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4.1.1.15: glutamate decarboxylase

This is an abbreviated version!
For detailed information about glutamate decarboxylase, go to the full flat file.

Word Map on EC 4.1.1.15

Reaction

L-glutamate
=
4-aminobutanoate
 +
CO2

Synonyms

42 kDa biotin-coupled protein, 65 kDa glutamic acid decarboxylase, 67 kDa glutamic acid decarboxylase, Aspartate 1-decarboxylase, Aspartic alpha-decarboxylase, AtGAD1, BmGAD, BmGadB, BMI_II334, Cysteic acid decarboxylase, Decarboxylase, glutamate, ERT D1, GAD, GAD B, GAD-65, GAD-67, GAD-alpha, GAD-beta, GAD-gamma, GAD1, GAD2, GAD3, Gad56, GAD65, GAD67, GadA, GadB, GADB1, gadB2, GADbeta, GADCase, gadlbhye1, gamma-Glutamate decarboxylase, GDC, GDCase, Glt decarboxylase, glutamate decarboxylase, glutamate decarboxylase 1, glutamate decarboxylase 65, glutamate decarboxylase 67, glutamate decarboxylase A, glutamate decarboxylase B, Glutamic acid decarboxylase, glutamic acid decarboxylase 65, glutamic acid decarboxylase 67, glutamic acid decarboxylase-65, glutamic acid decarboxylase-67, glutamic acid decarboxylase67, Glutamic decarboxylase, hGAD65, hGAD67, L-Aspartate-alpha-decarboxylase, L-glutamate 1-carboxylyase, L-Glutamate alpha-decarboxylase, L-Glutamate decarboxylase, L-glutamate decarboxylase 65, L-glutamate decarboxylase 67, L-Glutamic acid decarboxylase, L-Glutamic decarboxylase, LbGAD, LbGadB, MGAD, More, p42, PF1159, PfGAD, ScGAD, sll1641

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.15 glutamate decarboxylase

Crystallization

Crystallization on EC 4.1.1.15 - glutamate decarboxylase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, X-ray diffraction structure determination and analysis
sitting drop vapor diffusion method, using 100 mM sodium acetate pH 5.5, 720 mM sodium formate, 9% (w/v) PEG 8000, and 9% (w/v) PEG 1000
enzyme hexamer X-ray diffraction structure determination and analysis at pH 4.6 and pH 7.6
-
isoform GadB, native and reduced, vapour diffusion method
-
isozyme GADalpha in complex with L-glutarate
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N-terminally truncated mutants of both isoform GAD65 and GAD67. GAD67 shows a thethered loop covering the active site, providing a catalytic environment that sustains 4-aminobutanoate production. In isoform GAD65, the same catalytic loop is inherently mobile promoting a side reaction that results in cofactor release and enzyme autoinactivation
-
UV/Vis spectra show a strong peak for holo-enzyme at 308 nm and a weak peak at 336 nm. Apo-enzyme has a 20% increase in fluorescence emission at 308 nm. Holo-enzyme shows a greater beta-sheet content than apo-enzyme, but both have a similar alpha-helix content
-