Cloned (Comment) | Organism |
---|---|
- |
Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
solution structure of Escherichia coli HycI determined by high resolution nuclear magnetic resonance spectroscopy. The overall structure is similar to the crystal structure of holo-HybD in the same family. HycI shows an open conformation at the putative nickel-binding site, whereas HybD adopts a closed conformation | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ni2+ | HycI shows an open conformation at the putative nickel-binding site. Ni2+ has lower binding affinity with HycI than that of Cd2+, which is likely required for HycI to dissociate from HycE after the C-terminal processing | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
precursor of the large subunit of hydrogenase 3 + H2O | Escherichia coli | HycI is an endopeptidase that is responsible for the C-terminal cleavage of the large subunit of hydrogenase 3 in Escherichia coli (UniProt: A1AER2) | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0AEV9 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
precursor of the large subunit of hydrogenase 3 + H2O | HycI is an endopeptidase that is responsible for the C-terminal cleavage of the large subunit of hydrogenase 3 in Escherichia coli (UniProt: A1AER2) | Escherichia coli | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
HYCI | - |
Escherichia coli |