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EC 3.4.11.26 Details

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EC number

3.4.11.26

Accepted name

intermediate cleaving peptidase 55

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.

Other name(s)

Icp55, mitochondrial intermediate cleaving peptidase 55 kDa

Comment

Icp55 removes the destabilizing N-terminal amino acid residues that are left after cleavage by the mitochondrial processing peptidase, leading to the stabilisation of the substrate. The enzyme can remove single amino acids or a short peptide, as in the case of cysteine desulfurase (EC 2.8.1.7), where three amino acids are removed.

History

created 2011

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.3.1 With NAD⁺ or NADP⁺ as acceptor

1.3.2 With a cytochrome as acceptor

1.3.3 With oxygen as acceptor

1.3.4 With a disulfide as acceptor

1.3.5 With a quinone or related compound as acceptor

1.3.7 With an iron-sulfur protein as acceptor

1.3.8 With a flavin as acceptor

1.3.98 With other, known, physiological acceptors

1.3.99 With unknown physiological acceptors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.15 Acting on superoxide as acceptor

1.15.1 Acting on superoxide as acceptor (only sub-subclass identified to date)

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.21.1 With NAD⁺ or NADP⁺ as acceptor

1.21.3 With oxygen as acceptor

1.21.4 With a disulfide as acceptor

1.21.98 With other, known, physiological acceptors

1.21.99 With unknown physiological acceptors

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.97.1 Sole sub-subclass for oxidoreductases that do not belong in the other subclasses

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

2.1 Transferring one-carbon groups

2.2 Transferring aldehyde or ketonic groups

2.3 Acyltransferases

2.4 Glycosyltransferases

2.5 Transferring alkyl or aryl groups, other than methyl groups

2.6 Transferring nitrogenous groups

2.7 Transferring phosphorus-containing groups

2.8 Transferring sulfur-containing groups

2.9 Transferring selenium-containing groups

2.10 Transferring molybdenum- or tungsten-containing groups

3.1 Acting on ester bonds

3.2 Glycosylases

3.3 Acting on ether bonds

3.4 Acting on peptide bonds (peptidases)

3.4.1 α-Amino-acyl-peptide hydrolases (deleted sub-subclass)

3.4.2 Peptidyl-amino-acid hydrolases (deleted sub-subclass)

3.4.3 Dipeptide hydrolases (deleted sub-subclass)

3.4.4 Peptidyl peptide hydrolases (deleted sub-subclass)

3.4.11 Aminopeptidases

3.4.11.1 leucyl aminopeptidase

3.4.11.2 membrane alanyl aminopeptidase

3.4.11.3 cystinyl aminopeptidase

3.4.11.4 tripeptide aminopeptidase

3.4.11.5 prolyl aminopeptidase

3.4.11.6 aminopeptidase B

3.4.11.7 glutamyl aminopeptidase

3.4.11.8 created 1972, deleted 1981

3.4.11.9 Xaa-Pro aminopeptidase

3.4.11.10 bacterial leucyl aminopeptidase

3.4.11.11 created 1978, deleted 1992

3.4.11.12 created 1978, deleted 1997

3.4.11.13 clostridial aminopeptidase

3.4.11.14 cytosol alanyl aminopeptidase

3.4.11.15 aminopeptidase Y

3.4.11.16 Xaa-Trp aminopeptidase

3.4.11.17 tryptophanyl aminopeptidase

3.4.11.18 methionyl aminopeptidase

3.4.11.19 D-stereospecific aminopeptidase

3.4.11.20 aminopeptidase Ey

3.4.11.21 aspartyl aminopeptidase

3.4.11.22 aminopeptidase I

3.4.11.23 PepB aminopeptidase

3.4.11.24 aminopeptidase S

3.4.11.25 β-peptidyl aminopeptidase

3.4.11.26 intermediate cleaving peptidase 55

3.4.12 Peptidylamino-acid hydrolases or acylamino-acid hydrolases (deleted sub-subclass)

3.4.13 Dipeptidases

3.4.14 Dipeptidyl-peptidases and tripeptidyl-peptidases

3.4.15 Peptidyl-dipeptidases

3.4.16 Serine-type carboxypeptidases

3.4.17 Metallocarboxypeptidases

3.4.18 Cysteine-type carboxypeptidases

3.4.19 Omega peptidases

3.4.21 Serine endopeptidases

3.4.22 Cysteine endopeptidases

3.4.23 Aspartic endopeptidases

3.4.24 Metalloendopeptidases

3.4.25 Threonine endopeptidases

3.4.99 Endopeptidases of unknown catalytic mechanism (sub-subclass is currently empty)

3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

3.5.1 In linear amides

3.5.2 In cyclic amides

3.5.3 In linear amidines

3.5.4 In cyclic amidines

3.5.5 In nitriles

3.5.99 In other compounds

3.6 Acting on acid anhydrides

3.7 Acting on carbon-carbon bonds

3.8 Acting on halide bonds

3.9 Acting on phosphorus-nitrogen bonds

3.10 Acting on sulfur-nitrogen bonds

3.11 Acting on carbon-phosphorus bonds

3.12 Acting on sulfur-sulfur bonds

3.13 Acting on carbon-sulfur bonds

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Release 2023.1 (January 2023)