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EC 3.4.14.12 Details
EC number
3.4.14.12
Accepted name
Xaa-Xaa-Pro tripeptidyl-peptidase
Reaction
Hydrolysis of Xaa-Xaa-Pro┼Yaa- releasing the N-terminal tripeptide of a peptide with Pro as the third residue (position P1) and where Yaa is not proline
Other name(s)
prolyltripeptidyl amino peptidase, prolyl tripeptidyl peptidase, prolyltripeptidyl aminopeptidase, PTP-A, TPP
Comment
This cell-surface-associated serine exopeptidase is found in the Gram-negative, anaerobic bacterium Porphyromonas gingivalis, which has been implicated in adult periodontal disease [1]. The enzyme releases the N-terminal tripeptide of peptides, such as interleukin-6. It has an absolute requirement for a proline residue at the P1 position but is completely inactivated by a proline residue at the P1′ position [1]. The size of the peptide does not affect the rate of reaction [1].
History
created 2006
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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
3.4.14.1 dipeptidyl-peptidase I
3.4.14.2 dipeptidyl-peptidase II
3.4.14.3 created 1978, deleted 1981
3.4.14.4 dipeptidyl-peptidase III
3.4.14.5 dipeptidyl-peptidase IV
3.4.14.6 dipeptidyl-dipeptidase
3.4.14.7 created 1989, deleted 1992
3.4.14.8 created 1989, deleted 1992
3.4.14.9 tripeptidyl-peptidase I
3.4.14.10 tripeptidyl-peptidase II
3.4.14.11 Xaa-Pro dipeptidyl-peptidase
3.4.14.12 Xaa-Xaa-Pro tripeptidyl-peptidase
3.4.14.13 γ-D-glutamyl-L-lysine dipeptidyl-peptidase
3.4.14.14 [mycofactocin precursor peptide] peptidase
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
3.6 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