Information on EC 5.1.1.3 - Glutamate racemase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
5.1.1.3
-
RECOMMENDED NAME
GeneOntology No.
Glutamate racemase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-glutamate = D-glutamate
show the reaction diagram
-
-
-
-
L-glutamate = D-glutamate
show the reaction diagram
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
show the reaction diagram
two base mechanism, removal of alpha-hydrogen is the rate determining step
-
L-glutamate = D-glutamate
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
molecular dynamics simulations, mechanism by which binding mismatches are propagated into an opening of the active site
-
L-glutamate = D-glutamate
show the reaction diagram
analysis of active site, mechanism
-
L-glutamate = D-glutamate
show the reaction diagram
glutamate racemase faces the difficult task of deprotonating a relatively low acidicity proton, the amino acids 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
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
decarboxylation
-
-
racemization
-
-
-
-
racemization
-
-
racemization
-
-
racemization
-
-
racemization
Fusobacterium varium NCTC 10560/ATCC 8501
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
D-Glutamine and D-glutamate metabolism
-
Metabolic pathways
-
UDP-N-acetylmuramoyl-pentapeptide biosynthesis I (meso-DAP-containing)
-
UDP-N-acetylmuramoyl-pentapeptide biosynthesis II (lysine-containing)
-
SYSTEMATIC NAME
IUBMB Comments
Glutamate racemase
A pyridoxal-phosphate protein.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
BsGR
P94556
-
glutamate racemase
-
-
glutamate racemase
P56868
-
glutamate racemase
-
-
glutamate racemase
Q81LA8, Q81UL8
-
glutamate racemase
-
-
glutamate racemase
P94556
-
glutamate racemase
Q6L876
-
glutamate racemase
Q8REE6
-
glutamate racemase
-
-
glutamate racemase
-
-
glutamate racemase
-
-
glutamate racemase
-
-
MurI
P56868
-
RACE
Q6L876
-
RacE1
-
isozyme
RacE1
Q81UL8
-
RacE2
-
isozyme
RacE2
Q81LA8
-
Racemase, glutamate
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9024-08-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
; CU741; IFO 3336
-
-
Manually annotated by BRENDA team
enzyme genes glr and yrpC
-
-
Manually annotated by BRENDA team
IFO 3336
SwissProt
Manually annotated by BRENDA team
IFO 3336
-
-
Manually annotated by BRENDA team
isogenes racE and yrpC
-
-
Manually annotated by BRENDA team
Bacillus subtilis CU741
CU741
-
-
Manually annotated by BRENDA team
JM109/pGR3, overproducer of glutamate racemase and WM335 mutant defective in the gene of glutamate racemase
-
-
Manually annotated by BRENDA team
Fusobacterium varium NCTC 10560/ATCC 8501
-
-
-
Manually annotated by BRENDA team
J-99 strain, ARHp80 strain and SS1 strain
-
-
Manually annotated by BRENDA team
strain J99
Uniprot
Manually annotated by BRENDA team
Lactic acid bacteria
enzyme occurs exclusively in lactic acid bacteria
-
-
Manually annotated by BRENDA team
subsp. casei and subsp. rhamnosus
-
-
Manually annotated by BRENDA team
no activity in Clostridium sp.
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
essential enzyme in peptidoglycan biosynthesis
physiological function
Q8REE6
peptidoglycan synthesis
physiological function
-
peptidoglycan synthesis
physiological function
-
peptidoglycan synthesis
physiological function
Q6L876
peptidoglycan biosynthesis
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 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%
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-, P94556
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
-
-
-
-
D-Glu
L-Glu
show the reaction diagram
Bacillus subtilis CU741
-
-
-
-
D-glutamate
L-glutamate
show the reaction diagram
-
-
-
-
r
D-glutamate
L-glutamate
show the reaction diagram
-
-
-
-
r
D-glutamate
L-glutamate
show the reaction diagram
Q03469
-
-
-
r
D-glutamate
L-glutamate
show the reaction diagram
-
-
-
-
?
D-glutamate
L-glutamate
show the reaction diagram
-
-
-
-
?
D-glutamate
L-glutamate
show the reaction diagram
-
-
-
-
?
D-glutamate
L-glutamate
show the reaction diagram
-
catalytic action of glutamate racemase is driven by its own substrate, D-glutamate
-
-
r
D-glutamate
L-glutamate
show the reaction diagram
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
D-glutamate
L-glutamate
show the reaction diagram
Fusobacterium varium NCTC 10560/ATCC 8501
-
-
-
-
?
D-serine-O-sulfate
L-serine-O-sulfate
show the reaction diagram
-
-
-
-
r
L-2-aminoadipic acid
D-2-aminoadipic acid
show the reaction diagram
P94556
-
-
-
-
L-2-aminoadipic acid
D-2-aminoadipic acid
show the reaction diagram
Q8REE6
-
-
-
-
L-Glu
?
show the reaction diagram
-, P94556
glutamate racemase is mainly concerned in D-Glu synthesis for poly-gamma-glutamate production
-
-
-
L-Glu
?
show the reaction diagram
-
the biosynthesis of D-Glu, one of the essential components of bacterial cell-wall peptidoglycan, is catalyzed by glutamate racemase
-
-
-
L-Glu
?
show the reaction diagram
Lactic acid bacteria
-
the biosynthesis of D-Glu, one of the essential components of bacterial cell-wall peptidoglycan, is catalyzed by glutamate racemase
-
-
-
L-Glu
?
show the reaction diagram
Bacillus subtilis CU741
-
glutamate racemase is mainly concerned in D-Glu synthesis for poly-gamma-glutamate production
-
-
-
L-glutamate
D-glutamate
show the reaction diagram
-
-
-
-
?
L-glutamate
D-glutamate
show the reaction diagram
-
-
-
-
r
L-glutamate
D-glutamate
show the reaction diagram
-
-
-
-
r
L-glutamate
D-glutamate
show the reaction diagram
-
-
-
-
?
L-glutamate
D-glutamate
show the reaction diagram
Q9A1B7, -
-
-
-
r
L-glutamate
D-glutamate
show the reaction diagram
-
-
-
-
r
L-glutamate
D-glutamate
show the reaction diagram
-
-
-
-
?
L-glutamate
D-glutamate
show the reaction diagram
-
-
-
-
?
L-glutamate
D-glutamate
show the reaction diagram
-
-
-
-
r
L-glutamate
D-glutamate
show the reaction diagram
-
-
-
r
L-glutamate
D-glutamate
show the reaction diagram
Q03469
-
-
-
r
L-glutamate
D-glutamate
show the reaction diagram
-
-
-
-
?
L-glutamate
D-glutamate
show the reaction diagram
-
-
-
-
r
L-glutamate
D-glutamate
show the reaction diagram
-
-
-
-
?
L-glutamate
D-glutamate
show the reaction diagram
-, P94556
-
-
?
L-glutamate
D-glutamate
show the reaction diagram
-, Q81LA8, Q81UL8
-
-
-
r
L-glutamate
D-glutamate
show the reaction diagram
Q6L876
-
-
-
r
L-glutamate
D-glutamate
show the reaction diagram
-
the enzyme provides bacteria with a source of D-glutamate for use in peptidoglycan biosynthesis
-
?
L-glutamate
D-glutamate
show the reaction diagram
-, 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
show the reaction diagram
-
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
show the reaction diagram
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
show the reaction diagram
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-glutamate
D-glutamate
show the reaction diagram
-
-
-
-
?
L-glutamate
D-glutamate
show the reaction diagram
Fusobacterium varium NCTC 10560/ATCC 8501
-
-
-
-
?
L-Homocysteinesulfinate
D-Homocysteinesulfinate
show the reaction diagram
-, P94556
-
-
r
L-Homocysteinesulfinate
D-Homocysteinesulfinate
show the reaction diagram
-
slightly serves as substrate
-
-
additional information
?
-
-
enzyme does not catalyze the exchange between 2-oxolutarate and DL-Glu
-
-
-
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
?
-
-
the enzyme is an endogenous DNA gyrase inhibitor
-
?
additional information
?
-
-
enzyme exhibits both racemization activity and DNA gyrase inhibition. The two activities are unlinked and independent of each other. Enzyme-DNA gyrase interaction influences gyrase activity but has no effect on the racemization activity
-
-
-
additional information
?
-
-
in addition to racemization activity, enzyme exhibits DNA gyrase activity by preventing DNA binding of gyrase. Sequestration of gyrase results in inhibition of all reactions catalyzed by DNA gyrase. Overexpression additiionally provides protection against ciprofloxacin, 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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glutamate
L-glutamate
show the reaction diagram
-
catalytic action of glutamate racemase is driven by its own substrate, D-glutamate
-
-
r
D-glutamate
L-glutamate
show the reaction diagram
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
show the reaction diagram
P94556
-
-
-
-
L-2-aminoadipic acid
D-2-aminoadipic acid
show the reaction diagram
Q8REE6
-
-
-
-
L-Glu
?
show the reaction diagram
-, P94556
glutamate racemase is mainly concerned in D-Glu synthesis for poly-gamma-glutamate production
-
-
-
L-Glu
?
show the reaction diagram
-
the biosynthesis of D-Glu, one of the essential components of bacterial cell-wall peptidoglycan, is catalyzed by glutamate racemase
-
-
-
L-Glu
?
show the reaction diagram
Lactic acid bacteria
-
the biosynthesis of D-Glu, one of the essential components of bacterial cell-wall peptidoglycan, is catalyzed by glutamate racemase
-
-
-
L-Glu
?
show the reaction diagram
Bacillus subtilis CU741
-
glutamate racemase is mainly concerned in D-Glu synthesis for poly-gamma-glutamate production
-
-
-
L-glutamate
D-glutamate
show the reaction diagram
-
-
-
-
?
L-glutamate
D-glutamate
show the reaction diagram
-
-
-
r
L-glutamate
D-glutamate
show the reaction diagram
-
-
-
-
r
L-glutamate
D-glutamate
show the reaction diagram
Q6L876
-
-
-
r
L-glutamate
D-glutamate
show the reaction diagram
-, 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
show the reaction diagram
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
show the reaction diagram
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
?
-
-
enzyme exhibits both racemization activity and DNA gyrase inhibition. The two activities are unlinked and independent of each other. Enzyme-DNA gyrase interaction influences gyrase activity but has no effect on the racemization activity
-
-
-
additional information
?
-
-
in addition to racemization activity, enzyme exhibits DNA gyrase activity by preventing DNA binding of gyrase. Sequestration of gyrase results in inhibition of all reactions catalyzed by DNA gyrase. Overexpression additiionally provides protection against ciprofloxacin
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme is cofactor-independent
-
additional information
-
no cofactor required
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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
-
IC50: 0.01 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(2-bromo)benzyl pentanedioic acid
-
IC50: 6.3 mg/l, minimum inhibitor concentration: 31.3 mg/l
(2R,4S)-2-amino-4-(2-chloro)benzyl pentanedioic acid
-
IC50: 7.1 mg/l, minimum inhibitor concentration: 3.9 mg/l
(2R,4S)-2-amino-4-(2-naphthyl)methyl pentanedioic acid
-
IC50: 0.1 mg/l, minimum inhibitor concentration: 0.25 mg/l
(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-(3,4,5-trimethoxy)benzyl pentanedioic acid
-
IC50: 81 mg/l, minimum inhibitor concentration: above 250 mg/l
(2R,4S)-2-amino-4-(3,5-dichloro)benzyl pentanedioic acid
-
IC50: 3.0 mg/l, minimum inhibitor concentration: 3.9 mg/l
(2R,4S)-2-amino-4-(3-benzo[b]thienyl)methyl pentanedioic acid
-
IC50: 1.7 mg/l, minimum inhibitor concentration: 7.8 mg/l
(2R,4S)-2-amino-4-(3-bromo)benzyl pentanedioic acid
-
IC50: 0.13 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(3-chloro)benzyl pentanedioic acid
-
IC50: 3.4 mg/l, minimum inhibitor concentration: 1.0 mg/l
(2R,4S)-2-amino-4-(3-cyclohexyl)propyl pentanedioic acid
-
IC50: 0.6 mg/l, MIC: 2.0 mg/l
(2R,4S)-2-amino-4-(3-methoxy)benzyl pentanedioic acid
-
IC50: 0.2 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(3-nitro)benzyl pentanedioic acid
-
IC50: 5.2 mg/l, minimum inhibitor concentration: 2.0 mg/l
(2R,4S)-2-amino-4-(3-phenyl)benzyl pentanedioic acid
-
IC50: 0.7 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(3-phenyl)propargyl pentanedioic acid
-
IC50: 0.37 mg/l, minimum inhibitor concentration: 2.0 mg/l
(2R,4S)-2-amino-4-(3-phenyl)propyl pentanedioic acid
-
IC50: 0.5 mg/l, minimum inhibitor concentration: 3.9 mg/l
(2R,4S)-2-amino-4-(3-trifluoromethyl)benzyl pentanedioic acid
-
IC50: 0.8 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(4-chloro)benzyl pentanedioic acid
-
IC50: 0.3 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(4-methoxy)benzyl pentanedioic acid
-
IC50: 0.1 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-(4-nitro)benzyl pentanedioic acid
-
IC50: 5.2 mg/l, minimum inhibitor concentration: 2.0 mg/l
(2R,4S)-2-amino-4-(4-phenyl)benzyl pentanedioic acid
-
IC50: 0.078 mg/l, minimum inhibitor concentration: 1.0 mg/l
(2R,4S)-2-amino-4-(4-tert-butyl)benzyl pentanedioic acid
-
IC50: 0.6 mg/l, minimum inhibitor concentration: 1.0 mg/l
(2R,4S)-2-amino-4-(4-trifluoromethyl)benzyl pentanedioic acid
-
IC50: 0.8 mg/l, minimum inhibitor concentration: 7.8 mg/l
(2R,4S)-2-amino-4-(5-phenyl-2E,4E-pentadienyl)pentanedioic acid
-
IC50: 9.1 mg/l, minimum inhibitor concentration: 3.9 mg/l
(2R,4S)-2-amino-4-(prop-2-ynyl) pentanedioic acid
-
IC50: 5.5 mg/l, MIC: 31.3 mg/l
(2R,4S)-2-amino-4-[3-(2-benzo[b]thienyl)]benzyl pentanedioic acid
-
IC50: 0.3 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2R,4S)-2-amino-4-[3-(2-furyl)]benzyl pentanedioic acid
-
IC50: 0.5 mg/l, minimum inhibitor concentration: 0.24 mg/l
(2R,4S)-2-amino-4-[4-(2-benzo[b]thienyl)]benzyl pentanedioic acid
-
IC50: 0.65 mg/l, minimum inhibitor concentration: 3.9 mg/l
(2R,4S)-2-amino-4-[4-(2-naphthyl)]benzyl pentanedioic acid
-
IC50: 0.42 mg/l, minimum inhibitor concentration: 7.8 mg/l
(2R,4S)-2-amino-4-[4-(3-thienyl)]benzyl pentanedioic acid
-
IC50: 0.32 mg/l, minimum inhibitor concentration: 0.24 mg/l
(2R,4S)-2-amino-4-[4-(n-benzenesulfonylamino)]benzyl pentanedioic acid
-
IC50: 10.2 mg/l, minimum inhibitor concentration: above 250 mg/l
(2R,4S)-2-amino-4-[4-(N-phenylaminocarbonyl)amino]-benzyl pentanedioic acid
-
IC50: 0.49 mg/l, minimum inhibitor concentration: 15.6 mg/l
(2R,4S,E)-2-amino-4-(3-phenylprop-2-enyl) pentanedioic acid
-
IC50: 0.1 mg/l, minimum inhibitor concentration: 0.4 mg/l
(2R,4S,E)-2-amino-4-(3-phenylprop-2-enyl)pentanedioic acid
-
D-glutamate analog, good competitive inhibitor for RacE1; D-glutamate analog, only weak inhibitor of RacE2, but a potent competitive inhibitor for mutant V149A
(2R,4S,E)-2-amino-4-[3-(2-naphthyl)prop-2-enyl]pentanedioic acid
-
IC50: 0.5 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2S,4R)-2-amino-4-benzyl pentanedioic acid
-
IC50: 0.3 mg/l, minimum inhibitor concentration: 0.5 mg/l
(2S,4S)-2-amino-4-(1-naphthyl)methyl pentanedioic acid
-
IC50: 5.6 mg/l, minimum inhibitor concentration: 3.9 mg/l
(4R,2S)-2-cinnamyl-4-amino-5-hydroxypentanoic acid
-
D-glutamate analog, good competitive inhibitor for RacE1; D-glutamate analog, only weak inhibitor of RacE2, but a potent competitive inhibitor for mutant V149A
2-(2-Carboxyethyl)aziridine-2-carboxylic acid
-
i.e. aziridino-glutamate, inactivates glutamate racemase by alkylating an active site Cys residue
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
Q836J0
comparison with effect on Enterococcus faecium and Staphylococcus aureus
2-(butylsulfanyl)-9-(2-methoxy-5-nitrobenzyl)-9H-purin-6-amine
Q836J0
comparison with effect on Enterococcus faecalis and Staphylococcus aureus
2-(butylsulfanyl)-9-(2-methoxy-5-nitrobenzyl)-9H-purin-6-amine
Q9ZLT0
analysis of mouse and human internal clearance
2-(butylsulfanyl)-9-(3-chloro-2,6-difluorobenzyl)-9H-purin-6-amine
Q836J0
comparison with effect on Enterococcus faecium and Staphylococcus aureus
2-(butylsulfanyl)-9-(3-chloro-2,6-difluorobenzyl)-9H-purin-6-amine
Q836J0
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
Q836J0
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
Q836J0
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
Q9ZLT0
-
2-hydroxy-3,4,5-trioxocyclopent-1-en-1-olate
-
-
2-nitro-5-thiocyanatobenzoate
-, P94556
0.2 mM
2-Nitro-5-thiocyanobenzoate
-
-
2-Nitro-5-thiocyanobenzoate
-
complete inactivation at 0.1 mM
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
Q9ZLT0
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
Q9ZLT0
analysis of mouse and human internal clearance
3-(3-chlorothiophen-2-yl)-5-(furan-2-yl)-N-methyl-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Q9ZLT0
uncompetitive, inhibitor with improved solubility and reduced plasma protein binding, binds at the enzyme dimer interface
3-hydroxypropyl FAD
-
-
3-sulfobenzoic acid
Q6L876
structural analogue of dipicolinate dianion
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
4-chlorobenzene-1,2,3-triol
-
noncompetitive inhibition
-
4-Hydroxypropyl FAD
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5-(furan-2-yl)-N-methyl-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Q9ZLT0
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
-
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
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]-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
Q9ZLT0
analysis of mouse and human internal clearance
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
Q836J0
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
Q836J0
comparison with effect on Enterococcus faecalis and Staphylococcus aureus
benzene-1,3-disulfonate
-
-
-
D-Gln
-
competitive
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
dipicolinate dianion
Q6L876
DPA
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
Q9A1B7, -
potent competitive inhibitor that induces a disorder in one of the loops near the active site
hydroxylamine
-
different experimentators found inhibition or no inhibition
hydroxylamine
-
no inactivation
L-alpha-Aminohexanedioate
-
-
L-N-Hydroxyglutamate
-
weak
N,8-dimethyl-5-phenyl-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Q9ZLT0
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
Q9ZLT0
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
Q9ZLT0
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
Q9ZLT0
uncompetitive, inhibitor with improved solubility and reduced plasma protein binding, binds at the enzyme dimer interface
p-chloromercuribenzoate
-
-
riboflavin
-
slight inhibition, restoration by FAD
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
Thiol-blocking reagents
-
DL-Glu protects from inactivation
-
Thiol-blocking reagents
-
-
-
[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
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
additional information
-
no inactivation by carbonyl reagents such as hydroxylamine and NaBH4
-
additional information
-
insensitive to carbonyl reagents such as hydroxylamine, phenylhydrazine, or NaBH4
-
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
Q8REE6
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
UDP-MurNAc-Ala
-
strong activation by UDP-MurNAc-Ala, the product of the preceding enzyme in the peptidoglycan biosynthetic pathway
UDP-N-acetylmuramyl-L-Ala
-
absolutely required
UDP-N-acetylmuramyl-L-Ala
-
activator
additional information
-
-
-
additional information
-
not stimulated by the addition of pyridoxal 5'-phosphate
-
additional information
-
cofactor-independent enzyme
-
additional information
-
cofactor-independent enzyme
-
additional information
-
pyridoxal phosphate-independent enzyme
-
additional information
-, P94556
cofactor-independent enzyme
-
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4.2
-
D-Glu
-
in presence of 0.0065 mM of the activator UDP-N-acetylmuramyl-L-Ala
18.9
-
D-Glu
-
without activator
0.014
-
D-glutamate
-
-
0.063
-
D-glutamate
-
-
0.07
-
D-glutamate
-
recombinant wild type enzyme, reactions are conducted at 25C 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 25C 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 25C 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 25C 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 25C 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 25C 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
0.2
-
D-glutamate
-
-
0.21
-
D-glutamate
-
-
0.24
-
D-glutamate
-
-
0.25
-
D-glutamate
-
-
0.25
-
D-glutamate
-
mutant K29A, reactions are conducted at 25C 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
Q6L876
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
0.26
-
D-glutamate
-
pH 8, 30C, wild-type enzyme
0.275
-
D-glutamate
-
deletion mutant A75T
0.282
-
D-glutamate
-
deletion mutant E151T
0.3
-
D-glutamate
-
mutant R214A, reactions are conducted at 25C 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
0.35
-
D-glutamate
-
pH 8.5, mutant enzyme D7S
0.42
-
D-glutamate
-
mutant K106A, reactions are conducted at 25C 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
0.55
-
D-glutamate
-
pH 8.5, wild-type enzyme
0.77
-
D-glutamate
Q81LA8, Q81UL8
-
0.9
-
D-glutamate
-
-
1
-
D-glutamate
Q81LA8, Q81UL8
-
1.2
-
D-glutamate
-
pH 8, 30C, mutant enzyme D10N
1.5
-
D-glutamate
Q8REE6
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
1.7
-
D-glutamate
P94556
His-tagged recombinant BsGR, in potassium phosphate buffer (10 mM, pH 8.0)
1.7
-
D-glutamate
Q8REE6
recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
2.1
-
D-glutamate
-
-
2.5
-
D-glutamate
-, P94556
pH 8.0, 37C
3
-
D-glutamate
-
pH 8.5, mutant enzyme E147N
3.5
-
D-glutamate
-
pH 8, 30C, mutant enzyme H152Q
4.5
-
D-glutamate
-
pH 8, 30C, mutant enzyme H186N
8.6
-
D-glutamate
Q6L876
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
P94556
His-tagged recombinant BsGR mutant V149A, in potassium phosphate buffer (10 mM, pH 8.0)
41
-
D-glutamate
-
pH 8, 30C, mutant enzyme D36N
126
-
D-glutamate
Q9A1B7, -
-
10
-
D-Homocysteinesulfinate
-, P94556
pH 8.0, 37C
26
-
L-2-aminoadipic acid
Q8REE6
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
0.33
-
L-glutamate
-
pH 8, 30C, wild-type enzyme
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
Q8REE6
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
1.04
-
L-glutamate
Q8REE6
recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
1.1
-
L-glutamate
-
pH 8, 30C, mutant enzyme H186N
1.1
-
L-glutamate
-
-
1.3
-
L-glutamate
-
pH 8, 30C, mutant enzyme D10N
3.2
-
L-glutamate
-
pH 8.5, mutant enzyme E147N
3.3
-
L-glutamate
-
pH 8.5, wild-type enzyme
3.7
-
L-glutamate
-
-
3.74
-
L-glutamate
Q9A1B7, -
-
4.1
-
L-glutamate
-
mutant P99A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
4.6
-
L-glutamate
-
-
5.8
-
L-glutamate
-
pH 8, 30C, mutant enzyme H152Q
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
7.36
-
L-glutamate
-
deletion mutant E151T
7.4
-
L-glutamate
-
deletion mutant A75T
8
-
L-glutamate
-
-
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
-
pH 8.5, mutant enzyme D7S
11
-
L-glutamate
-
mutant R214A/K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
14
-
L-glutamate
Q81LA8, Q81UL8
-
14
-
L-glutamate
P94556
His-tagged recombinant BsGR, in potassium phosphate buffer (10 mM, pH 8.0)
14
-
L-glutamate
Q6L876
wild type enzyme, 50 mM boric acid, 100 mM KCl, 0.2 mM dithiothreitol, pH 8.0 at 25C in the presence of 0.22 microM glutamate racemase
35
-
L-glutamate
-
pH 8, 30C, mutant enzyme D36N
38
-
L-glutamate
Q81LA8, Q81UL8
-
47
-
L-glutamate
P94556
His-tagged recombinant BsGR mutant V149A, in potassium phosphate buffer (10 mM, pH 8.0)
50
-
L-glutamate
-, P94556
pH 8.0, 37C
200
-
L-Homocysteinesulfinate
-, P94556
pH 8.0, 37C
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00034
-
D-glutamate
-
pH 8.5, mutant enzyme D7S
0.056
-
D-glutamate
-
pH 8.5, wild-type enzyme
0.063
-
D-glutamate
-
pH 8, 30C, mutant enzyme D10N
0.065
-
D-glutamate
-
deletion mutant A75T
0.08
-
D-glutamate
-
deletion mutant E151T
0.093
-
D-glutamate
-
pH 8, 30C, mutant enzyme H186N
0.2
-
D-glutamate
-
-
0.41
-
D-glutamate
-
-
0.43
-
D-glutamate
Q6L876
mutant T76A, at 25C 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
0.49
-
D-glutamate
Q9A1B7, -
-
0.56
-
D-glutamate
-
-
1.3
-
D-glutamate
Q6L876
wild type enzyme, at 25C 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
1.6
-
D-glutamate
-
-
1.8
-
D-glutamate
Q81LA8, Q81UL8
-
2
-
D-glutamate
Q81LA8, Q81UL8
-
3.3
-
D-glutamate
-
-
3.9
-
D-glutamate
-
-
8.3
-
D-glutamate
P94556
His-tagged recombinant BsGR, in potassium phosphate buffer (10 mM, pH 8.0)
11.73
-
D-glutamate
-
-
15
-
D-glutamate
-
-
15
-
D-glutamate
P94556
His-tagged recombinant BsGR mutant V149A, in potassium phosphate buffer (10 mM, pH 8.0)
22
-
D-glutamate
-
pH 8, 30C, mutant enzyme D36N and H152Q
22
-
D-glutamate
Q8REE6
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
26
-
D-glutamate
Q8REE6
recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
43.33
-
D-glutamate
-
-
68
-
D-glutamate
-
pH 8, 30C, wild-type enzyme
780
-
D-glutamate
-
recombinant wild type enzyme, reactions are conducted at 25C 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 25C 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 25C 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 25C 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 25C 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 25C 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 25C 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 25C 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 25C 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
2.4
-
L-2-aminoadipic acid
Q8REE6
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
0.0023
-
L-glutamate
-
pH 8.5, mutant enzyme E147N
0.0047
-
L-glutamate
-
pH 8.5, mutant enzyme E147N
0.037
-
L-glutamate
-
pH 8.5, mutant enzyme D7S
0.045
-
L-glutamate
-
pH 8, 30C, mutant enzyme H186N
0.068
-
L-glutamate
-
pH 8, 30C, mutant enzyme D10N
0.21
-
L-glutamate
-
pH 8.5, wild-type enzyme
0.41
-
L-glutamate
-
-
1.05
-
L-glutamate
-
-
1.63
-
L-glutamate
Q9A1B7, -
-
1.78
-
L-glutamate
-
deletion mutant A75T
2.26
-
L-glutamate
-
deletion mutant E151T
3.4
-
L-glutamate
-
-
6.8
-
L-glutamate
-
pH 8.0, 30C
8.5
-
L-glutamate
-
-
12
-
L-glutamate
Q81LA8, Q81UL8
-
12.16
-
L-glutamate
-
-
13.8
-
L-glutamate
Q8REE6
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
17.4
-
L-glutamate
Q8REE6
recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
17.7
-
L-glutamate
-
-
18
-
L-glutamate
Q81LA8, Q81UL8
-
20
-
L-glutamate
-
pH 8, 30C, mutant enzyme D36N
25
-
L-glutamate
-
-
36.66
-
L-glutamate
-
-
38
-
L-glutamate
-
pH 8, 30C, mutant enzyme H152Q
38
-
L-glutamate
-
-
63
-
L-glutamate
P94556
His-tagged recombinant BsGR, in potassium phosphate buffer (10 mM, pH 8.0)
69
-
L-glutamate
-
pH 8, 30C, wild-type enzyme
76
-
L-glutamate
P94556
His-tagged recombinant BsGR mutant V149A, in potassium phosphate buffer (10 mM, pH 8.0)
87
-
L-glutamate
Q6L876
wild type enzyme, 50 mM boric acid, 100 mM KCl, 0.2 mM dithiothreitol, pH 8.0, at 25C 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
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0031
-
D-glutamate
-
recombinant wild type enzyme, reactions are conducted at 25C 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
9221
0.0035
-
D-glutamate
-
mutant K106A, reactions are conducted at 25C 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
9221
0.0059
-
D-glutamate
-
mutant Y221A, reactions are conducted at 25C 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
9221
0.006
-
D-glutamate
-
mutant Q86A, reactions are conducted at 25C 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
9221
0.0062
-
D-glutamate
-
mutant R214A, reactions are conducted at 25C 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
9221
0.0083
-
D-glutamate
-
mutant K29A, reactions are conducted at 25C 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
9221
0.0125
-
D-glutamate
-
mutant P99A, reactions are conducted at 25C 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
9221
0.0139
-
D-glutamate
-
mutant R214A/K106A, reactions are conducted at 25C 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
9221
0.015
-
D-glutamate
-
mutant R25A, reactions are conducted at 25C 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
9221
1.5
-
D-glutamate
P94556
His-tagged recombinant BsGR mutant V149A, in potassium phosphate buffer (10 mM, pH 8.0)
9221
4
-
D-glutamate
Q8REE6
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
9221
5
-
D-glutamate
P94556
His-tagged recombinant BsGR, in potassium phosphate buffer (10 mM, pH 8.0)
9221
15
-
D-glutamate
Q8REE6
recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
9221
0.09
-
L-2-aminoadipic acid
Q8REE6
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
293336
0.0045
-
L-glutamate
-
mutant Q86A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
12211
0.0053
-
L-glutamate
-
recombinant wild type enzyme, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
12211
0.0056
-
L-glutamate
-
mutant K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
12211
0.007
-
L-glutamate
-
mutant R214A/K106A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
12211
0.0071
-
L-glutamate
-
mutant Y221A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
12211
0.0098
-
L-glutamate
-
mutant R214A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
12211
0.0111
-
L-glutamate
-
mutant P99A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
12211
0.0118
-
L-glutamate
-
mutant K29A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
12211
0.014
-
L-glutamate
-
mutant R25A, in 10 mM potassium phosphate (pH 8.2) and 0.2 mM dithiothreitol
12211
1.8
-
L-glutamate
P94556
His-tagged recombinant BsGR mutant V149A, in potassium phosphate buffer (10 mM, pH 8.0)
12211
4.6
-
L-glutamate
P94556
His-tagged recombinant BsGR, in potassium phosphate buffer (10 mM, pH 8.0)
12211
15
-
L-glutamate
Q8REE6
His-tagged recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
12211
17
-
L-glutamate
Q8REE6
recombinant FnGR, in potassium phosphate buffer (10 mM, pH 8.0)
12211
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
0.042
-
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
-
0.0058
-
D-glutamate
-
-
0.661
-
D-glutamate
-
deletion mutant A75T
100
-
D-glutamate
-
value above 100 for deletion mutant E151K
1.97
-
dipicolinate dianion
Q6L876
competitive inhibition
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
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0009
-
2-(butylsulfanyl)-8-(4-fluorobenzyl)-4-(methylamino)-5,8-dihydropteridine-6,7-dione
-
-
0.0038
-
2-(butylsulfanyl)-8-(4-fluorobenzyl)-4-(methylamino)-5,8-dihydropteridine-6,7-dione
-
-
0.0014
-
2-(butylsulfanyl)-9-(2-methoxy-5-nitrobenzyl)-9H-purin-6-amine
Q836J0
-
0.0025
-
2-(butylsulfanyl)-9-(2-methoxy-5-nitrobenzyl)-9H-purin-6-amine
Q836J0
-
0.0022
-
2-(butylsulfanyl)-9-(3-chloro-2,6-difluorobenzyl)-9H-purin-6-amine
Q836J0
-
0.0026
-
2-(butylsulfanyl)-9-(3-chloro-2,6-difluorobenzyl)-9H-purin-6-amine
Q836J0
-
0.007
-
2-(butylsulfanyl)-9-(4-nitrophenyl)-9H-purin-6-amine
-
-
0.018
-
2-(butylsulfanyl)-9-(4-nitrophenyl)-9H-purin-6-amine
-
-
0.4
-
2-(butylsulfanyl)-9-(4-nitrophenyl)-9H-purin-6-amine
-
-
0.000026
-
2-butoxy-9-(3-chloro-2,6-difluorobenzyl)-N-(pyridin-3-ylmethyl)-9H-purin-6-amine
Q9ZLT0
-
0.002
-
2-butoxy-9-(3-chloro-2,6-difluorobenzyl)-N-(pyridin-3-ylmethyl)-9H-purin-6-amine
Q836J0
-
0.0027
-
2-butoxy-9-(3-chloro-2,6-difluorobenzyl)-N-(pyridin-3-ylmethyl)-9H-purin-6-amine
Q836J0
-
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
Q9ZLT0
-
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
Q9ZLT0
-
0.0028
-
3-(3-chlorothiophen-2-yl)-5-(furan-2-yl)-N-methyl-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Q9ZLT0
-
2.9
-
3-sulfobenzoic acid
Q6L876
structural analogue of dipicolinate dianion
0.0015
-
4-amino-2-(butylsulfanyl)-8-(2,6-difluorobenzyl)-5,8-dihydropteridine-6,7-dione
-
-
0.0031
-
4-amino-2-(butylsulfanyl)-8-(2,6-difluorobenzyl)-5,8-dihydropteridine-6,7-dione
-
-
0.00065
-
4-amino-2-(butylsulfanyl)-8-(3,4-dichlorobenzyl)-5,8-dihydropteridine-6,7-dione
-
-
0.0015
-
4-amino-2-(butylsulfanyl)-8-(3,4-dichlorobenzyl)-5,8-dihydropteridine-6,7-dione
-
-
0.0011
-
4-amino-2-(butylsulfanyl)-8-(4-fluorobenzyl)-5,8-dihydropteridine-6,7-dione
-
-
0.0035
-
4-amino-2-(butylsulfanyl)-8-(4-fluorobenzyl)-5,8-dihydropteridine-6,7-dione
-
-
0.0076
-
4-amino-8-benzyl-2-(benzylsulfanyl)-5,8-dihydropteridine-6,7-dione
-
-
0.021
-
4-amino-8-benzyl-2-(benzylsulfanyl)-5,8-dihydropteridine-6,7-dione
-
-
0.0024
-
4-amino-8-benzyl-2-(butylsulfanyl)-5,8-dihydropteridine-6,7-dione
-
-
0.0064
-
4-amino-8-benzyl-2-(butylsulfanyl)-5,8-dihydropteridine-6,7-dione
-
-
0.0019
-
4-amino-8-benzyl-2-(cyclopentylsulfanyl)-5,8-dihydropteridine-6,7-dione
-
-
0.052
-
4-amino-8-benzyl-2-(cyclopentylsulfanyl)-5,8-dihydropteridine-6,7-dione
-
-
0.002
-
5-(furan-2-yl)-N-methyl-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Q9ZLT0
-
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
Q9ZLT0
-
0.0043
-
9-(2,6-difluoro-3-methylbenzyl)-2-[(1,1,1,2,2-pentafluoropentan-3-yl)oxy]-9H-purin-6-amine
Q836J0
-
0.0044
-
9-(2,6-difluoro-3-methylbenzyl)-2-[(1,1,1,2,2-pentafluoropentan-3-yl)oxy]-9H-purin-6-amine
Q836J0
-
0.0044
-
exiguaquinol
-
substrate D-serine-O-sulfate
0.361
-
exiguaquinol
-
substrate D-glutamate
0.0017
-
N,8-dimethyl-5-phenyl-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Q9ZLT0
-
0.0007
-
N-methyl-3,5-di(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Q9ZLT0
-
0.0006
-
N-methyl-5-(1H-pyrrol-3-yl)-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Q9ZLT0
-
0.0022
-
N-methyl-5-phenyl-3-(thiophen-2-yl)-3H-pyrido[2,3-e][1,4]diazepin-2-amine
Q9ZLT0
-
0.0014
-
pyrazolopyrimidinedione analogue
-
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
-
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
-
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
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
12
-
-
pH 8.0, 30C
42
-
-, P94556
-
45.7
-
Q03469
pH 8.5
158
-
-
enzyme from Lactobacillus fermenti
161
-
-
enzyme expressed in Escherichia coli
additional information
-
-
-
additional information
-
Q03469
polarimetric assay method, protocol for measurement of enzyme activity in 96-well microtiter plates
additional information
-
Q81LA8, Q81UL8
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
-
-
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
-
-
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
-
-
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
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
Q9A1B7, -
assay at
8
-
-, P94556
-
8
-
-
soluble and immobilized enzyme
8.1
-
Q81LA8, Q81UL8
maximum activity
8.2
-
Q81LA8, Q81UL8
maximum activity
8.2
-
-
assay at
8.5
-
P94556
5 mM Tris-HCl
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
-, P94556
enzyme shows significant activity in the range pH 7.0-10.0
8
8.5
Q8REE6
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
Q8REE6
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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
Q81LA8, Q81UL8
assay at; assay at
25
-
-
assay at
30
-
Q9A1B7, -
assay at
37
-
-, P94556
-
40
-
-
soluble and immobilized enzyme
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
70
-
20C: about 65% of maximal activity, 70C: about 30% of maximal activity, soluble enzyme; more than 80% of maximal activity is observed between 20C and 70C, immobilized enzyme
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-, P94556
highest activity in the early stationary phase of growth
Manually annotated by BRENDA team
Bacillus subtilis CU741
-
highest activity in the early stationary phase of growth
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the overexpression results in the formation of inclusion bodies, little activity is found in the soluble fraction
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Escherichia coli (strain K12)
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)
Staphylococcus aureus (strain MRSA252)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20000
-
-
gel filtration
23000
-
-
gel filtration
28800
-
-
MALDI-TOF analysis
29000
-
-
gel filtration
29000
-
Q9A1B7, -
method not indicated
29000
-
-
calculated from amino acid sequence
29140
-
-
calculation from nucleotide sequence
29430
-
-
calculation from nucleotide sequence
30000
-
-
gel filtration
30000
-
-, P94556
; gel filtration
32050
-
Q8REE6
calculated His-tagged FnGR
32130
-
P94556
calculated His-BsGR V149A
32160
-
P94556
calculated His-tagged BsGR
32320
-
Q81LA8, Q81UL8
predicted cDNA
32530
-
Q81LA8, Q81UL8
predicted from cDNA
34000
-
P94556
BsGR, determined by gel filtration
35000
-
Q8REE6
FnGR, determined by SDS-PAGE
37000
-
-
gel filtration
40000
-
-
HPLC gel filtration
additional information
-
-
glutamate racemase shows significant sequence homology with mammalian myoglobins, in particular, in the regions corresponding to the E and F helices
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 31000
dimer
-
each monomer consists of two alpha/beta fold domains
dimer
-
both enzymes RacE1 and Rac2 are dimers with monomers arranged in a tail-to-tail orientation which is determined by gel filtration
dimer
Q9A1B7, -
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
dimer
Q8REE6
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
-
determined by gel filtration, RacE2 exist as a dimer in solution, but the monomeric enzyme is more active than the dimeric form
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
-
1 * 40000, SDS-PAGE
monomer
-
1 * 29000, SDS-PAGE
monomer
-
1 * 29000, SDS-PAGE
monomer
-
1 * 30000, SDS-PAGE
monomer
-, P94556
1 * 29866, calculation from nucleotide sequence; 1 * 30000; 1 * 30000, SDS-PAGE
monomer
-
1 * 37000, calculated
monomer
Q81LA8, Q81UL8
gel filtration
monomer
P94556
determined by gel filtration, BsGR is a monomeric enzyme, which dimerizes in the presence of either 10 mM D- or L-glutamate
monomer
-
mutants R25A and K106A/R214A are completely monomeric at the concentration of 5 mg/ml
additional information
Q81LA8, Q81UL8
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
in complex with D-glutamate
-
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
-
in complex with 9-benzyl purine inhibitors
Q836J0
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
-
in complex with 9-benzyl purine inhibitors
Q836J0
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
-
in complex with pyridodiazepine amine inhibitors
Q9ZLT0
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
-
recombinant enzyme
-
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.
Q9A1B7, -
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
8.5
-
25C, 15 min, stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-, P94556
fully stable up to
49
-
-
Tm value (midpoint of thermal unfolding) of the wild type enzyme
50
-
-, P94556
pH 8.0, 0.1 M Tris-HCl buffer containing 10% glycerol, retains 90% of its activity after 10 min
51
-
-
Tm value (midpoint of thermal unfolding) of the R25A mutant
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
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stabilized by immobilization to Chitopearl 2505 or Chitopearl 2605. The enzyme remains active at 4C for 30 days, remaining activity is 32%
-
stabilized by presence of reduced thiols. After 3 h at 30C, 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
-
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
-
repeated thawing and melting of the enzyme causes inactivation
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
no loss of activity is noted after the enzyme is stored at 80C for more than 8 months, at least 80% of enzyme activity is retained after incubation for 8 h at 4C
Q8REE6
enzyme can be kept frozen at all stages of the purification for several weeks without loss of activity
-
-20C, 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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate precipitation, Co2+-affinity column chromatography, and anion-exchange chromatography
-
by using nickel-nitrilotriacetic acid affinity chromatography and gel filtration
-
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
-
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
Q81LA8, Q81UL8
-
-, P94556
by using nickel-chelate chromatography
Q6L876
by using of nickel ion affinity chromatography at 4C
P94556
enzyme is purified by using standard chromatographic methods
-
enzyme is purified by using standard chromatographic methods
-
by using of nickel ion affinity chromatography at 4C
Q8REE6
ammonium sulfate precipitation
-
enzyme is purified by using standard chromatographic methods
-
enzyme is purified by using standard chromatographic methods
-
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
Q9A1B7, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cloned in Escherichia coli as a fusion protein with a 6xHis tag at the N-terminus
-
cloned in Escherichia coli; cloned in Escherichia coli
Q81LA8, Q81UL8
expressed in Escherichia coli BL21(DE3) cells
-
recombinant wild type and mutants are expressed in BL21(DE3) Escherichia coli cells
-
expressed in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
overexpression in BL21(DE3) Escherichia coli as fusion protein bearing an N-terminal hexahistidine tag
P94556
overexpression in Escherichia coli JM109
-, P94556
recombinant wild type and mutant proteins are expressed in Escherichia coli cells
Q6L876
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
Q8REE6
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
-
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
-
expression in Escherichia coli
-
expression in Escherichia coli
-
overexpression in homologous expression system
-
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
-
cloned in Escherichia coli as a fusion protein with a 6x His tag at the N-terminus
Q9A1B7, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
Q81LA8, Q81UL8
predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold
C188A
Q81LA8, Q81UL8
predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold
C74A
Q81LA8, Q81UL8
predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold
C77A
Q81LA8, Q81UL8
predicted active site is mutated by site-directed mutagenesis, detectable racemase activity is attenuated by at least 100fold
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
K106A
-
the isozyme RacE2 mutant is insensitive to dipicolinic acid
P99A
-
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
-
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
-
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
-
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
-
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
S207A
-
the isozyme RacE2 mutant is insensitive to dipicolinic acid
V149A
-
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)
T76A
Q6L876
production by site-directed mutagenesis, strong RacE-glutamate carbanion interaction energy is notably dissipated with the mutant
A151V
Q8REE6
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
-
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
-
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
-
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
-
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
-
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
-
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
-
decrease in racemization activity, mutant retains its gyrase inhibition ability
C75S
-
decrease in racemization activity, mutant retains its gyrase inhibition ability
K29A
-
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
additional information
Q81LA8, Q81UL8
RacE1 and RacE2 share 51% sequence identity and 67% sequence similarity; RacE1 and RacE2 share 51% sequence identity and 67% sequence similarity
Y221A
-
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
additional information
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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
V149A
P94556
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
additional information
-
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
C75SC185S
-
less than 10% of wild-type activity, mutant retains its gyrase inhibition ability
additional information
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overexpression in vivo provides resistance to the action of ciprofloxacin
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
drug development
-
einzyme is potentially an attractive target for the development of new antibacterial agents because of being an essential enzyme
drug development
P94556
enzyme is an attractive target for the development of antibacterial agents
drug development
Q6L876
glutamate racemase is an attractive target for the design of antibacterial agents
synthesis
-
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
-
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
Q8REE6
enzyme is an attractive target for the development of antibacterial agents
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
-
glutamate racemase is an enzyme essential to the bacterial cell wall biosynthesis pathway, and is therefore considered as a target for antibacterial drug discovery
medicine
-
the enzyme may be a viable target for developing new antibacterial agents