Cloned (Comment) | Organism |
---|---|
gene gadB, recombinant expression of holoenzyme | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate | Escherichia coli | - |
4-aminobutanoate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P69910 | - |
- |
Purification (Comment) | Organism |
---|---|
purification of recombinant holoenzyme, preparation of apoenzyme, and reconstitution with pyridoxal 5'-phosphate, overview | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate | - |
Escherichia coli | 4-aminobutanoate + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | at alkaline pH | Escherichia coli |
hexamer | - |
Escherichia coli |
More | in GadB, the dimer is the functional unit as each active site is made of amino acid residues that are provided by both monomers in the dimer. Structural organization of EcGadB in solution in the pH range 7.5-8.6, overview. Analysis by small angle X-ray scattering combined with size exclusion chromatography and analytical ultracentrifugation analysis shows that the compact and entangled EcGadB hexameric structure undergoes dissociation into dimers as pH alkalinizes. When pyridoxal 5'-phosphate is not present, the dimeric species is the most abundant in solution, though evidence for the occurrence of a likely tetrameric species is also obtained. Molecular modeling | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
GadB | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyridoxal 5'-phosphate | PLP, plays a key role in the acquisition of a folding necessary for the canonical catalytic activity. Preparation of recombinant apoenzyme, and reconstitution with pyridoxal 5'-phosphate, overview | Escherichia coli |