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Enzyme Nomenclature
Information on EC 5.1.1.3 - glutamate racemase
for references in articles please use BRENDA:EC5.1.1.3
Word Map on EC 5.1.1.3
- 5.1.1.3
- d-glutamate
- peptidoglycan
-
cofactor-independent
-
d-amino
- pediococcus
- drug development
-
poly-gamma-glutamate
- d-glu
-
aquifex
- pentosaceus
- pyrophilus
-
two-base
-
stereoinversion
- fermenti
- medicine
- synthesis
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
5.1.1.3
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RECOMMENDED NAME
GeneOntology No.
glutamate racemase
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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
-
L-glutamate = D-glutamate
two base mechanism, removal of alpha-hydrogen is the rate determining step
-
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
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L-glutamate = D-glutamate
the molecular mechanism involves deprotonation of the glutamate alpha-proton, followed by substrate reprotonation on the opposite stereochemical face
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
racemization
racemization
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
JM109/pGR3, overproducer of glutamate racemase and WM335 mutant defective in the gene of glutamate racemase
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-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
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
-
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%
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physiological function
-
glutamate racemase provides D-glutamate for the construction of N-acetylglucosamine-N-acetylmuramic acid peptidoglycan subunits assimilated into the bacterial cell wall
-
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
-
MurI from Lactobacillus plantarum NC8 seems to exhibit pseudosymmetry for the racemisation of Glu in both directions
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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
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
-
-
-
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
-
-
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
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-
r
L-glutamate
D-glutamate
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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
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-
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
?
-
-
the enzyme is an endogenous DNA gyrase inhibitor
-
?
additional information
?
-
-
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
?
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-
enzyme does not catalyze the exchange between 2-oxolutarate and DL-Glu
-
-
-
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
?
-
-
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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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
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
?
-
-
the enzyme is an endogenous DNA gyrase inhibitor
-
?
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
-
-
-
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
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-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,4R)-2-amino-4-(2-benzo[b]furyl)methyl pentanedioic acid
-
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
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IC50: 0.01 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(2-bromo)benzyl pentanedioic acid
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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
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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
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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
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
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
dipicolinic acid
-
allosteric inhibitor of both Bacillus anthracis glutamate racemase isozymes which exhibits low micromolar inhibition with clear noncompetitive behavior
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
[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
hydroxylamine
-
different experimentators found inhibition or no inhibition
additional information
-
the pressure does not affect catalysis after substrate binding
-
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 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)
0.74
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)
-
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
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
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
0.0015 - 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
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
-
-
0.0007
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
-
-
0.0009
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
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
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
6.5 - 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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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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
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Helicobacter pylori (strain J99 / ATCC 700824)
Helicobacter pylori (strain J99 / ATCC 700824)
Helicobacter pylori (strain J99 / ATCC 700824)
Helicobacter pylori (strain J99 / ATCC 700824)
Helicobacter pylori (strain J99 / ATCC 700824)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
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)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29000
30000
additional information
-
glutamate racemase shows significant sequence homology with mammalian myoglobins, in particular, in the regions corresponding to the E and F helices
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
-
method: gel filtration. The Helicobacter pylori MurI enzyme also forms a homodimer but with the active sites in close proximity in a face-to-face orientation
monomer
additional information
dimer
-
both enzymes RacE1 and Rac2 are dimers with monomers arranged in a tail-to-tail orientation which is determined by gel filtration
dimer
-
determined by gel filtration, RacE2 exist as a dimer in solution, but the monomeric enzyme is more active than the dimeric form
dimer
determined by blue native PAGE, FnGR is a pseudosymmetric enzyme, the presence of glutamate does not significantly alter the position of the monomer-dimer equilibrium of the enzyme
dimer
crystal structure analysis, GluR is composed of two domains of alpha/beta protein that are related by pseudo-2fold symmetry and the active site is located at the domain interface
monomer
-
mutants R25A and K106A/R214A are completely monomeric at the concentration of 5 mg/ml
monomer
1 * 29866, calculation from nucleotide sequence; 1 * 30000; 1 * 30000, SDS-PAGE
monomer
determined by gel filtration, BsGR is a monomeric enzyme, which dimerizes in the presence of either 10 mM D- or L-glutamate
additional information
although RacE1 and RacE2 share significant sequence similarity, these proteins have different quaternary structural properties; although RacE1 and RacE2 share significant sequence similarity, these proteins have different quaternary structural properties; by gel filtration it is shown that in solution RacE2 may be polydisperse, existing as both monomers and higher-order complexes
additional information
although RacE1 and RacE2 share significant sequence similarity, these proteins have different quaternary structural properties; although RacE1 and RacE2 share significant sequence similarity, these proteins have different quaternary structural properties; by gel filtration it is shown that in solution RacE2 may be polydisperse, existing as both monomers and higher-order complexes
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure of apo-enzyme and enzyme complexed with a substrate analog, D-glutamine, by multiwavelength anomalous dispersion method using a thimerosal-bound MurI crystal, determined at 2.3 A resolution
-
crystallization trials are performed by the hanging-drop, vapor-diffusion method. X-ray structure analysis shows that RacE1 and RacE2 are both dimers with monomers arranged in a tail-to-tail orientation, RCSB Protein Data Bank: 2DWU; crystallization trials are performed by the hanging-drop, vapor-diffusion method, X-ray structure analysis shows that RacE1 and RacE2 are both dimers with monomers arranged in a “tail-to-tail” orientation, RCSB Protein Data Bank: 2GZM
-
crystal structures of MurI of Helicobacter pylori, Escherichia coli, Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium are analysed under similar, physiologically relevant conditons. MurI of Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium all form homodimeric structures. In all these structures, monomers oligomerize in a tail-to-tail orientation with active sites opposed and fully exposed to solvent
-
crystal structures of MurI of Helicobacter pylori, Escherichia coli, Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium are analysed under similar, physiologically relevant conditons. MurI of Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium all form homodimeric structures. In all these structures, monomers oligomerize in a tail-to-tail orientation with active sites opposed and fully exposed to solvent
-
crystal structures of MurI of Helicobacter pylori, Escherichia coli, Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium are analysed under similar, physiologically relevant conditons. The Escherichia coli MurI co-crystallizes as a monomer with both L-glutamate and its activator UDP-MurNAc-Ala. The activator binds in the hinge region on the side opposite to the catalytically active site through contacts between the uracil ring system and domain B and through specific salt bridge interactions with R104 in domain A and the alanyl moiety of the activator, consistent with the strict requirement of the alanine and uracil moieties for activation
-
the different kinetic profiles of MurI enzymes across the species suggest fundamental structural differences and therefore, crystal structures of MurI of Helicobacter pylori, Escherichia coli, Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium are analysed under similar, physiologically relevant conditons. The Helicobacter pylori MurI enzyme also forms a homodimer but with the active sites in close proximity in a face-to-face orientation
-
crystal structures of MurI of Helicobacter pylori, Escherichia coli, Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium are analysed under similar, physiologically relevant conditons. MurI of Staphylococcus aureus, Enterococcus faecalis and Enterococcus faecium all form homodimeric structures. In all these structures, monomers oligomerize in a tail-to-tail orientation with active sites opposed and fully exposed to solvent
-
crystallization is carried out by the sitting-drop,vapor-diffusion method, crystal structures of GluR from Streptococcus pyogenes in both inhibitor-free and inhibitor-bound forms. The inhibitor-free GluR crystallizes in two different forms, which diffracts to 2.25 A and 2.5 A resolution, while the inhibitor-bound crystal diffracted to 2.5 A resolution.
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
97% activity remaining after 22 h at pH 7.0-8.0, half-life, by extrapolation of the data, is 287 h at pH 7.0, 154 h at pH 8.0, 25 h at pH 9.0, and 6 h at pH 10.0
728742
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
pH 8.0, 0.1 M Tris-HCl buffer containing 10% glycerol, retains 90% of its activity after 10 min
60
-
pH 7, 60 min, about 25% loss of activity of soluble and immobilized enzyme
80
-
pH 7, 60 min, about 20% loss of activity of immobilized enzyme, about 70% loss of activity of soluble enzyme
90
-
pH 7, 60 min, 50% loss of activity of immobilized enzyme, about 75% loss of activity of soluble enzyme
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
irreversible inactivation upon storage in the absence of 10% glycerol, 1 mM DL-Glu, and 0.1% 2-mercaptoethanol
-
irreversible loss of activity on storage at DL-Glu and a reducing thiol such as 2-mercaptoethanol. Inactivation may be due to air oxidation of a free thiol residue
-
stabilized by immobilization to Chitopearl 2505 or Chitopearl 2605. The enzyme remains active at 4°C for 30 days, remaining activity is 32%
-
stabilized by presence of reduced thiols. After 3 h at 30°C, samples of the enzyme containing either dithiothreitol or Glu or both show about 80% retention of the original activity, whereas samples that lack both dithiothreitol and Glu retain less than 40% of the starting activity
-
stabilized in presence of mercaptoethanol and other sulfhydryl containing compounds
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM Tris-HCl, pH 7.5, 1 mM DL-GLu, 10% glycerol, 0.1% 2-mercaptoethanol, 0.1 mM phenylmethanesulfonyl fluoride, stable for several months
-
enzyme can be kept frozen at all stages of the purification for several weeks without loss of activity
-
no loss of activity is noted after the enzyme is stored at 80°C for more than 8 months, at least 80% of enzyme activity is retained after incubation for 8 h at 4°C
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Co2+-affinity column chromatography, and anion-exchange chromatography
-
by using nickel-nitrilotriacetic acid affinity chromatography and gel filtration
-
by using of nickel ion affinity chromatography at 4°C
enzyme is purified by using standard chromatographic methods
protein extract is loaded on a HiTrap affinity column charged with Co2+, the His-tags are not removed as the enzyme activities with and without these tags are not significantly different
-
protein extract is purified by using a nickel-chelated Hi-trap chelating column, Hi-trap sp-FF cation-exchange column and by by gel-filtration on a Superdex-200 prep-grade column
RacE1 is expressed as in Escherichia coli with an amino-terminal hexahistidine fusion peptide to facilitate purification via nickel-chelate affinity chromatography; RacE1 is expressed as in Escherichia coli with an amino-terminal hexahistidine fusion peptide to facilitate purification via nickel-chelate affinity chromatography
recombinant enzyme 9.16fold from Escherichia coli strain BL21(DE3)/pET20b-murI by L-Glu affinity and anion exchange chromatography
by using of nickel ion affinity chromatography at 4°C
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned in Escherichia coli as a fusion protein with a 6x His tag at the N-terminus
cloned in Escherichia coli as a fusion protein with a 6xHis tag at the N-terminus
-
construction of a glutamate racemase-overexpressing strain by transformation, recombinant strains Hp80.1 and Hp80.2 are constructed in the wild-type background of strain ARHp80
-
Escherichia coli strains DH5a and BL26(DE3) are used for cloning and overexpression of mycobacterial MurI, respectively
-
expression in Escherichia coli
full-length MurI proteins are prepared by expression either as native (Helicobacter pylori, Escherichia coli) or N-terminal 6xHis-tagged (Staphylococcus aureus, Enterococcus faecalis, Enterococcus faecium) recombinant proteins in Escherichia coli strains co-expressing the chaperone proteins GroEL/GroES27 and purified by standard chromatographic methods
gene murI from strain NC-8, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)/pET20b-murI
overexpression in BL21(DE3) Escherichia coli as fusion protein bearing an N-terminal hexahistidine tag
recombinant wild type and mutant proteins are expressed in Escherichia coli cells
recombinant wild type and mutants are expressed in BL21(DE3) Escherichia coli cells
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full-length MurI proteins are prepared by expression either as native (Helicobacter pylori, Escherichia coli) or N-terminal 6xHis-tagged (Staphylococcus aureus, Enterococcus faecalis, Enterococcus faecium) recombinant proteins in Escherichia coli strains co-expressing the chaperone proteins GroEL/GroES27 and purified by standard chromatographic methods
-
full-length MurI proteins are prepared by expression either as native (Helicobacter pylori, Escherichia coli) or N-terminal 6xHis-tagged (Staphylococcus aureus, Enterococcus faecalis, Enterococcus faecium) recombinant proteins in Escherichia coli strains co-expressing the chaperone proteins GroEL/GroES27 and purified by standard chromatographic methods
-
full-length MurI proteins are prepared by expression either as native (Helicobacter pylori, Escherichia coli) or N-terminal 6xHis-tagged (Staphylococcus aureus, Enterococcus faecalis, Enterococcus faecium) recombinant proteins in Escherichia coli strains co-expressing the chaperone proteins GroEL/GroES27 and purified by standard chromatographic methods
-
full-length MurI proteins are prepared by expression either as native (Helicobacter pylori, Escherichia coli) or N-terminal 6xHis-tagged (Staphylococcus aureus, Enterococcus faecalis, Enterococcus faecium) recombinant proteins in Escherichia coli strains co-expressing the chaperone proteins GroEL/GroES27 and purified by standard chromatographic methods
-
full-length MurI proteins are prepared by expression either as native (Helicobacter pylori, Escherichia coli) or N-terminal 6xHis-tagged (Staphylococcus aureus, Enterococcus faecalis, Enterococcus faecium) recombinant proteins in Escherichia coli strains co-expressing the chaperone proteins GroEL/GroES27 and purified by standard chromatographic methods
-
overexpression in BL21(DE3) Escherichia coli as fusion protein bearing an N-terminal hexahistidine tag
overexpression in BL21(DE3) Escherichia coli as fusion protein bearing an N-terminal hexahistidine tag
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the racemase is constitutive and not induced by D-glutamate
the racemase is constitutive and not induced by D-glutamate
Fusobacterium varium NCTC 10560 / ATCC 8501
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D7S
-
turnover number is decreased by 170fold compared to wild-type enzyme in the D to L reaction, it is decreased by about 6fold compared to wild-type enzyme in the L to D reaction
E147N
-
turnover number is decreased by 100fold compared to wild-type enzyme in the D to L reaction, it is decreased by about 7fold compared to wild-type enzyme in the L to D reaction
C185A
predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold
C188A
predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold
C74A
predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold
C77A
predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold
K106A
K29A
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production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with a 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface
P99A
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production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with a 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface
Q86A
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production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with an at most 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface
R214A
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production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with a 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface
R214A/K106A
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production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with a 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface
R25A
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production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with a 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface
V149A
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mutant V149A has about a 2fold higher kcat than wild-type RacE2 (67/sec versus 38/sec), and has a Km value for L-glutamate similar to that of RacE2 (4.6 mM versus 3.7 mM), in the reverse reaction, V149A has a higher kcat than RacE2 (4.9/sec versus 1.6/sec, respectively), and its Km value for D-glutamate is the same as that of RacE2 (0.2 mM)
Y221A
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production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with an at most 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface
T76A
production by site-directed mutagenesis, strong RacE-glutamate carbanion interaction energy is notably dissipated with the mutant
V149A
while V149A BsGR exhibits a 3- and 6fold increase in the value of Km for L- and D-glutamate relative to wild-type BsGR, respectively, the values of kcat are slightly increased relative to the wild-type enzyme
A151V
production by site-directed mutagenesis, alanine ist essential for activity, mutation of residue 151 located at the entryway to the active site reveals that FnGR is very sensitive to increased steric bulk at this position
A75T
-
Ki: 0.661 mM (inhibitor: D-glutamate). Turnover number: 1.78/sec (substrate: L-glutamate), 0.065/sec (substrate: D-glutamate). Km: 7.4 mM (substrate: L-glutamate), Km: 0.275 mM (substrate: D-glutamate)
E151T
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Ki: 100 mM (value above 100 for inhibitor: D-glutamate). Turnover number: 0.08/sec (substrate: D-glutamate), 2.26/sec (substrate: L-glutamate). Km: 7.36 mM (substrate: L-glutamate), Km: 0.282 mM (substrate: D-glutamate)
D10N
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1015fold decrease of turnover number for L-glutamate compared to wild-type enzyme, 3.9fold increase in Km-value for L-glutamate compared to wild-type enzyme. 1079fold decrease of turnover number for D-glutamate compared to wild-type enzyme, 4.6fold increase in Km-value for D-glutamate compared to wild-type enzyme
D36N
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3.4fold decrease of turnover number for L-glutamate compared to wild-type enzyme, 106fold increase in Km-value for L-glutamate compared to wild-type enzyme. 3.1fold decrease of turnover number for D-glutamate compared to wild-type enzyme, 158fold increase in Km-value for D-glutamate compared to wild-type enzyme
E152Q
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1.8fold decrease of turnover number for L-glutamate compared to wild-type enzyme, 3.1fold increase in Km-value for L-glutamate compared to wild-type enzyme. 3.1fold decrease of turnover number for D-glutamate compared to wild-type enzyme, 13.5fold increase in Km-value for D-glutamate compared to wild-type enzyme
H186N
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1533fold decrease of turnover number for L-glutamate compared to wild-type enzyme, 3.4fold increase in Km-value for L-glutamate compared to wild-type enzyme. 731fold decrease of turnover number for D-glutamate compared to wild-type enzyme, 17.3fold increase in Km-value for D-glutamate compared to wild-type enzyme
C184A
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mutant C73A and C184A enzymes are inactive as racemases. However they are capable of catalyzing the elimination of HCl from opposite enantiomers of threo-3-chloroglutamic acid, a process that presumably requires only one enzymic base. It appears that Cys73 is responsible for the abstraction of the C-2 hydrogen from R-Glu and Cys184 abstracts the proton from S-glutamate in the racemization reaction of the wild type enzyme
C73A
-
mutant C73A and C184A enzymes are inactive as racemases. However they are capable of catalyzing the elimination of HCl from opposite enantiomers of threo-3-chloroglutamic acid, a process that presumably requires only one enzymic base. It appears that Cys73 is responsible for the abstraction of the C-2 hydrogen from R-Glu and Cys184 abstracts the proton from S-glutamate in the racemization reaction of the wild type enzyme
C185S
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decrease in racemization activity, mutant retains its gyrase inhibition ability
C75S
-
decrease in racemization activity, mutant retains its gyrase inhibition ability
C75SC185S
-
less than 10% of wild-type activity, mutant retains its gyrase inhibition ability
additional information
K106A
-
production by site-directed mutagenesis, catalytic rate is higher than that of the wild type in D-glutamine to L-glutamine direction, kinetics in the L-glutamine to D-glutamine direction is not as significantly affected with an a 2-3fold increase in the overall catalytic efficiency, disruption of the dimer interface
additional information
RacE1 and RacE2 share 51% sequence identity and 67% sequence similarity; RacE1 and RacE2 share 51% sequence identity and 67% sequence similarity
additional information
RacE1 and RacE2 share 51% sequence identity and 67% sequence similarity; RacE1 and RacE2 share 51% sequence identity and 67% sequence similarity
additional information
-
disruption of enzyme gene yrpC, no effect on growth or production of poly-gamma-glutamte. Disruption of enzyme gene glr, cells are only viable when an exogenous gene copy is present on a plasmid. Glr gene product is responsible for supply of D-glutamate both to the synthesis of peptidoglycan and poly-gamma-glutamate
additional information
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enzyme knockout mutants, gene racE is essential for growth in rich medium but dispensable for growth in minimal medium. YrpC gene is expressed only in minimal medium. Neither gene is required for synthesis of poly-gamma-DL-glutamate. RacE or yrpC mutant cells accumulate signifcant amounts of D- but not L-glutamate. RacE/yrpC double mutant shows severely impaired D-amino acid utilization
additional information
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site-directed mutagenesis experiments are described demonstrating the participation of Cys96 and Cys208 in the two-base reaction mechanism of the enzyme. The construction of N-terminal-truncated or C-terminal-truncated enzymes shows that the characteristic N-terminal amino acid extension of 20 residues is not involved in its activation by the nucleotide precursor
additional information
-
with 0.0065 mM UDP-N-acetylmuramoyl-L-Ala added, the N-terminal truncated enzyme displays a loss of more than 80% of the activity compared to the full-length enzyme
additional information
-
overexpression in vivo provides resistance to the action of ciprofloxacin
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
medicine
-
the enzyme may be a viable target for developing new antibacterial agents
synthesis
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production of D-glutamate from L-glutamate with glutamate racemase and L-glutamate oxidase from Streptomyces sp. X119-6. Both enzymes are highly stabilized by immobilization
drug development
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glutamate racemase is an enzyme essential to the bacterial cell wall biosynthesis pathway, and is therefore considered as a target for antibacterial drug discovery
drug development
-
glutamate racemase is an enzyme essential to the bacterial cell wall biosynthesis pathway, and is therefore considered as a target for antibacterial drug discovery
drug development
-
glutamate racemase is an enzyme essential to the bacterial cell wall biosynthesis pathway, and is therefore considered as a target for antibacterial drug discovery
drug development
-
glutamate racemase is an enzyme essential to the bacterial cell wall biosynthesis pathway, and is therefore considered as a target for antibacterial drug discovery
drug development
-
glutamate racemase is an enzyme essential to the bacterial cell wall biosynthesis pathway, and is therefore considered as a target for antibacterial drug discovery
drug development
-
inhibitors of glutamate racemase are potential targets as antibiotic agents against Helicobacter pylori
drug development
enzyme is an attractive target for the development of antibacterial agents
drug development
enzyme is an attractive target for the development of antibacterial agents
drug development
-
einzyme is potentially an attractive target for the development of new antibacterial agents because of being an essential enzyme
drug development
glutamate racemase is an attractive target for the design of antibacterial agents
Show AA Sequence (18577 entries)
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