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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Subunits
Subunits on EC 5.1.1.3 - glutamate racemase
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dimer
homodimer
monomer
additional information
dimer
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both enzymes RacE1 and Rac2 are dimers with monomers arranged in a tail-to-tail orientation which is determined by gel filtration
dimer
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determined by gel filtration, RacE2 exist as a dimer in solution, but the monomeric enzyme is more active than the dimeric form
dimer
determined by blue native PAGE, FnGR is a pseudosymmetric enzyme, the presence of glutamate does not significantly alter the position of the monomer-dimer equilibrium of the enzyme
dimer
crystal structure analysis, GluR is composed of two domains of alpha/beta protein that are related by pseudo-2fold symmetry and the active site is located at the domain interface
homodimer
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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
homodimer
2 * 28900, about, sequence calcuation and analytical ultracentrifugation
homodimer
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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2 * 28900, about, sequence calcuation and analytical ultracentrifugation
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homodimer
2 * 29500, about, sequence calcuation and analytical ultracentrifugation
homodimer
Mycolicibacterium smegmatis ATCC 700084 / mc(2)155
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2 * 29500, about, sequence calcuation and analytical ultracentrifugation
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monomer
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mutants R25A and K106A/R214A are completely monomeric at the concentration of 5 mg/ml
monomer
determined by gel filtration, BsGR is a monomeric enzyme, which dimerizes in the presence of either 10 mM D- or L-glutamate
Q81LA8
although RacE1 and RacE2 share significant sequence similarity, these proteins have different quaternary structural properties
additional information
Q81UL8
although RacE1 and RacE2 share significant sequence similarity, these proteins have different quaternary structural properties
additional information
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although RacE1 and RacE2 share significant sequence similarity, these proteins have different quaternary structural properties
additional information
Q81LA8
by gel filtration it is shown that in solution RacE2 may be polydisperse, existing as both monomers and higher-order complexes
additional information
Q81UL8
by gel filtration it is shown that in solution RacE2 may be polydisperse, existing as both monomers and higher-order complexes
additional information
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by gel filtration it is shown that in solution RacE2 may be polydisperse, existing as both monomers and higher-order complexes
additional information
the active site is located in a surface-exposed cleft that is formed at the interface of domains 1 and 2, subunit interaction analysis
additional information
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the active site is located in a surface-exposed cleft that is formed at the interface of domains 1 and 2, subunit interaction analysis
additional information
Mycobacterium tuberculosis ATCC 25618 / H37Rv
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the active site is located in a surface-exposed cleft that is formed at the interface of domains 1 and 2, subunit interaction analysis
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additional information
the active site is located in a surface-exposed cleft that is formed at the interface of domains 1 and 2, subunit interaction analysis
additional information
-
the active site is located in a surface-exposed cleft that is formed at the interface of domains 1 and 2, subunit interaction analysis
additional information
Mycolicibacterium smegmatis ATCC 700084 / mc(2)155
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the active site is located in a surface-exposed cleft that is formed at the interface of domains 1 and 2, subunit interaction analysis
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