3.4.23.51: HycI peptidase
This is an abbreviated version!
For detailed information about HycI peptidase, go to the full flat file.
Reaction
This enzyme specifically removes a 32-amino acid peptide from the C-terminus of the precursor of the large subunit of hydrogenase 3 in Escherichia coli by cleavage at the C-terminal side of Arg537. =
Synonyms
HycE processing protein, HYCI, HycI endopeptidase
ECTree
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Metals Ions
Metals Ions on EC 3.4.23.51 - HycI peptidase
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Cd2+
conserved amino-acid residues involved in cadmium ligation in the crystal are essential for the endoproteolytic activity in HycI
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
Ni2+
the reaction requires nickel to be bound to the precursor and the protease does not have a function in nickel delivery to the substrate. Radioactive labelling of cells with 63Ni, devoid of endopeptidase, resolves several forms of the precursor which are possibly intermediates in the maturation pathway. The endopeptidase uses the metal in the large subunit of [NiFe]-hydrogenases as a recognition motif