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Information on EC 3.4.23.51 - HycI peptidase and Organism(s) Escherichia coli and UniProt Accession P0AEV9

for references in articles please use BRENDA:EC3.4.23.51
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.51 HycI peptidase
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This record set is specific for:
Escherichia coli
UNIPROT: P0AEV9 not found.
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
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
hyci endopeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
HycE processing protein
-
PATHWAY SOURCE
PATHWAYS
-
-
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 SUBSTRATE
NATURAL 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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
conserved amino-acid residues involved in cadmium ligation in the crystal are essential for the endoproteolytic activity in HycI
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
not inhibited by phenylmethylsulfonyl fluoride, benzamidine or EDTA
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 17000
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D16N
no processing activity
D62M
no processing activity
D62N
no processing activity
H90Q
some minor processing activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified endopeptidases HycI is devoid of metal
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Theodoratou, E.; Paschos, A.; Mintz-Weber, S.; Bock, A.
Analysis of the cleavage site specificity of the endopeptidase involved in the maturation of the large subunit of hydrogenase 3 from Escherichia coli
Arch. Microbiol.
173
110-116
2000
Escherichia coli (P0AEV9)
Manually annotated by BRENDA team
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
Eur. J. Biochem.
267
1995-1999
2000
Escherichia coli (P0AEV9)
Manually annotated by BRENDA team
Yang, F.; Hu, W.; Xu, H.; Li, C.; Xia, B.; Jin, C.
Solution structure and backbone dynamics of an endopeptidase HycI from Escherichia coli: implications for mechanism of the [NiFe] hydrogenase maturation
J. Biol. Chem.
282
3856-3863
2007
Escherichia coli (P0AEV9)
Manually annotated by BRENDA team
Theodoratou, E.; Huber, R.; Bck A.
[NiFe]-Hydrogenase maturation endopeptidase: structure and function
Biochem. Soc. Trans.
33
108-111
2005
Escherichia coli (P0AEV9)
Manually annotated by BRENDA team
Maier, T.; Bck, A.
Generation of active [NiFe] hydrogenase in vitro from a nickel-free precursor form
Biochemistry
35
10089-10093
1996
Escherichia coli (P0AEV9)
Manually annotated by BRENDA team
Rossmann, R.M.; Sauter, M.; Lottspeich, F.; Bck, A.
Maturation of the large subunit (HYCE) of Escherichia coli hydrogenase 3 requires nickel incorporation followed by C-terminal processing at Arg537
Eur. J. Biochem.
220
377-384
1994
Escherichia coli (P0AEV9)
Manually annotated by BRENDA team
Rossmann, R.; Maier, T.; Lottspeich, F.; Boeck, A.
Characterization of a protease from Escherichia coli involved in hydrogenase maturation
Eur. J. Biochem.
227
545-550
1995
Escherichia coli (P0AEV9)
Manually annotated by BRENDA team