Literature summary for 3.4.23.51 extracted from

Theodoratou, E.; Paschos, A.; Magalon, A.; Fritsche, E.; Huber, R.; Bock, A.
Nickel serves as a substrate recognition motif for the endopeptidase involved in hydrogenase maturation (2000), Eur. J. Biochem., 267, 1995-1999.

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Protein Variants

Protein Variants	Comment	Organism
D16N	no processing activity	Escherichia coli
D62M	no processing activity	Escherichia coli
D62N	no processing activity	Escherichia coli
H90Q	some minor processing activity	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cd2+	conserved amino-acid residues involved in cadmium ligation in the crystal are essential for the endoproteolytic activity in HycI	Escherichia coli
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	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AEV9	-	-

Purification (Commentary)

Purification (Comment)	Organism
purified endopeptidases HycI is devoid of metal	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
precursor of the large subunit of hydrogenase 3 + H2O	HycI is specific for hydrogenase 3 maturation	Escherichia coli	?	-	?

Synonyms

Synonyms	Comment	Organism
HYCI	-	Escherichia coli

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Release 2023.1 (January 2023)