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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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
UNIPROT
ORGANISM
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
Show AA Sequence (155 entries)
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