccine strain Sterne and fully virulent, capsulating strain Ames, even in the absence of exogenous D-glutamate. Modeling of Bacillus anthracis, similar to Bacillus subtilis, utilizing two functionally redundant racemase enzymes to synthesize D-glutamic acid for peptidoglycan synthesis
-
physiological function
-
overexpression of the glutamate racemase gene not only increases the production of poly-gamma-glutamic acid by 22.5% but also increases the proportion of D-glutamate in poly-gamma-glutamic acid from 77 to 85%
-
physiological function
-
glutamate racemase (GR) catalyzes the cofactor independent stereoinversion of L- to D-glutamate for biosynthesis of bacterial cell walls. Glutamate racemase is a flexible enzyme capable of binding a variety of small molecules both in the active site and at allosteric binding pockets
-
physiological function
-
glutamate racemase provides D-glutamate for the construction of N-acetylglucosamine-N-acetylmuramic acid peptidoglycan subunits assimilated into the bacterial cell wall
-
physiological function
Mycobacterium tuberculosis ATCC 25618 / H37Rv
-
enzyme MurI function is essential for the growth of Mycobacterium tuberculosis cells; glutamate racemase (MurI) is responsible for providing D-glutamate for peptidoglycan biosynthesis in bacteria; glutamate racemase racemizes D-glutamate from L-glutamate, a key step in peptidoglycan synthesis
-
physiological function
Mycolicibacterium smegmatis ATCC 700084 / mc(2)155
-
glutamate racemase (MurI) is responsible for providing D-glutamate for peptidoglycan biosynthesis in bacteria; MurI is essential for growth, and glutamate racemase is the only source of D-glutamate for peptidoglycan synthesis in Mycobacterium smegmatis
-
physiological function
Streptococcus mutans serotype c ATCC 700610 / UA159
-
glutamate racemase (MurI) is an essential enzyme in peptidoglycan biosynthesis
-
additional information
-
mechanism of Helicobacter pylori glutamate racemase to generate the thermodynamically unfavorable reverse protonation state of the catalytic residue cysteine required for the proton abstraction from the alpha-carbon of glutamate, molecular dynamics simulations with a molecular mechanics force field along with QM/MM calculations starting from the crystal structure and from different MD snapshot, structural fluctuations of the enzyme-substrate complex, structural analysis of the four transition state structures,overview
additional information
MurI from Lactobacillus plantarum NC8 seems to exhibit pseudosymmetry for the racemisation of Glu in both directions
additional information
-
molecular dynamics simulations on the enzyme have suggested particular regions that undergo relatively large changes, both in terms of substrate unbinding, as well as equilibrated enzyme-ligand complexes that show movement relative to one another (i.e., enzyme complexes with different types of active site small molecules equilibrated to distinct conformers)
additional information
-
the mycobacterial MurI dimer is tightly associated, with a KD in the nanomolar range. The enzyme binds D- and L-glutamate specifically, but is inactive in solution unless the dimer interface is mutated. Enzyme structure analysis, active site structure and substrate binding structure, overview
additional information
-
the mycobacterial MurI dimer is tightly associated, with a KD in the nanomolar range. The enzyme binds D- and L-glutamate specifically, but is inactive in solution unless the dimer interface is mutated. Enzyme structure analysis, active site structure and substrate binding structure, overview
additional information
-
the structure of Chlamydia DAP epimerase exhibits significant remodeling in the substrate-binding pocket, overview. DapFCT requires the epimerase active-site cysteines for glutamate racemase activity
additional information
-
structure homology modeling, in BcGR, all critical residues for enzymatic activity and substrate recognition are fully conserved within the 2-domain glutamate racemase fold
additional information
-
molecular dynamics simulations on the enzyme have suggested particular regions that undergo relatively large changes, both in terms of substrate unbinding, as well as equilibrated enzyme-ligand complexes that show movement relative to one another (i.e., enzyme complexes with different types of active site small molecules equilibrated to distinct conformers)
-
additional information
-
MurI from Lactobacillus plantarum NC8 seems to exhibit pseudosymmetry for the racemisation of Glu in both directions
-
additional information
Mycobacterium tuberculosis ATCC 25618 / H37Rv
-
the mycobacterial MurI dimer is tightly associated, with a KD in the nanomolar range. The enzyme binds D- and L-glutamate specifically, but is inactive in solution unless the dimer interface is mutated. Enzyme structure analysis, active site structure and substrate binding structure, overview
-
additional information
Mycolicibacterium smegmatis ATCC 700084 / mc(2)155
-
the mycobacterial MurI dimer is tightly associated, with a KD in the nanomolar range. The enzyme binds D- and L-glutamate specifically, but is inactive in solution unless the dimer interface is mutated. Enzyme structure analysis, active site structure and substrate binding structure, overview
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Enterococcus faecalis (strain ATCC 700802 / V583)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Helicobacter pylori (strain J99 / ATCC 700824)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)