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Information on EC 3.4.11.26 - intermediate cleaving peptidase 55 and Organism(s) Saccharomyces cerevisiae and UniProt Accession P40051

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.26 intermediate cleaving peptidase 55
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Saccharomyces cerevisiae
UNIPROT: P40051 not found.
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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The enzyme cleaves the Pro36-Pro37 bond of cysteine desulfurase (EC 2.8.1.7) removing three amino acid residues (Tyr-Ser-Pro) from the N-terminus after cleavage by mitochondrial processing peptidase.
Synonyms
At1g09300, Icp55, YER078c, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Met-Pro-Ala + H2O
Met + Pro-Ala
show the reaction diagram
-
-
-
?
Tyr-Ala-Ala + H2O
Tyr + Ala-Ala
show the reaction diagram
-
-
-
?
Tyr-Pro-Ala + H2O
Tyr + Pro-Ala
show the reaction diagram
-
-
-
?
Tyr-Ser-Ala + H2O
Tyr + Ser-Ala
show the reaction diagram
-
-
-
?
Tyr-Ser-Pro-Nfs1 + H2O
Nfs1 + Tyr-Ser-Pro
show the reaction diagram
Tyr-Thr-Ala + H2O
Tyr + Thr-Ala
show the reaction diagram
-
-
-
?
Isa2 + H2O
?
show the reaction diagram
-
-
substrate is likely processed by isoform Icp55 in two consecutive steps, in which Icp55 removes two destabilizing amino acids: first Phe and then in a second round of processing Tyr, resulting in the mature stable protein
-
?
additional information
?
-
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
Tyr-Ser-Pro-Nfs1 + H2O
Nfs1 + Tyr-Ser-Pro
show the reaction diagram
the enzyme is involved in the processing pathway of yeast Nfs1 during its translocation into the mitochondrial matrix. Nfs1 from Saccharomyces cerevisiae undergoes two steps of proteolytic processing: first the mitochondrial processing peptidase (MPP) cleaves the precursor between Phe33 and Tyr34. Then Icp55 cleaves between Pro36 and Pro37 removing three amino acids residues (Tyr-Ser-Pro)
-
-
?
additional information
?
-
Icp55 is critical for stabilization of the mitochondrial proteome. Icp55 removes an amino acid from a characteristic set of N-termini of preprotein intermediates generated by mitochondrial processing peptidase. Thereby Icp55 converts instable intermediates into stable proteins
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
not activating: Mg2+, Ca2+, Co2+, Ni2+, Zn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
apstatin
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
Met-Pro-Ala
pH 7.5, 40°C
0.72
Tyr-Ala-Ala
pH 7.5, 40°C
1.8
Tyr-Pro-Ala
pH 7.5, 40°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
25.7
Met-Pro-Ala
pH 7.5, 40°C
1.4
Tyr-Ala-Ala
pH 7.5, 40°C
14
Tyr-Pro-Ala
pH 7.5, 40°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12.8
Met-Pro-Ala
pH 7.5, 40°C
1.94
Tyr-Ala-Ala
pH 7.5, 40°C
7.78
Tyr-Pro-Ala
pH 7.5, 40°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5
Tyr-Ala-Ala
pH 7.5, 40°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
Icp55 is critical for stabilization of the mitochondrial proteome. The cleavage by Icp55 stabilizes the substrate proteins by removing destabilizing amino acids
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
106000
53000
and 106000, gel filtration, truncated variant lacking 42 N-terminal amino acids
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 52000, gel filtration, the enzyme exists in a rapid equilibrium between monomer and dimer. The dimer, not monomer, is the active species of the enzyme with loop dynamics at the dimer interface playing an important role in activity. Dynamics of Icp55 protein between two conformations of dimer are found to be important for activity of the enzyme
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
free enzyme and in complex with inhibitor apstatin. The enzyme exists in a rapid equilibrium between monomer and dimer. The dimer, and not the monomer, is the active species with loop dynamics at the dimer interface playing an important role in activity
oil microbatch method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y284D
mutation of a conserved Tyr284 residue located at hinge helix that interacts with its counterpart across the dimer interface. Mutant is a monomer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21(DE3). Full-length Icp55 construct can not be expressed in the soluble fraction. Two truncated versions, Icp55t1 with 42 amino acid N-terminal truncation and Icp55t2 with 57 amino acid N-terminal truncation, are successfully expressed in soluble forms. All activity assays for Icp55 are reported for Icp55t1 construct
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
identification of 36 substrates utilizing charge-based fractional diagonal chromatography, enabling the differential quantitation of 1459 nonredundant N-terminal peptides between two Saccharomyces cerevisiae samples within 10 h of LC-MS, starting from only 50 microg of protein per condition and analyzing only 40% of the obtained fractions
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Voegtle, F.N.; Wortelkamp, S.; Zahedi, R.P.; Becker, D.; Leidhold, C.; Gevaert, K.; Kellermann, J.; Voos, W.; Sickmann, A.; Pfanner, N.; Meisinger, C.
Global analysis of the mitochondrial N-proteome identifies a processing peptidase critical for protein stability
Cell
139
428-439
2009
Saccharomyces cerevisiae (P40051)
Manually annotated by BRENDA team
Naamati, A.; Regev-Rudzki, N.; Galperin, S.; Lill, R.; Pines, O.
Dual targeting of Nfs1 and discovery of its novel processing enzyme, Icp55
J. BIOL. CHEM.
284
30200-30208
2009
Saccharomyces cerevisiae (P40051)
Manually annotated by BRENDA team
Venne, A.S.; Voegtle, F.N.; Meisinger, C.; Sickmann, A.; Zahedi, R.P.
Novel highly sensitive, specific, and straightforward strategy for comprehensive N-terminal proteomics reveals unknown substrates of the mitochondrial peptidase Icp55
J. Proteome Res.
12
3823-3830
2013
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Singh, R.; Goyal, V.D.; Kumar, A.; Sabharwal, N.S.; Makde, R.D.
Crystal structures and biochemical analyses of intermediate cleavage peptidase role of dynamics in enzymatic function
FEBS Lett.
593
443-454
2019
Saccharomyces cerevisiae (P40051), Saccharomyces cerevisiae ATCC 204508 (P40051)
Manually annotated by BRENDA team