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EC 3.4.11.24 Details
EC number
3.4.11.24
Accepted name
aminopeptidase S
Reaction
Release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
Other name(s)
Mername-AA022 peptidase, SGAP, aminopeptidase (Streptomyces griseus), Streptomyces griseus aminopeptidase, S. griseus AP, double-zinc aminopeptidase
Comment
Aminopeptidases are associated with many biological functions, including protein maturation, protein degradation, cell-cycle control and hormone-level regulation [3,4]. This enzyme contains two zinc molecules in its active site and is activated by Ca2+ [4]. In the presence of Ca2+, the best substrates are Leu-Phe, Leu-Ser, Leu-pNA (aminoacyl-p-nitroanilide), Phe-Phe-Phe and Phe-Phe [3]. Peptides with proline in the P1′ position are not substrates [3]. Belongs in peptidase family M28.
History
created 2008
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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 Transferases
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 Hydrolases
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
4 Lyases
5 Isomerases
6 Ligases
7 Translocases