3.4.11.26: intermediate cleaving peptidase 55

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For detailed information about intermediate cleaving peptidase 55, go to the full flat file.

Reaction

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

ECTree

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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Results	in table
10	AA Sequence
1	Application
3	Cloned(Commentary)
2	Crystallization (Commentary)
4	General Information
3	Inhibitors
3	kcat/KM [mM/s]
1	Ki Value [mM]
3	KM Value [mM]
7	Localization
3	Metals/Ions
4	Molecular Weight [Da]
2	Natural Substrates/ Products (Substrates)
7	Organism
3	PDB ID
1	pH Optimum
2	Protein Variants
1	Purification (Commentary)
1	Reaction
7	Reference
18	Substrates and Products (Substrate)
6	Subunits
8	Synonyms
1	Temperature Optimum [°C]
3	Turnover Number [1/s]

Application

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Application on EC 3.4.11.26 - intermediate cleaving peptidase 55

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analysis

Saccharomyces cerevisiae

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

732385