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Information on EC 3.4.23.51 - HycI peptidase
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The expected taxonomic range for this enzyme is: Escherichia coli
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EC NUMBER 
COMMENTARY 
3.4.23.51
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RECOMMENDED NAME
GeneOntology No.
HycI peptidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
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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
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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
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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
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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
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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
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HycI is specific for hydrogenase 3 maturation
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precursor of the large subunit of hydrogenase 3 + H2O
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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
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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
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the HycI endopeptidase is involved in the C-terminal processing of the large subunit of hydrogenase 3 (HycE)
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
?
P0AEV9
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
?
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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
?
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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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
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conserved amino-acid residues involved in cadmium ligation in the crystal are essential for the endoproteolytic activity in HycI
Ni2+
Ni2+
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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
Ni2+
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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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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not inhibited by phenylmethylsulfonyl fluoride, benzamidine or EDTA
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12);
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
1 * 17000, HycI exists as a monomer in solution, X-ray crystallography
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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sitting drop vapor diffusion method, using 28% (w/v) polyethylene glycol 400, 0.2 M CaCl2, and 0.1 M Na-HEPES (pH 7.5), at 20°C
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisTrap HP5 column chromatography, HiPrep column chromatography, and Superdex 200 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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