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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Substrates Products on EC 3.4.23.51 - HycI peptidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
precursor of the large subunit of hydrogenase 3 + H2O
?
i.e. HycE
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-
?
precursor of the large subunit of hydrogenase 3 + H2O
?
HycI involved in the C-terminal processing of HycE, the large subunit of the hydrogenase 3 from Escherichia coli
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?
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)
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-
?
precursor of the large subunit of hydrogenase 3 + H2O
?
the final step of maturation of [NiFe]-hydrogenases involves the activity of an endopeptidase which removes an oligopeptide from the C-terminus of the large subunit. The proteolytic maturation is followed by a conformational change, closing of the metal centre, its assembly with the small hydrogenase subunit and finally in the appearance of enzyme activity. HycI is specific for hydrogenase 3 maturation
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-
?
precursor of the large subunit of hydrogenase 3 + H2O
?
cleavage occurs at the C-terminal side of the Arg537 (removal of a 32-amino acid peptide from the C-terminus). Nickel incorporation into the HYCE precursor is a prerequisite for processing
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?
precursor of the large subunit of hydrogenase 3 + H2O
?
HycI involved in the C-terminal processing of HycE (UniProt: A1AER2), the large subunit of the hydrogenase 3 from Escherichia coli. Mutational alteration of the amino acid residues neighbouring the cleavage site shows that proteolysis still occurs when chemically similar amino acids are exchanged. Processing is blocked in a variant in which the methionine at the C-terminal side is replaced by a glutamate residue. Truncation of the precursor from the C-terminal end renders variants amenable to maturation even when two-thirds of the extension are removed but abolishes proteolysis upon further deletion of a cluster of six basic amino acids. A construct in which the C-terminal extension from the large subunit of the hydrogenase 2 is fused to the mature part of the large subunit of hydrogenase 3 is neither processed by HycI nor by HybD, the endopeptidase specific for the large subunit of hydrogenase 2
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-
?
precursor of the large subunit of hydrogenase 3 + H2O
?
HycI is specific for hydrogenase 3 maturation
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-
?
precursor of the large subunit of hydrogenase 3 + H2O
?
i.e. HycE (UniProt: A1AER2). Cleavage of HycE is specific in that the maturation of the large subunits of hydrogenases 1 and 2 is not affected in strains lacking hycl
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-
?
precursor of the large subunit of hydrogenase 3 + H2O
?
i.e. hycE. Once the metallocenter [NiMeL] is formed in the HycE precursor, processing by HycI and assembly with the other Hyc subunits takes place
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?
precursor of the large subunit of hydrogenase 3 + H2O
?
the HycI endopeptidase is involved in the C-terminal processing of the large subunit of hydrogenase 3 (HycE)
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?
