5.1.1.3: glutamate racemase
This is an abbreviated version!
For detailed information about glutamate racemase, go to the full flat file.
Word Map on EC 5.1.1.3
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5.1.1.3
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peptidoglycan
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l-glutamate
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cofactor-independent
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drug development
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pediococcus
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poly-gamma-glutamate
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pyrophilus
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pentosaceus
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fermenti
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ciceri
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stereoinversion
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medicine
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synthesis
- 5.1.1.3
- peptidoglycan
- l-glutamate
-
cofactor-independent
- drug development
- pediococcus
-
poly-gamma-glutamate
- pyrophilus
- pentosaceus
- fermenti
-
ciceri
-
stereoinversion
- medicine
- synthesis
Reaction
Synonyms
AAR, BAS0806, BAS4379, BcGR, BsGR, BsRacE, CBL/ALR, cystathionine beta-lyase, D-glutamate racemase, DapF, FnGR, GBAA_0847, GBAA_4717, GLR, GluR, glutamate racemase, glutamic acid racemases, GRL, HpMurI, MetC, More, MurI, RACE, RacE1, RacE2, Racemase, glutamate, Rv1338, TmCBL, wMelCBL
ECTree
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Reaction
Reaction on EC 5.1.1.3 - glutamate racemase
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deprotonation/protonation mechanism for racemization in which the breaking of the carbon-hydrogen bond at C-2 is partially rate-determining
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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
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L-glutamate = D-glutamate
two base mechanism, removal of alpha-hydrogen is the rate determining step
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L-glutamate = D-glutamate
the enzyme uses a two-base mechanism in which two Cys thiolates serve as the general base/acid catalysts. An initial deprotonation event produces a resonance-stabilized carbanionic intermediate that is subsequently protonated on the opposite face to generate the enantiomeric product
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L-glutamate = D-glutamate
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
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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
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L-glutamate = D-glutamate
molecular dynamics simulations, mechanism by which binding mismatches are propagated into an opening of the active site
L-glutamate = D-glutamate
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
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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L-glutamate = D-glutamate
MurI is a member of the two-base mechanism (dual-cysteine) racemase family, where two essential active-site cysteine residues act as catalytic base and acid to stereospecifically de- and reprotonate, respectively, the alpha position of glutamate in order to enact substrate racemization
L-glutamate = D-glutamate
MurI is a member of the two-base mechanism (dual-cysteine) racemase family, where two essential active-site cysteine residues act as catalytic base and acid to stereospecifically de- and reprotonate, respectively, the alpha position of glutamate in order to enact substrate racemization. C185 of BsMurI corresponds to the essential catalytic cysteine residue that deprotonates an incoming L-glutamate substrate (or reprotonates a carbanionic intermediate to form the D-stereoconfiguration)
L-glutamate = D-glutamate
MurI is a member of the two-base mechanism (dual-cysteine) racemase family, where two essential active-site cysteine residues act as catalytic base and acid to stereospecifically de- and reprotonate, respectively, the alpha position of glutamate in order to enact substrate racemization. C185 of BsMurI corresponds to the essential catalytic cysteine residue that deprotonates an incoming L-glutamate substrate (or reprotonates a carbanionic intermediate to form the D-stereoconfiguration)
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L-glutamate = D-glutamate
MurI is a member of the two-base mechanism (dual-cysteine) racemase family, where two essential active-site cysteine residues act as catalytic base and acid to stereospecifically de- and reprotonate, respectively, the alpha position of glutamate in order to enact substrate racemization
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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