HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 3.4.11.26 - intermediate cleaving peptidase 55
for references in articles please use BRENDA:EC3.4.11.26Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Saccharomyces cerevisiae
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
3.4.11.26
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
intermediate cleaving peptidase 55
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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.
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
malfunction
-
icp55DELTA cells are defective in growth on nonfermentable medium at elevated temperature (37�C)
malfunction
-
Nfs1 purified from the knockout strain, DELTAip55, detected three additional amino acids (Tyr-Ser-Pro), at the N-terminus of Nfs1
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Isa2 + H2O
?
-
-
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
-
?
Tyr-Ser-Pro-Nfs1 + H2O
Nfs1 + Tyr-Ser-Pro
-
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)
-
-
?
Tyr-Ser-Pro-Nfs1 + H2O
Nfs1 + Tyr-Ser-Pro
-
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). In the absence of Nfs1 processing by mitochondrial processing peptidase (MPP), the Nfs1 precursor is not cleaved by Icp55. The two prolines are of importance for the Icp55 cleavage reaction, because the replacement of a single proline changes the specificity to a new cleavage site without eliminating the cleavage reaction per se
-
-
?
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
-
-
-
additional information
?
-
global analysis of the N-proteome of yeast mitochondria, revealing the N-termini of 615 different proteins. The N-proteome of icp55DELTA mitochondria yielded proteins whose N-terminus differs by one residue from the mature N-terminus of wild-type mitochondria. Icp55 cleaves between the last amino acid of the presequence (tyrosine, leucine or phenylalanine) and the first residue of the mature protein, preferentially serine, alanine and threonine. The most frequent residue tyrosine is efficiently removed by Icp55 and thus is the best substrate of Icp55. The efficiency of cleavage is lower for leucine and phenylalanine
-
-
-
additional information
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Tyr-Ser-Pro-Nfs1 + H2O
Nfs1 + Tyr-Ser-Pro
-
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
?
-
P40051
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
Icp55 behaves like a protein that is peripherally attached to the mitochondrial inner membrane from the matrix side
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 3.4.11.26)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
