220.127.116.11 - Glutamate synthase (ferredoxin)
- Ferredoxin-dependent glutamate synthase.
2 L-glutamate + 2 oxidized [2Fe-2S]-[ferredoxin] = 2-oxoglutarate + 2 H(+) + L-glutamine + 2 reduced [2Fe-2S]-[ferredoxin]
FAD; FMN; Iron-sulfur.
- The hydrolysis of glutamine to glutamate and ammonia. This reaction occurs in the N-terminal amidotransferase domain (CATH code 18.104.22.168, residues 1-422) and proceeds via the classical cysteine covalent intermediate.
- The second half reaction occur in the FMN-binding domain (CATH code 22.214.171.124, residues 787-1223). In this reaction the ammonia initiates a nucleophilic attack on the C2 carbonyl carbon of the 2-oxoglutarate substrate. The FMN cofactor then donates a hydride ion to the intermediate and Ferredoxin regenerates the FMN cofactor.
|AA||Uniprot||Uniprot Resid||PDB||PDB Resid|
overall product formed, proton transfer, enzyme-substrate complex formation, native state of cofactor regenerated, intermediate formation, dehydration, schiff base formed, cofactor used, electron relay, enzyme-substrate complex cleavage, radical termination, redox reaction, intermediate terminated, native state of enzyme regenerated, aromatic unimolecular elimination by the conjugate base, electron transfer, intermediate collapse, hydride transfer, radical formation, overall reactant used, inferred reaction step, proton relay, unimolecular elimination by the conjugate base, bimolecular nucleophilic addition, deamination
There are no kinetic parameters information for this Enzyme
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