Information on EC 3.4.23.51 - HycI peptidase

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
3.4.23.51
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RECOMMENDED NAME
GeneOntology No.
HycI peptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
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.
show the reaction diagram
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-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
precursor of the large subunit of hydrogenase 3 + H2O
?
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
precursor of the large subunit of hydrogenase 3 + H2O
?
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
3.7
calculated from amino acid sequence
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisTrap HP5 column chromatography, HiPrep column chromatography, and Superdex 200 gel filtration
purified endopeptidases HycI is devoid of metal
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D16N
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no processing activity
D62M
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no processing activity
D62N
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no processing activity
H90Q
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some minor processing activity