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Information on EC 3.4.19.1 - acylaminoacyl-peptidase
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3.4.19.1 acylaminoacyl-peptidaseSpecify your search results
Word Map
- 3.4.19.1
- marrow
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immunocytochemical
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oligopeptidase
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anti-alkaline
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prolyl
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immunophenotyping
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hla-dr
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smear
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cryosta
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phosphatase-anti-alkaline
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cytospins
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immunoenzymatic
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moabs
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aeropyrum
- pernix
- fluorophosphate
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immunoenzyme
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immunoalkaline
- medicine
- acylase
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cytocentrifuge
- analysis
- drug development
- synthesis
- degradation
The enzyme appears in viruses and cellular organisms
Reaction Schemes
cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
Synonyms
apaap, acylpeptide hydrolase, acylaminoacyl peptidase, acylamino acid-releasing enzyme, acyl-peptide hydrolase, spaap, aphdr, acyl peptide hydrolase, apaph, aare/oph, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAP
AARE
Acyl-peptide hydrolase
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acyl-peptide releasing enzyme
acylamino acid-releasing enzyme
acylamino-acid-releasing enzyme
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acylaminoacyl peptidase
Acylaminoacyl-peptidase
acylpeptide hydrolase
alpha-N-acylpeptide hydrolase
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ApAAP
APEH
apeH-2
APEH-3
APEH-3Ss
APE_1547.1
APH
DNF15S2 protein
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N-acylaminoacyl-peptide hydrolase
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N-acylpeptide hydrolase
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N-formylmethionine (fMet) aminopeptidase
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PhAAP
PM hydrolase
PMH
SpAAP
sso2141
SSO2693
ST0779
yuxL
Acylaminoacyl-peptidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
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cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
substrate binding and catalytic mechanisms, overview. Three main pathways are observed most frequently, namely P1, P2A, and P3, evaluation by comparing the average force profiles and potential of mean force calculations revealing that P3 is the unbinding pathway. P1 is located in a tunnel in the beta-propeller domain and contained the D158, R160, S157, S201, A200, S199, W250, D69, Q28, and R287 residues. P2A is located between blades 1 and 2 (G86, E88, K85, H90, D82, and N65), whereas P2D penetrates through blades 1 and 2 formed by loop A, which is close to P2A (S481, F485, D482, L115, I114, R113, H90, E88, R526, and S525). P3 is located between the beta-propeller domain and alpha/beta hydrolase containing the residues M561, A564, L568, F381, T380, I20, A21, F41, K24, G40, G44, and V46
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Henry (nitroaldol) reaction
hydrolysis of peptide bond
hydrolysis of peptide bond
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PATHWAY SOURCE
PATHWAYS
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CAS REGISTRY NUMBER
COMMENTARY
73562-30-8
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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
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala + H2O
2-aminobenzoyl-Ala-Leu-Phe + Gln-Gly-Pro-Phe(NO2)-Ala
2-aminobenzoyl-GFEPF(NO2)RA + H2O
?
good substrate, displays greater kinetic specificity than acetyl-Phe-2-naphthylamide
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?
Ac-Ala-7-amido-4-methylcoumarin + H2O
N-acetyl-L-Ala + 7-amino-4-methylcoumarin
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?
Ac-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
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?
Ac-Phe-2-naphthylamide + H2O
N-acetyl-L-Phe + 2-naphthylamine
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?
Ac-Phe-4-nitroanilide + H2O
N-acetyl-L-Phe + 4-nitroaniline
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?
acetyl-Ala-7-amido-4-methylcoumarin + H2O
?
very slow hydrolysis
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?
acetyl-Ala-7-amido-4-methylcoumarin + H2O
acetyl-Ala + 7-amino-4-methylcoumarin
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?
acetyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O
acetyl-Ala + Ala-Ala-Ala-Ala-Ala
AB009494
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?
acetyl-Ala-Met + H2O
acetyl-Ala + Met
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native enzyme shows 70.4% of the activity compared to acetyl-Ala-Ala as substrate
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?
acetyl-Gly-Leu + H2O
acetyl-Gly + Leu
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native enzyme shows 30.3% of the activity compared to acetyl-Ala-Ala as substrate
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?
acetyl-Met-7-amido-4-methylcoumarin + H2O
acetyl-Met + 7-amino-4-methylcoumarin
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?
acetyl-Met-Ala-Ala-Ala-Ala-Ala + H2O
acetyl-Met + Ala-Ala-Ala-Ala-Ala
AB009494
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?
acetyl-Met-Asn + H2O
acetyl-Met + Asn
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native enzyme shows 34.1% of the activity compared to acetyl-Ala-Ala as substrate
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?
acetyl-Met-Phe + H2O
acetyl-Met + Phe
native enzyme shows 5% of the activity compared to acetyl-Ala-Ala as substrate
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?
acetyl-Phe-2-naphthylamide + H2O
?
classical substrate of AAP
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?
acetyl-Phe-2-naphthylamide + H2O
acetyl-Phe + 2-naphthylamine
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?
acetyl-Phe-4-nitroanilide + H2O
acetyl-Phe + 4-nitroaniline
specificity rate constant is lower by one order of magnitude for acetyl-Leu-4-nitroanilide than for acetyl-Phe-4-nitroanilide
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?
acetyl-Tyr-4-nitroanilide + H2O
acetyl-Tyr + 4-nitroaniline
AB009494
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?
formyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala-Ala-Ala-Ala
AB009494
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?
formyl-Gly-Val + H2O
formyl-Gly + Val
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native enzyme shows 30.3% of the activity compared to acetyl-Ala-Ala as substrate
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?
formyl-Met-Ala-Ala-Ala-Ala-Ala + H2O
formyl-Met + Ala-Ala-Ala-Ala-Ala
AB009494
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?
formylmethionine-beta-naphthylamide + H2O
formylmethionine + beta-naphthylamine
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?
glutaryl-GGF-7-amido-4-methylcoumarin + H2O
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has a rate constant comparable to that of acetyl-Phe-2-naphthylamide
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?
glycated ribulose-1,5-diphosphate carboxylase/oxygenase protein + H2O
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no degradation of the native protein
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?
N-acetyl-Ala-beta-naphthylamide + H2O
N-acetyl-Ala + beta-naphthylamine
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?
N-acetyl-L-alanine 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
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?
N-acetyl-L-Met-epsilon-L-Lys-Ala-NH2 + H2O
N-acetyl-L-Met + L-Lys-L-Ala-NH2
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?
N-acetyl-L-Phe-4-nitroanilide + H2O
N-acetyl-L-Phe + 4-nitroaniline
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?
N-acetyl-Leu p-nitroanilide + H2O
N-acetyl-Leu + p-nitroaniline
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?
N-acetyl-Leu-4-nitroanilide + H2O
N-acetyl-Leu + 4-nitroaniline
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?
N-acetyl-Leu-p-nitroanilide + H2O
N-acetyl-Leu + p-nitroaniline
esterase activity of wild-type enzyme with p-nitrophenyl caprylate as substrate is 7times higher than peptidase activity with N-acetyl-Leu-p-nitroanilide as substrate, 150fold higher for mutant enzyme R526V, peptidase activity for mutant R526E is abolished
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?