Information on EC 3.4.19.1 - acylaminoacyl-peptidase

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The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.4.19.1
-
RECOMMENDED NAME
GeneOntology No.
acylaminoacyl-peptidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
AAP
Q9YBQ2
-
AAP
Aeropyrum pernix DSM 11879
Q9YBQ2
-
-
AARE
Q973W9
-
AARE
Sulfolobus tokodaii 7
Q973W9
-
-
acyl peptide hydrolase
-
-
Acyl-peptide hydrolase
-
-
-
-
acyl-peptide releasing enzyme
Q973W9
-
acyl-peptide releasing enzyme
Sulfolobus tokodaii 7
Q973W9
-
-
acylamino acid-releasing enzyme
-
-
acylamino-acid-releasing enzyme
-
-
-
-
acylaminoacyl peptidase
Q9YBQ2
-
acylaminoacyl peptidase
O58323
-
Acylaminoacyl-peptidase
-
-
-
-
acylpeptide hydrolase
Q9YBQ2
-
acylpeptide hydrolase
-
-
acylpeptide hydrolase
-
-
acylpeptide hydrolase
-
-
acylpeptide hydrolase
Q7LX61
-
acylpeptide hydrolase
Q7LX61
-
-
acylpeptide hydrolase
-
-
acylpeptide hydrolase
synthetic construct
-
-
acylpeptide hydrolase/esterase
-
-
alpha-N-acylpeptide hydrolase
-
-
-
-
ApAAP
Q9YBQ2
-
APEH
Q7LX61
-
-
apeH-2
Q7LX61
gene name
apeH-2
Q7LX61
gene name
-
APEH-3Ss
Q97VD6
-
APH
-
-
APH
synthetic construct
-
-
AtAARE
Q84LM4
-
DNF15S2 protein
-
-
-
-
N-acylaminoacyl-peptide hydrolase
-
-
-
-
N-acylpeptide hydrolase
-
-
-
-
N-formylmethionine (fMet) aminopeptidase
-
-
-
-
OP85
-
-
PhAAP
Pyrococcus horikoshii DSM 12428
O58323
-
-
pi-APH
-
-
PM hydrolase
-
-
PM hydrolase
Streptomyces morookaense JCM4673
-
-
-
PMH
Streptomyces morookaense JCM4673
-
-
-
sso2141
Q7LX61
gene name
sso2141
Q7LX61
gene name
-
SSO2693
Q97VD6
gene name
ST0779
Q973W9
-
ST0779
Sulfolobus tokodaii 7
Q973W9
-
-
CAS REGISTRY NUMBER
COMMENTARY
73562-30-8
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain K1
-
-
Manually annotated by BRENDA team
Aeropyrum pernix DSM 11879
-
Uniprot
Manually annotated by BRENDA team
L. suyo
-
-
Manually annotated by BRENDA team
Pyrococcus horikoshii DSM 12428
-
UniProt
Manually annotated by BRENDA team
Sprague-Dawley rat
-
-
Manually annotated by BRENDA team
strain JCM4673
-
-
Manually annotated by BRENDA team
Streptomyces morookaense JCM4673
strain JCM4673
-
-
Manually annotated by BRENDA team
Sulfolobus tokodaii 7
-
SwissProt
Manually annotated by BRENDA team
synthetic construct
-
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
-
endopeptidase activity
-
-
?
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala + H2O
2-aminobenzoyl-Ala-Leu-Phe + Gln-Gly-Pro-Phe(NO2)-Ala
show the reaction diagram
Aeropyrum pernix DSM 11879
Q9YBQ2
endopeptidase activity
-
-
?
2-aminobenzoyl-EALFQGPF(NO2)A + H2O
?
show the reaction diagram
Q9YBQ2
very good substrate
-
-
?
2-aminobenzoyl-EFSPF(NO2)RA + H2O
?
show the reaction diagram
Q9YBQ2
-
-
-
?
2-aminobenzoyl-GFEPF(NO2)RA + H2O
?
show the reaction diagram
Q9YBQ2
good substrate, displays greater kinetic specificity than acetyl-Phe-2-naphthylamide
-
-
?
2-aminobenzoyl-KARVLF(NO2)EA-Nle + H2O
?
show the reaction diagram
Q9YBQ2
poor substrate
-
-
?
2-aminobenzoyl-RPIITTAGPSF(NO2)A + H2O
?
show the reaction diagram
Q9YBQ2
-
-
-
?
2-aminobenzoyl-SAVLQSGF(NO2)A + H2O
?
show the reaction diagram
Q9YBQ2
good substrate
-
-
?
2-naphthyl butyrate + H2O
2-naphthol + butanoate
show the reaction diagram
-
-
-
-
?
Abz-EFSPF(NO2)RA + H2O
?
show the reaction diagram
O58323
-
-
-
?
Abz-GFEPF(NO2)RA + H2O
?
show the reaction diagram
O58323
-
-
-
?
Abz-KARVLF(NO2)EANle + H2O
?
show the reaction diagram
O58323
-
-
-
?
Abz-SAVLQSGF(NO2)A + H2O
?
show the reaction diagram
O58323
-
-
-
?
Ac-Ala-7-amido-4-methylcoumarin + H2O
N-acetyl-L-Ala + 7-amino-4-methylcoumarin
show the reaction diagram
O58323
-
-
-
?
Ac-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
show the reaction diagram
O58323
-
-
-
?
Ac-Leu-p-nitroanilide + H2O
Ac-Leu + p-nitroaniline
show the reaction diagram
-
substrate peptidase assay
-
-
?
Ac-Phe-2-naphthylamide + H2O
?
show the reaction diagram
O58323
-
-
-
?
Ac-Phe-2-naphthylamide + H2O
N-acetyl-L-Phe + 2-naphthylamine
show the reaction diagram
O58323
-
-
-
?
Ac-Phe-4-nitroanilide + H2O
N-acetyl-L-Phe + 4-nitroaniline
show the reaction diagram
O58323
-
-
-
?
acety-Ala-Ala methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
acety-Ala-Ala-Phe-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
acety-Ala-Gly-D-Ala-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Ala-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
Q9YBQ2
very slow hydrolysis
-
-
?
acetyl-Ala-7-amido-4-methylcoumarin + H2O
acetyl-Ala + 7-amino-4-methylcoumarin
show the reaction diagram
synthetic construct
-
-
-
-
?
acetyl-Ala-Ala + H2O
acetyl-Ala + Ala
show the reaction diagram
-
-
-
?
acetyl-Ala-Ala + H2O
acetyl-Ala + Ala
show the reaction diagram
Q84LM4
-
-
?
Acetyl-Ala-Ala-Ala + H2O
Acetyl-Ala + Ala-Ala
show the reaction diagram
-
native enzyme shows 147% of the activity compared to acetyl-Ala-Ala as substrate
-
?
Acetyl-Ala-Ala-Ala + H2O
Acetyl-Ala + Ala-Ala
show the reaction diagram
Q84LM4
native enzyme shows 81% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Ala-Ala-Ala-Ala + H2O
acetyl-Ala + Ala-Ala-Ala
show the reaction diagram
Q84LM4
native enzyme shows 126% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Ala-Ala-Ala-Ala + H2O
acetyl-Ala + Ala-Ala-Ala
show the reaction diagram
-
native enzyme shows 85.6% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Ala-Met + H2O
acetyl-Ala + Met
show the reaction diagram
-
native enzyme shows 70.4% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Gly-Gly + H2O
acetyl-Gly + Gly
show the reaction diagram
-
native enzyme shows 37% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Gly-Gly + H2O
acetyl-Gly + Gly
show the reaction diagram
Q84LM4
native enzyme shows 4% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Gly-Leu + H2O
acetyl-Gly + Leu
show the reaction diagram
-
native enzyme shows 30.3% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Leu-4-nitroanilide + H2O
acetyl-Leu + 4-nitroaniline
show the reaction diagram
Q9YBQ2
specificity rate constant is lower by one order of magnitude for acetyl-Leu-4-nitroanilide than for acetyl-Phe-4-nitroanilide
-
-
?
acetyl-Met-Ala + H2O
acetyl-Met + Ala
show the reaction diagram
-
native enzyme shows 4% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Met-Ala + H2O
acetyl-Met + Ala
show the reaction diagram
Q84LM4
native enzyme shows 45% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Met-Asn + H2O
acetyl-Met + Asn
show the reaction diagram
-
native enzyme shows 34.1% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Met-Glu + H2O
acetyl-Met + Glu
show the reaction diagram
-
native enzyme shows 4.3% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Met-Glu + H2O
acetyl-Met + Glu
show the reaction diagram
Q84LM4
native enzyme shows 6% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Met-Phe + H2O
acetyl-Met + Phe
show the reaction diagram
Q84LM4
native enzyme shows 5% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Phe-2-naphthylamide + H2O
?
show the reaction diagram
Q9YBQ2
classical substrate of AAP
-
-
?
acetyl-Phe-2-naphthylamide + H2O
acetyl-Phe + 2-naphthylamine
show the reaction diagram
Q9YBQ2
-
-
-
?
acetyl-Phe-4-nitroanilide + H2O
acetyl-Phe + 4-nitroaniline
show the reaction diagram
Q9YBQ2
specificity rate constant is lower by one order of magnitude for acetyl-Leu-4-nitroanilide than for acetyl-Phe-4-nitroanilide
-
-
?
Ala-Ala + H2O
Ala + Ala
show the reaction diagram
Sulfolobus tokodaii, Sulfolobus tokodaii 7
Q973W9
-
-
-
?
Ala-Ala-Ala + H2O
Ala-Ala + Ala
show the reaction diagram
-
-
-
?
Ala-Ala-Ala + H2O
Ala + Ala-Ala
show the reaction diagram
Sulfolobus tokodaii, Sulfolobus tokodaii 7
Q973W9
-
-
-
?
Ala-Ala-Ala-Ala + H2O
Ala-Ala + Ala-Ala
show the reaction diagram
-
-
-
?
Ala-Ala-Ala-Ala + H2O
Ala + Ala-Ala-Ala
show the reaction diagram
Sulfolobus tokodaii, Sulfolobus tokodaii 7
Q973W9
-
-
-
?
Ala-beta-naphthylamide + H2O
Ala + 2-naphthylamine
show the reaction diagram
Streptomyces morookaense, Streptomyces morookaense JCM4673
-
-
-
-
?
Ala-p-nitroanilide + H2O
Ala + p-nitroaniline
show the reaction diagram
Streptomyces morookaense, Streptomyces morookaense JCM4673
-
prefered substrate for PMH
-
-
?
alpha-melanocyte stimulating hormone + H2O
?
show the reaction diagram
-
-
-
-
?
amyloid-beta peptide + H2O
?
show the reaction diagram
-
-
-
-
?
Asp-Ala-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Asp-Pro-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
butyryl thiocholine + H2O
?
show the reaction diagram
-
-
-
-
?
butyryl-Ala-Ala-Ala + H2O
butyryl-Ala + Ala-Ala
show the reaction diagram
-
native enzyme shows 33.6% of the activity compared to acetyl-Ala-Ala as substrate
-
?
butyryl-Ala-Ala-Ala + H2O
butyryl-Ala + Ala-Ala
show the reaction diagram
Q84LM4
native enzyme shows 77% of the activity compared to acetyl-Ala-Ala as substrate
-
?
formyl-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala
show the reaction diagram
Q973W9
-
-
-
?
formyl-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala
show the reaction diagram
-
native enzyme shows 62.4% of the activity compared to acetyl-Ala-Ala as substrate
-
?
formyl-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala
show the reaction diagram
Q84LM4
native enzyme shows 81% of the activity compared to acetyl-Ala-Ala as substrate
-
?
formyl-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala
show the reaction diagram
Sulfolobus tokodaii 7
Q973W9
-
-
-
?
formyl-Gly-Val + H2O
formyl-Gly + Val
show the reaction diagram
-
native enzyme shows 30.3% of the activity compared to acetyl-Ala-Ala as substrate
-
?
formylalanine-Ala-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
formylalanine-Ala-Ala-Ala-Ala-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
formylmethionine p-nitroanilide + H2O
formylmethionine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
formylmethionine-Ala + H2O
formylmethionine + Ala
show the reaction diagram
-
-
-
-
?
formylmethionine-Ala-Ala-Ala-Ala-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
formylmethionine-Ala-Ser + H2O
?
show the reaction diagram
-
-
-
-
?
formylmethionine-beta-naphthylamide + H2O
formylmethionine + beta-naphthylamine
show the reaction diagram
-
-
-
-
?
formylmethionine-Leu + H2O
formylmethionine + Leu
show the reaction diagram
-
-
-
-
?
formylmethionine-Leu-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
formylmethionine-Leu-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
formylmethionine-Leu-Tyr + H2O
?
show the reaction diagram
-
-
-
-
?
formylmethionine-Phe + H2O
formylmethionine + Phe
show the reaction diagram
-
-
-
-
?
formylmethionine-Trp + H2O
formylmethionine + Trp
show the reaction diagram
-
-
-
-
?
formylmethionine-Val + H2O
formylmethionine + Val
show the reaction diagram
-
-
-
-
?
glutaryl-GGF-7-amido-4-methylcoumarin + H2O
?
show the reaction diagram
Q9YBQ2
has a rate constant comparable to that of acetyl-Phe-2-naphthylamide
-
-
?
Gly-Ala-Ala + H2O
Gly-Ala + Ala
show the reaction diagram
-
-
-
?
Gly-Phe-2-naphthylamide + H2O
Gly-Phe + 2-naphthylamine
show the reaction diagram
O58323
-
-
-
?
Gly-Phe-2-naphthylamide + H2O
?
show the reaction diagram
Q9YBQ2
-
-
-
?
glycated ribulose-1,5-diphosphate carboxylase/oxygenase protein + H2O
?
show the reaction diagram
-
no degradation of the native protein
-
?
isoAsp-Ala-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
isoD/DAEFRHDSGYEVHHQKLVFFAEDVGSNKGA-NH2 + H2O
?
show the reaction diagram
-
-
-
-
?
N-acety-Ala-Ala + H2O
N-acetyl-Ala + Ala
show the reaction diagram
Sulfolobus tokodaii, Sulfolobus tokodaii 7
Q973W9
-
-
-
?
N-acety-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
show the reaction diagram
Q973W9
-
-
-
?
N-acetyl-Ala ethyl ester + H2O
N-acetyl-Ala + ethanol
show the reaction diagram
-
-
-
?
N-acetyl-Ala p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
show the reaction diagram
-
-
-
?
N-acetyl-Ala p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala + H2O
N-acetyl-Ala + Ala
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala + H2O
N-acetyl-Ala + Ala
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala + H2O
N-acetyl-Ala + Ala
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala + H2O
N-acetyl-Ala + Ala
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala + H2O
N-acetyl-Ala + Ala
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala + H2O
N-acetyl-Ala + Ala
show the reaction diagram
-
N-acetyl-Ala-Ala
-
?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
show the reaction diagram
-
N-acetyl-Ala-Ala-Ala
-
?
N-acetyl-Ala-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala-Ala
show the reaction diagram
-
-
-
-
N-acetyl-Ala-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala-Ala
show the reaction diagram
-
-
-
-
-
N-acetyl-Ala-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala-Ala
show the reaction diagram
-
-
-
-
-
N-acetyl-Ala-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala-Ala
show the reaction diagram
-
-
-
-
-
N-acetyl-Ala-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala-Ala
show the reaction diagram
-
-
-
-
-
N-acetyl-Ala-Ala-Ala-Ala-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala-Ala-Ala-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala-Ala-Ala-Glu-Glu-Glu-Lys + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala-Gln-Nepsilon-acetyl-Lys + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala-Gln-Nepsilon-succinyl-Lys + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala-His-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ala-Pro + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Asp + H2O
N-acetyl-Ala + Asp
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-beta-naphthylamide + H2O
N-acetyl-Ala + beta-naphthylamine
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Gly + H2O
N-acetyl-Ala + Gly
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Gly-Ala-D-Ala-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-His-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Leu + H2O
N-acetyl-Ala + Leu
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Lys + H2O
N-acetyl-Ala + Lys
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Met + H2O
N-acetyl-Ala + Met
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
show the reaction diagram
-
-
-
?
N-acetyl-Ala-p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
show the reaction diagram
-
-
-
?
N-acetyl-Ala-p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
show the reaction diagram
-
-
-
?
N-acetyl-Ala-p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
show the reaction diagram
-
substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Gly-p-nitranilide, N-acetyl-Met-p-nitranilide
-
?
N-acetyl-Ala-p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
show the reaction diagram
Q84LM4
substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Met-p-nitranilide, N-acetyl-Gly-p-nitranilide
-
?
N-acetyl-Ala-Phe + H2O
N-acetyl-Ala + Phe
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Ser + H2O
N-acetyl-Ala + Ser
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Thr + H2O
N-acetyl-Ala + Thr
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Trp + H2O
N-acetyl-Ala + Trp
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Tyr + H2O
N-acetyl-Ala + Tyr
show the reaction diagram
-
-
-
-
?
N-acetyl-Ala-Tyr-Ile + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-alanyl-4-nitroanilide + H2O
N-acetyl-L-Ala + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-acetyl-Glu p-nitroanilide + H2O
N-acetyl-Glu + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-acetyl-Gly-Ala + H2O
N-acetyl-Gly + Ala
show the reaction diagram
-
weak activity
-
-
?
N-acetyl-Gly-p-nitroanilide + H2O
N-acetyl-Gly + p-nitroaniline
show the reaction diagram
-
substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Gly-p-nitranilide, N-acetyl-Met-p-nitranilide
-
?
N-acetyl-Gly-p-nitroanilide + H2O
N-acetyl-Gly + p-nitroaniline
show the reaction diagram
Q84LM4
substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Met-p-nitranilide, N-acetyl-Gly-p-nitranilide
-
?
N-acetyl-L-alanine 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-acetyl-L-alanyl 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
show the reaction diagram
Q97VD6
-
-
-
?
N-acetyl-L-alanyl 4-nitroanilide + H2O
N-acetyl-L-alanyl + 4-nitroaniline
show the reaction diagram
Q7LX61
-
-
-
?
N-acetyl-L-alanyl-p-nitroanilide + H2O
N-acetyl-L-alanine + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-acetyl-L-leucyl 4-nitroanilide + H2O
N-acetyl-L-leucine + 4-nitroaniline
show the reaction diagram
Q97VD6
-
-
-
?
N-acetyl-L-leucyl 4-nitroanilide + H2O
N-acetyl-L-leucine + 4-nitroaniline
show the reaction diagram
Q7LX61
preference for N-acetyl-L-leucyl 4-nitroanilide over N-acetyl-L-alanyl 4-nitroanilide
-
-
?
N-acetyl-L-Met-alpha-L-Lys-Ala-NH2 + H2O
N-acetyl-L-Met + L-Lys-Ala-NH2
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Met-epsilon-L-Lys-Ala-NH2 + H2O
N-acetyl-L-Met + L-Lys-L-Ala-NH2
show the reaction diagram
-
-
-
?
N-acetyl-L-phenylalanyl 4-nitroanilide + H2O
N-acetyl-L-phenylalanyl + 4-nitroaniline
show the reaction diagram
Q97VD6
-
-
-
?
N-acetyl-Leu p-nitroanilide + H2O
N-acetyl-Leu + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-acetyl-Leu-4-nitroanilide + H2O
N-acetyl-Leu + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-acetyl-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
show the reaction diagram
Aeropyrum pernix, Aeropyrum pernix DSM 11879
-
switch of substrate specificity of hyperthermophilic promiscuous acylaminoacyl peptidase by combination of protein and solvent engineering into a specific carboxylesterase
-
-
?
N-acetyl-Leu-Ala + H2O
N-acetyl-Leu + Ala
show the reaction diagram
-
-
-
-
?
N-acetyl-Leu-p-nitroanilide + H2O
N-acetyl-Leu + p-nitroaniline
show the reaction diagram
Q9YBQ2
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
-
-
?
N-acetyl-Met-Ala + H2O
N-acetyl-Met + Ala
show the reaction diagram
-
-
-
-
?
N-acetyl-Met-Ala + H2O
N-acetyl-Met + Ala
show the reaction diagram
-
-
-
-
?
N-acetyl-Met-Ala + H2O
N-acetyl-Met + Ala
show the reaction diagram
-
-
-
-
?
N-acetyl-Met-Ala-Ala-Ala-Ala-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Met-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Met-Asp-Arg-Val-Leu-Ser-Arg-Tyr + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Met-Asp-Glu-Thr-Gly-Asp-Thr-Ala-Leu-Val-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Met-epsilon-Lys + H2O
N-acetyl-Met + Lys
show the reaction diagram
-
-
-
?
N-acetyl-Met-Leu + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Met-Leu-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Met-Leu-Phe + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-Met-Lys + H2O
N-acetyl-Met + Lys
show the reaction diagram
-
-
-
?
N-acetyl-Met-p-nitroanilide + H2O
N-acetyl-Met + p-nitroaniline
show the reaction diagram
-
substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Gly-p-nitranilide, N-acetyl-Met-p-nitranilide
-
?
N-acetyl-Met-p-nitroanilide + H2O
N-acetyl-Met + p-nitroaniline
show the reaction diagram
Q84LM4
substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Met-p-nitranilide, N-acetyl-Gly-p-nitranilide
-
?
N-acetyl-Phe-2-naphthylamide + H2O
N-acetyl-L-Phe + 2-naphthylamine
show the reaction diagram
-
kinetic assay
-
-
?
N-acetyl-Phe-2-naphthylamide + H2O
N-acetyl-Phe + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
N-acetyl-Phe-2-naphthylamide + H2O
N-acetyl-Phe + 2-naphthylamine
show the reaction diagram
Aeropyrum pernix DSM 11879
Q9YBQ2
-
-
-
?
N-acetyl-Phe-Ala + H2O
N-acetyl-Phe + Ala
show the reaction diagram
-
weak activity
-
-
?
N-acetyl-Ser-Ala + H2O
N-acetyl-Ser + Ala
show the reaction diagram
-
-
-
-
?
N-acetyl-Tyr p-nitroanilide + H2O
N-acetyl-Tyr + p-nitroaniline
show the reaction diagram
-
-
-
-
?
N-acetyl-Tyr-Ala + H2O
N-acetyl-Tyr + Ala
show the reaction diagram
-
weak activity
-
-
?
N-acylpeptide + H2O
?
show the reaction diagram
-
acylpeptide hydrolase catalyzes the hydrolysis of short peptides of the type Nalpha-acyl to form an acyl amino acid and a peptide with a free N-terminus
-
-
-
p-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl butyrate + H2O
?
show the reaction diagram
-
-
-
-
?
p-nitrophenyl caprylate + H2O
nitrophenol + caprylate
show the reaction diagram
Q9YBQ2
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
-
-
?
p-nitrophenyl hexanoate + H2O
p-nitrophenol + hexanoate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl propionate + H2O
p-nitrophenol + propionate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl valerate + H2O
p-nitrophenol + pentanoate
show the reaction diagram
-
-
-
-
?
Phe-beta-naphthylamide + H2O
Phe + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
Phe-p-nitroanilide + H2O
Phe + p-nitroaniline
show the reaction diagram
-
prefered substrate for PMH
-
-
?
Pro-beta-naphthylamide + H2O
Pro + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
puromycin + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-AAPF-2-naphthylamide + H2O
?
show the reaction diagram
Q9YBQ2
hydrolysed at a significantly slower rate than acetyl-Phe-2-naphthylamide
-
-
?
Tyr-beta-naphthylamide + H2O
Tyr + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
Tyr-Leu + H2O
Tyr + Leu
show the reaction diagram
Streptomyces morookaense, Streptomyces morookaense JCM4673
-
-
-
-
?
Tyr-Phe + H2O
Tyr + Phe
show the reaction diagram
Streptomyces morookaense, Streptomyces morookaense JCM4673
-
-
-
-
?
Leu-beta-naphthylamide + H2O
Leu + 2-naphthylamine
show the reaction diagram
Streptomyces morookaense, Streptomyces morookaense JCM4673
-
-
-
-
?
additional information
?
-
-
specific for N-terminal acylmethionine residues
-
-
-
additional information
?
-
-
rapid removal of acetyl-Thr, acetyl-Ala, acetyl-Met, acetyl-Ser and more slowly acetyl-Gly from peptides of different lengths. Other N-acetylated amino acids, Cys, Tyr, Asp, Val, Phe, Ile, Leu, may be removed at 1% or less of the rate of the good substrates
-
-
-
additional information
?
-
-
the trypsin-modified enzyme is able to unblock alphaA-crystallin and displays endoprotease activity unlike the native enzyme
-
-
-
additional information
?
-
-
N-acetylated peptides with D-Ala in position 3 or 4 as are good substrates as those containing L-Ala. Peptides with Pro in position 2 are inactive, and most of the peptides with Pro in the third position are very good substrates. Only the peptide acetyl-AAP gives 30% of the activity of acetyl-AAA, which is reduced to 1-2% if additional residues are present at the C-terminus, acety-AAPA or acetyl-AAPAA. The presence of a positive charge in position 2,3,4,5 and 6 gives strong reduction in hydrolase activity, varying with the charge's distance from the N-terminus from 9 to 15-20% of the rate obtained with the reference peptides without positive charges. Deprotonation of His at high pH generates excellent substrates, and removal of the positive charges of Lys by acetylation or succinylation give improved substrate quality. Long peptides with 10-29 residues, are poor substrates, especially when they contain positive charges and Pro
-
-
-
additional information
?
-
-
peptidase activity is only exerted on peptides with Gly or Ala at their N-termini
-
-
-
additional information
?
-
-
the enzyme might not only be involved in the catabolism of intracellular N-acylated protein catabolism but also be responsible for the biological utilization of N-acylated food proteins
-
-
-
additional information
?
-
-
the enzyme may be involved in N-terminal deacylation of nascent polypeptide chains and of bioactive peptides
-
-
-
additional information
?
-
-
the enzyme may be involved in regulation of neuropeptide turnover
-
?
additional information
?
-
-
the enzyme might be involved in not only catalysis of the N-terminal hydrolysis of Nalpha-acylpeptides but also the elimination of glycated proteins
-
?
additional information
?
-
-
His507 of acylaminoacyl peptidase stabilizes the active site conformation, not the catalytic intermediate
-
-
-
additional information
?
-
-
catalyzes the NH2-terminal hydrolysis of N-acylpeptides to release N-acylated amino acids
-
-
-
additional information
?
-
O58323
cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
-
-
-
additional information
?
-
-
removal of an N-acylated amino acid from blocked peptides
-
-
-
additional information
?
-
Q7LX61
no activity with L-leucyl 4-nitroanilide or L-alanyl 4-nitroanilide. The enzyme is able to hydrolyse N-succinyl-Gly-Gly-Phe 4-nitroanilide, showing endopeptidase activity
-
-
-
additional information
?
-
Q97VD6
no activity with L-leucyl 4-nitroanilide, L-alanyl 4-nitroanilide or L-phenylalanyl 4-nitroanilide. The enzyme also shows endopeptidase activity
-
-
-
additional information
?
-
Aeropyrum pernix, Aeropyrum pernix DSM 11879
-
hundreds nanosecond all-atom atomistic molecular dynamics simulations of a representative member of the acylaminoacyl peptidase subfamily (Aeropyrum pernix K1) allow to identify the presence of a tunnel which from the surrounding of the N-terminal alpha1-helix bring to the catalytic site and it is regulated by conformational changes of the N-terminal alpha-helix itself and its surroundings in the native conformational ensemble
-
-
-
additional information
?
-
Q7LX61
no activity with L-leucyl 4-nitroanilide or L-alanyl 4-nitroanilide. The enzyme is able to hydrolyse N-succinyl-Gly-Gly-Phe 4-nitroanilide, showing endopeptidase activity
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme might not only be involved in the catabolism of intracellular N-acylated protein catabolism but also be responsible for the biological utilization of N-acylated food proteins
-
-
-
additional information
?
-
-
the enzyme may be involved in N-terminal deacylation of nascent polypeptide chains and of bioactive peptides
-
-
-
additional information
?
-
-
the enzyme may be involved in regulation of neuropeptide turnover
-
?
additional information
?
-
-
the enzyme might be involved in not only catalysis of the N-terminal hydrolysis of Nalpha-acylpeptides but also the elimination of glycated proteins
-
?
additional information
?
-
-
catalyzes the NH2-terminal hydrolysis of N-acylpeptides to release N-acylated amino acids
-
-
-
additional information
?
-
O58323
cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
-
-
-
additional information
?
-
-
removal of an N-acylated amino acid from blocked peptides
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cl-
-
activates
Cl-
-
0.1-0.5 M, activates activity towards N-acetyl-Ala p-nitroanilide and N-acetyl-Ala beta-naphthylamide
SCN-
-
0.1-0.5 M, activates towards N-acetyl-Ala p-nitroanilide and N-acetyl-Ala beta-naphthylamide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(10E,12Z)-octadeca-10,12-dienoic acid
-
non-competitive inhibition mechanism
1-butane boronic acid
-
-
1-ethyl-3,3'-dimethylaminopropylcarbodiimide
-
-
1-methylethyl dodecylphosphonofluoridoate
-
IC50: 0.00026 mM
1-methylethyl dodecylphosphonofluoridoate
-
IC50: 0.0015 mM
2-(octyloxy)-4H-1,3,2-benzodioxaphosphinine 2-oxide
-
IC50: 0.00018 mM
2-(octyloxy)-4H-1,3,2-benzodioxaphosphinine 2-oxide
-
IC50: 0.00023 mM
2-(pentylsulfanyl)-4H-1,3,2-benzodioxaphosphinine 2-oxide
-
IC50: 0.0015 mM
2-(pentylsulfanyl)-4H-1,3,2-benzodioxaphosphinine 2-oxide
-
IC50: 0.0011 mM
2-heptyl-4H-1,3,2-benzodioxaphosphinine 2-oxide
-
IC50: 0.0014 mM
2-heptyl-4H-1,3,2-benzodioxaphosphinine 2-oxide
-
IC50: 0.0016 mM
4-(2-aminoethyl) benzenesulfonyl fluoride
-
-
5,5'-dithiobis-(2-nitrobenzoate)
-
partial
Ac-Ala
-
competitive inhibitor
Ac-Gly-prolineboronic acid
synthetic construct
-
-
Ac-Leu-CH2-Cl
-
irreversible inhibitor
Ac-Met
-
competitive inhibitor
Ac-Phe-OH
-
product-like inhibitor
acephate
-
IC50: 0.0062 mM
acetyl-Gly-prolineboronic acid
synthetic construct
-
selectivity for APH 25fold higher than for fibroblast activation protein
Acetyl-Phe
-
-
Acetyl-Phe
-
forms hydrogen bonds with both NH groups of the oxyanion binding site of AAP. In the mutant enzyme the NH bond of Gly369 points in a different direction
activated-thiol-Sepharose
-
-
-
ampicillin
-
partial
bis(1-methylethyl) 4-nitrophenyl phosphate
-
IC50: 0.016 mM
bis(sulfosuccinimidyl)suberate
-
-
CaCl2
Q7LX61
100 mM, 52% inhibition
carbodiimide/aminoalkyl-agarose
-
-
-
carbodiimide/dicarboxylic acid
-
-
-
chlorfenvinphos
-
IC50 at pH 7.4, 37C: 1386 nM
chlorpyrifos
-
IC50: 0.000021 mM
chlorpyrifos
-
IC50: 0.000071 mM
chlorpyrifos cyclohexyl
-
IC50: 0.00086 mM
chlorpyrifos cyclohexyl
-
IC50: 0.00035 mM
chlorpyrifos isopropyl
-
IC50: 0.0033 mM
chlorpyrifos methyl
-
IC50: 0.000080 mM
chlorpyrifos methyl
-
IC50: 0.00031 mM
chlorpyrifos n-butyl
-
IC50: 0.00006 mM
chlorpyrifos n-propyl
-
IC50: 0.00007 mM
chlorpyrifos-methyl oxon
-
IC50 at pH 7.4, 37C: 18.3 nM
Cl-
-
activity towards N-acetyl-Ala-Ala and N-acetyl-Ala-Ala-Ala
CoCl2
-
1 mM, 21% inhibition
Cu2+
Q84LM4
1 mM, complete inhibition of recombinant enzyme
Cu2+
-
1 mM, complete inhibition of recombinant enzyme
DFP
-
IC50 at pH 7.4, 37C: 22.5 nM
DFP
-
-
DFP
-
-
DFP
-
the reactive residue is Ser587
di(2-pyridyl)disulfide
-
-
diazoxon
-
IC50 at pH 7.4, 37C: 1386 nM
diazoxon
-
IC50: 0.00093 mM
diazoxon
-
IC50: 0.00089 mM
dichlorvos
-
IC50 at pH 7.4, 37C: 118.6 nM
dichlorvos
-
IC50: 0.00023 mM
dichlorvos
-
IC50: 0.00056 mM
dichlorvos
-
shows selectivity for acylpeptide hydrolase inhibition in vivo
dichlorvos
-
exhibits high affinity for acylpeptide hydrolase, possibly blocks its activity toward N-acylpeptide
dichlorvos
-
acylpeptide hydrolase activity shows a significant inhibition
dicyclohexyl 2,2-dichloroethenyl phosphate
-
IC50: 0.00010 mM
dicyclohexyl 2,2-dichloroethenyl phosphate
-
IC50: 0.00025 mM
diethyl 4-methyl-3-nitrophenyl phosphate
-
IC50: 0.002 mM
diethyl dicarbonate
-
-
diethyl dicarbonate
-
-
diisopropyl fluorophosphate
Q84LM4
1 mM, complete inactivation
diisopropyl fluorophosphate
-
1 mM, complete inactivation
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
-
diisopropylfluorophosphate
-
IC50: 0.000011 mM
diisopropylfluorophosphate
-
IC50: 0.000017 mM
dipentyl fluorophosphate
-
IC50: 0.000011 mM
dipentyl fluorophosphate
-
IC50: 0.0000099 mM
diphenylphosphinic fluoride
-
IC50: 0.00041 mM
diphenylphosphinic fluoride
-
IC50: 0.00024 mM
dithiothreitol
-
-
ebelactone A
-
-
EDTA
Q973W9
1 mM, 10% inhibition
epoxy-Sepharose
-
-
-
ethyl octylphosphonofluoridoate
-
IC50: 0.00011 mM
ethyl octylphosphonofluoridoate
-
IC50: 0.00021 mM
FeCl2
-
1 mM, 21% inhibition
Glutaraldehyde
-
-
Gly methyl ester
-
-
Guanidine-HCl
Q97VD6
1 M, complete loss of activity, after removal of guanidine-HCl the enzyme recovers 25% of its activity
guanidine/HCl
-
1 M, complete inactivation
heptyl ethylphosphonofluoridoate
-
IC50: 0.000027 mM
heptyl ethylphosphonofluoridoate
-
IC50: 0.00023 mM
Hg2+
-
HgCl2
iodoacetamide
-
partial
iodoacetamide
-
-
iodoacetamide
-
-
iodoacetic acid
-
partial
iodoacetic acid
-
-
K+
Q973W9
1 mM, 4% inhibition
malaoxon
-
IC50 at pH 7.4, 37C: 1400000 nM
N,N-Dimethylformamide
-
-
N-acetyl-Ala
-
competitive
N-acetyl-Ala
-
N-acetyl-D-Ala; N-acetyl-L-Ala
N-acetyl-Ala
-
-
N-acetyl-Ala chloromethyl ketone
-
inactivation follows first order kinetics, acetyl-Ala protects
N-acetyl-Leu chloromethyl ketone
-
-
N-acetyl-Met
-
-
N-acetyl-Met
-
-
N-acetyl-Val
-
-
N-ethyl-5-phenylisoxazolium 3'-sulfonate
-
i.e. Woodward's reagent
N-hydroxysuccinimide agarose
-
-
-
NaCl
-
1 mM, 78% loss of activity
naled
-
IC50: 0.00037 mM
naled
-
IC50: 0.00087 mM
NEM
Q84LM4
1 mM
NEM
-
1 mM
NEM
-
-
nonyl ethylphosphonofluoridoate
-
IC50: 0.000052 mM
nonyl ethylphosphonofluoridoate
-
IC50: 0.00028 mM
octane-1-sulfonyl fluoride
-
IC50: 0.073 mM
octane-1-sulfonyl fluoride
-
IC50: 0.067 mM
octyl methylphosphonofluoridoate
-
IC50: 0.000043 mM
octyl methylphosphonofluoridoate
-
IC50: 0.00016 mM
p-hydroxymercuribenzoate
-
-
p-nitrophenyl-N-propyl carbamate
-
potent active site-directed, pseudo-first-order kinetics
Paraoxon
-
IC50 at pH 7.4, 37C: 3805 nM
Paraoxon
-
IC50: 0.0047 mM
PCMB
Q84LM4
0.1 mM
PCMB
-
0.1 mM
PCMB
-
-
penicillin G
-
partial
pentyl ethylphosphonofluoridoate
-
IC50: 0.00013 mM
pentyl ethylphosphonofluoridoate
-
IC50: 0.00027 mM
peptide SsCEI 2
-
specific and efficient inhibition. No inhibition in presence of peptide SsCEI 3 and peptide SsCEI 4
-
phenylmethylsulfonyl fluoride
-
-
phosphatidylethanolamine-binding protein inhibitor SsCEI
-
-
-
PMSF
Q84LM4
1 mM, 50% inhibition
PMSF
-
1 mM, 50% inhibition
profenofos
-
IC50: 0.002 mM
SCN-
-
activity towards N-acetyl-Ala-Ala and N-acetyl-Ala-Ala-Ala
SDS
Q7LX61
above 0.3 mM, complete inhibition
SDS
Q973W9
1 mg/ml, complete inhibition
SDS
-
-
thimerosal
-
-
Trichlorfon
-
IC50: 0.018 mM
tridecyl methylphosphonofluoridoate
-
IC50: 0.00032 mM
tridecyl methylphosphonofluoridoate
-
IC50: 0.0048 mM
Triton X-100
Q973W9
1 mg/ml, 4% inhibition
Tween 20
Q973W9
1 mg/ml, 10% inhibition
Tween 80
Q973W9
1 mg/ml, 18% inhibition
Urea
Q97VD6
6 M, about 70% loss of activity, regains activity at almost all urea concentrations upon removal of the denaturinf agent
Urea
-
-
Zn2+
Q84LM4
1 mM, complete inhibition of recombinant enzyme
Zn2+
-
1 mM, complete inhibition of recombinant enzyme
Zn2+
-
most potent inhibitor
Mipafox
-
IC50 at pH 7.4, 37C: 3013 nM
additional information
-
alphabeta peptide (1-40) can inhibit APH activity from the cell lysates of APH transfected cells after IP at 0.01 and 0.001 mM concentration, while reversed alphabeta peptide (40-1) at the same concentrations does not show any inhibitory effect
-
additional information
-
acylpeptide hydrolase is a direct target for some organophosphate compounds
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
-
maintains catalytic activity of PMH
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00129
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala
-
pH 7.0, 70C, wild-type enzyme
-
0.00281
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala
-
pH 7.0, 70C, mutant enzyme D524N
-
0.0071
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala
-
pH 7.0, 70C, mutant enzyme D524A
-
0.06
4-nitrophenyl hexanoate
-
-
0.00913
Ac-Leu-p-nitroanilide
-
mutant D15A
0.0094
Ac-Leu-p-nitroanilide
-
mutant R18A
0.00958
Ac-Leu-p-nitroanilide
-
mutant DELTAN21
0.00963
Ac-Leu-p-nitroanilide
-
mutant D15A/R18A
0.01038
Ac-Leu-p-nitroanilide
-
wild-type
0.467
Ac-Leu-p-nitroanilide
-
mutant R526V, in the presence of 1 M sodium chloride
0.49
Ac-Leu-p-nitroanilide
-
wild-type
0.695
Ac-Leu-p-nitroanilide
-
mutant E88A/R526V, in the presence of 1 M sodium chloride
0.748
Ac-Leu-p-nitroanilide
-
wild-type, in the presence of 1 M sodium chloride
1.14
Ac-Leu-p-nitroanilide
-
mutant E88A
1.19
Ac-Leu-p-nitroanilide
-
mutant E88A/R526V
1.76
Ac-Leu-p-nitroanilide
-
mutant E88A, in the presence of 1 M sodium chloride
0.0082
acetyl-Phe-2-naphthylamide
-
wild-type
0.1
acetyl-Phe-2-naphthylamide
-
mutant H367A
0.39
Ala-beta-naphthylamide
-
-
1
butyryl thiocholine
-
-
1.7
formylmethionine-beta-naphthylamide
-
-
0.04
formylmethionine-Leu
-
-
0.18
formylmethionine-Leu-Phe
-
-
0.22
formylmethionine-Leu-Tyr
-
-
0.63
formylmethionine-Phe
-
-
0.71
formylmethionine-Trp
-
-
0.06
formylmethionine-Val
-
-
0.12
Leu-beta-naphthylamide
-
-
1.8
N-acetyl-Ala p-nitroanilide
-
-
18.4
N-acetyl-Ala p-nitroanilide
-
-
0.616
N-acetyl-Ala-4-nitroanilide
-
-
0.8
N-acetyl-Ala-Ala
-
-
7.6
N-acetyl-Ala-Ala
-
-
0.6
N-acetyl-Ala-Ala-Ala
-
-
0.8
N-acetyl-Ala-Ala-Ala-Ala
-
-
2.1
N-acetyl-Ala-Ala-Ala-Ala
-
-
13
N-acetyl-Ala-Ala-Ala-Ala
-
-
1.7
N-acetyl-Ala-Ala-Arg-Gly
-
-
2
N-acetyl-Ala-Ala-Phe-Gly
-
-
3.6
N-acetyl-Ala-Ala-Pro-Ala
-
-
0.006
N-acetyl-Ala-p-nitroanilide
-
pH 7.5
1.5
N-acetyl-Ala-p-nitroanilide
Q84LM4
pH 7.0, 37C
4.6
N-acetyl-Ala-p-nitroanilide
-
pH 7.0, 37C
0.8
N-acetyl-L-alanyl 4-nitroanilide
Q97VD6
pH 7.5, 90C
11.4
N-acetyl-L-alanyl 4-nitroanilide
Q7LX61
pH 7.5, 80C
0.3
N-acetyl-L-leucyl 4-nitroanilide
Q7LX61
pH 7.5, 80C
-
0.6
N-acetyl-L-leucyl 4-nitroanilide
Q97VD6
pH 7.5, 90C
-
4
N-acetyl-L-phenylalanyl 4-nitroanilide
Q97VD6
pH 7.5, 90C
-
11
N-acetyl-Leu p-nitroanilide
-
-
0.4
N-acetyl-Leu-p-nitroanilide
-
80C, wild-type enzyme
1.3
N-acetyl-Leu-p-nitroanilide
-
80C, mutant enzyme R526L
1.7
N-acetyl-Leu-p-nitroanilide
-
80C, mutant enzyme R526V
2.1
N-acetyl-Leu-p-nitroanilide
-
80C, mutant enzyme R526I
4.3
N-acetyl-Leu-p-nitroanilide
-
80C, mutant enzyme R526A
5.8
N-acetyl-Leu-p-nitroanilide
-
80C, mutant enzyme R526E
10.5
N-acetyl-Leu-p-nitroanilide
-
80C, mutant enzyme R526K
0.49
N-acetyl-Met-Ala
-
wild-type enzyme
0.56
N-acetyl-Met-Ala
-
recombinant wild-type enzyme
0.68
N-acetyl-Met-Ala
-
mutant enzyme D562N
0.02
N-acetyl-Met-Leu
-
-
0.16
N-acetyl-Met-Leu-Phe
-
-
0.00566
N-acetyl-Phe-2-naphthylamide
-
pH 7.0, 70C, wild-type enzyme
0.0082
N-acetyl-Phe-2-naphthylamide
-
wild-type enzyme
0.1
N-acetyl-Phe-2-naphthylamide
-
mutant H367A, larger than 0.1
0.01
naphthyl butyrate
-
-
35.7
p-nitrophenyl caprylate
-
80C, mutant enzyme R526V
38.2
p-nitrophenyl caprylate
-
80C, mutant enzyme R526K; 80C, mutant enzyme R526L
40.1
p-nitrophenyl caprylate
-
80C, mutant enzyme R526I
41.6
p-nitrophenyl caprylate
-
80C, mutant enzyme R526A
43.3
p-nitrophenyl caprylate
-
80C, wild-type enzyme
114.6
p-nitrophenyl caprylate
-
80C, mutant enzyme R526E
0.63
p-Nitrophenylacetate
-
-
0.02
p-nitrophenylbutyrate
-
-
0.16
p-nitrophenylpropionate
-
-
0.07
p-nitrophenylvalerate
-
-
0.028
Phe-beta-naphthylamide
-
-
0.013
Pro-beta-naphthylamide
-
-
1.91
puromycin
-
-
0.067
Tyr-beta-naphthylamide
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000917
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala
-
pH 7.0, 70C, mutant enzyme D524A
-
0.00525
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala
-
pH 7.0, 70C, mutant enzyme D524N
-
8.2
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala
-
pH 7.0, 70C, wild-type enzyme
-
0.49
Ac-Leu-p-nitroanilide
-
mutant E88A
2.04
Ac-Leu-p-nitroanilide
-
wild-type
2.1
Ac-Leu-p-nitroanilide
-
mutant R18A
2.14
Ac-Leu-p-nitroanilide
-
mutant D15A/R18A
2.21
Ac-Leu-p-nitroanilide
-
mutant D15A
2.64
Ac-Leu-p-nitroanilide
-
mutant DELTAN21
8.75
Ac-Leu-p-nitroanilide
-
mutant E88A/R526V
10.5
Ac-Leu-p-nitroanilide
-
mutant R526V, in the presence of 1 M sodium chloride
10.6
Ac-Leu-p-nitroanilide
-
wild-type
10.9
Ac-Leu-p-nitroanilide
-
mutant E88A/R526V, in the presence of 1 M sodium chloride
32.4
Ac-Leu-p-nitroanilide
-
mutant E88A, in the presence of 1 M sodium chloride
36.4
Ac-Leu-p-nitroanilide
-
wild-type, in the presence of 1 M sodium chloride
8.79
Ala-beta-naphthylamide
-
-
76.4
formylmethionine-beta-naphthylamide
-
-
5.17
formylmethionine-Leu
-
-
12.3
formylmethionine-Leu-Phe
-
-
15.5
formylmethionine-Leu-Tyr
-
-
70.2
formylmethionine-Phe
-
-
31.3
formylmethionine-Trp
-
-
5.94
formylmethionine-Val
-
-
17.3
N-acetyl-Ala p-nitroanilide
-
-
790
N-acetyl-Ala-Ala
-
-
281
N-acetyl-Ala-Ala-Ala-Ala
-
-
461
N-acetyl-Ala-p-nitroanilide
-
pH 7.5
5
N-acetyl-L-alanyl 4-nitroanilide
Q7LX61
pH 7.5, 80C
14
N-acetyl-L-alanyl 4-nitroanilide
Q97VD6
pH 7.5, 90C
5
N-acetyl-L-leucyl 4-nitroanilide
Q7LX61
pH 7.5, 80C
-
18
N-acetyl-L-leucyl 4-nitroanilide
Q97VD6
pH 7.5, 90C
-
8
N-acetyl-L-phenylalanyl 4-nitroanilide
Q97VD6
pH 7.5, 90C
-
330
N-acetyl-Leu p-nitroanilide
-
-
0.5
N-acetyl-Leu-p-nitroanilide
-
80C, mutant enzyme R526E
9.2
N-acetyl-Leu-p-nitroanilide
-
80C, mutant enzyme R526I
9.3
N-acetyl-Leu-p-nitroanilide
-
80C, wild-type enzyme
9.6
N-acetyl-Leu-p-nitroanilide
-
80C, mutant enzyme R526L
9.7
N-acetyl-Leu-p-nitroanilide
-
80C, mutant enzyme R526V
12.6
N-acetyl-Leu-p-nitroanilide
-
80C, mutant enzyme R526A
26.9
N-acetyl-Leu-p-nitroanilide
-
80C, mutant enzyme R526K
13.4
N-acetyl-Met-Ala
-
mutant enzyme D562N
29
N-acetyl-Met-Ala
-
recombinant wild-type enzyme
33
N-acetyl-Met-Ala
-
wild-type enzyme
5.45
N-acetyl-Met-Leu
-
-
27.1
N-acetyl-Met-Leu-Phe
-
-
4.28
N-acetyl-Phe-2-naphthylamide
-
pH 7.0, 70C, wild-type enzyme
6.6
p-nitrophenyl caprylate
-
80C, wild-type enzyme
8.1
p-nitrophenyl caprylate
-
80C, mutant enzyme R526E
9.4
p-nitrophenyl caprylate
-
80C, mutant enzyme R526K
9.6
p-nitrophenyl caprylate
-
80C, mutant enzyme R526A
20.8
p-nitrophenyl caprylate
-
80C, mutant enzyme R526I
28.5
p-nitrophenyl caprylate
-
80C, mutant enzyme R526L
30.9
p-nitrophenyl caprylate
-
80C, mutant enzyme R526V
1.69
Phe-beta-naphthylamide
-
-
1.61
Pro-beta-naphthylamide
-
-
0.98
puromycin
-
-
1.85
Tyr-beta-naphthylamide
-
-
4.07
Leu-beta-naphthylamide
-
-
additional information
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.129
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala
-
pH 7.0, 70C, mutant enzyme D524A
0
1.87
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala
-
pH 7.0, 70C, mutant enzyme D524N
0
6347
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala
-
pH 7.0, 70C, wild-type enzyme
0
0.4
N-acetyl-L-alanyl 4-nitroanilide
Q7LX61
pH 7.5, 80C
12219
17.5
N-acetyl-L-alanyl 4-nitroanilide
Q97VD6
pH 7.5, 90C
12219
16.8
N-acetyl-L-leucyl 4-nitroanilide
Q7LX61
pH 7.5, 80C
0
32.7
N-acetyl-L-leucyl 4-nitroanilide
Q97VD6
pH 7.5, 90C
0
2
N-acetyl-L-phenylalanyl 4-nitroanilide
Q97VD6
pH 7.5, 90C
0
0.414
N-acetyl-Phe-2-naphthylamide
-
pH 7.0, 70C, mutant enzyme D524A, measured under first-order conditions
39225
1.31
N-acetyl-Phe-2-naphthylamide
-
pH 7.0, 70C, mutant enzyme D524N, measured under first-order conditions
39225
865
N-acetyl-Phe-2-naphthylamide
-
pH 7.0, 70C, wild-type enzyme
39225
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.14
(10E,12Z)-octadeca-10,12-dienoic acid
-
pH 7.5, 37C
0.000575
Ac-Gly-prolineboronic acid
synthetic construct
-
-
0.0105
Ac-Phe-OH
-
wild-type enzyme
0.0178
Ac-Phe-OH
-
mutant H367A
0.0105
Acetyl-Phe
-
wild-type
0.0178
Acetyl-Phe
-
mutant H367A
0.001
peptide SsCEI 2
-
pH 7.5, 37C
-
0.00002
phosphatidylethanolamine-binding protein inhibitor SsCEI
Q7LX61
pH 7.5, 80C, substrate: N-acetyl-L-leucyl 4-nitroanilide
-
0.008
phosphatidylethanolamine-binding protein inhibitor SsCEI
Q97VD6
pH 7.5, 90C, substrate: acetyl-Leu-4-nitroanilide
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08
(10E,12Z)-octadeca-10,12-dienoic acid
-
pH 7.5, 37C
0.00026
1-methylethyl dodecylphosphonofluoridoate
-
IC50: 0.00026 mM
0.0015
1-methylethyl dodecylphosphonofluoridoate
-
IC50: 0.0015 mM
0.00018
2-(octyloxy)-4H-1,3,2-benzodioxaphosphinine 2-oxide
-
IC50: 0.00018 mM
0.00023
2-(octyloxy)-4H-1,3,2-benzodioxaphosphinine 2-oxide
-
IC50: 0.00023 mM
0.0011
2-(pentylsulfanyl)-4H-1,3,2-benzodioxaphosphinine 2-oxide
-
IC50: 0.0011 mM
0.0015
2-(pentylsulfanyl)-4H-1,3,2-benzodioxaphosphinine 2-oxide
-
IC50: 0.0015 mM
0.0014
2-heptyl-4H-1,3,2-benzodioxaphosphinine 2-oxide
-
IC50: 0.0014 mM
0.0016
2-heptyl-4H-1,3,2-benzodioxaphosphinine 2-oxide
-
IC50: 0.0016 mM
0.0062
acephate
-
IC50: 0.0062 mM
0.016
bis(1-methylethyl) 4-nitrophenyl phosphate
-
IC50: 0.016 mM
0.001386
chlorfenvinphos
-
IC50 at pH 7.4, 37C: 1386 nM
0.000021
chlorpyrifos
-
IC50: 0.000021 mM
0.000071
chlorpyrifos
-
IC50: 0.000071 mM
0.00035
chlorpyrifos cyclohexyl
-
IC50: 0.00035 mM
0.00086
chlorpyrifos cyclohexyl
-
IC50: 0.00086 mM
0.0033
chlorpyrifos isopropyl
-
IC50: 0.0033 mM
0.00008
chlorpyrifos methyl
-
IC50: 0.000080 mM
0.00031
chlorpyrifos methyl
-
IC50: 0.00031 mM
0.00006
chlorpyrifos n-butyl
-
IC50: 0.00006 mM
0.00007
chlorpyrifos n-propyl
-
IC50: 0.00007 mM
0.0000183
chlorpyrifos-methyl oxon
-
IC50 at pH 7.4, 37C: 18.3 nM
0.0000225
DFP
-
IC50 at pH 7.4, 37C: 22.5 nM
0.00089
diazoxon
-
IC50: 0.00089 mM
0.00093
diazoxon
-
IC50: 0.00093 mM
0.001386
diazoxon
-
IC50 at pH 7.4, 37C: 1386 nM
0.0001186
dichlorvos
-
IC50 at pH 7.4, 37C: 118.6 nM
0.00023
dichlorvos
-
IC50: 0.00023 mM
0.00056
dichlorvos
-
IC50: 0.00056 mM
0.0001
dicyclohexyl 2,2-dichloroethenyl phosphate
-
IC50: 0.00010 mM
0.00025
dicyclohexyl 2,2-dichloroethenyl phosphate
-
IC50: 0.00025 mM
0.002
diethyl 4-methyl-3-nitrophenyl phosphate
-
IC50: 0.002 mM
0.000011
diisopropylfluorophosphate
-
IC50: 0.000011 mM
0.000017
diisopropylfluorophosphate
-
IC50: 0.000017 mM
0.0000099
dipentyl fluorophosphate
-
IC50: 0.0000099 mM
0.000011
dipentyl fluorophosphate
-
IC50: 0.000011 mM
0.00024
diphenylphosphinic fluoride
-
IC50: 0.00024 mM
0.00041
diphenylphosphinic fluoride
-
IC50: 0.00041 mM
0.00011
ethyl octylphosphonofluoridoate
-
IC50: 0.00011 mM
0.00021
ethyl octylphosphonofluoridoate
-
IC50: 0.00021 mM
0.000027
heptyl ethylphosphonofluoridoate
-
IC50: 0.000027 mM
0.00023
heptyl ethylphosphonofluoridoate
-
IC50: 0.00023 mM
1.4
malaoxon
-
IC50 at pH 7.4, 37C: 1400000 nM
0.003013
Mipafox
-
IC50 at pH 7.4, 37C: 3013 nM
0.00037
naled
-
IC50: 0.00037 mM
0.00087
naled
-
IC50: 0.00087 mM
0.000052
nonyl ethylphosphonofluoridoate
-
IC50: 0.000052 mM
0.00028
nonyl ethylphosphonofluoridoate
-
IC50: 0.00028 mM
0.067
octane-1-sulfonyl fluoride
-
IC50: 0.067 mM
0.073
octane-1-sulfonyl fluoride
-
IC50: 0.073 mM
0.000043
octyl methylphosphonofluoridoate
-
IC50: 0.000043 mM
0.00016
octyl methylphosphonofluoridoate
-
IC50: 0.00016 mM
0.003805
Paraoxon
-
IC50 at pH 7.4, 37C: 3805 nM
0.0047
Paraoxon
-
IC50: 0.0047 mM
0.00013
pentyl ethylphosphonofluoridoate
-
IC50: 0.00013 mM
0.00027
pentyl ethylphosphonofluoridoate
-
IC50: 0.00027 mM
0.01
peptide SsCEI 2
-
pH 7.5, 37C
-
0.00000002
phosphatidylethanolamine-binding protein inhibitor SsCEI
Q7LX61
pH 7.5, 80C, substrate: N-acetyl-L-leucyl 4-nitroanilide
-
0.002
profenofos
-
IC50: 0.002 mM
0.018
Trichlorfon
-
IC50: 0.018 mM
0.00032
tridecyl methylphosphonofluoridoate
-
IC50: 0.00032 mM
0.0048
tridecyl methylphosphonofluoridoate
-
IC50: 0.0048 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.1
Q7LX61
pH 7.5, 80C
0.124
-
recombinant enzyme, after the induction with IPTG, at 8 h of culture in LB medium
0.172
-
recombinant enzyme, after the induction with IPTG, at 18 h of culture in TB medium
4.8
Q97VD6
pH 7.5, 90C
13
-
with Tyr-Leu as substrate
19
-
with Tyr-Phe as substrate
23
-
with Ala-p-nitroanilide as substrate
109.2
-
-
154
-
with Phe-p-nitroanilide as substrate
186
-
with Ala-beta-naphthylamide as substrate
1490
-
-
additional information
-
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8 - 5.5
-
at 85C
6
-
hydrolysis of N-acetyl-Glu p-nitroanilide
7
-
kinetic assay
7
-
heat activated enzyme
7
-
hydrolysis of N-acetyl-Met-Leu-Gly
7.2 - 7.6
-
-
7.2
-
activity assay
7.5 - 8
-
hydrolysis of N-acetyl-Ala p-nitroanilide
7.5 - 9
-
hydrolysis of formylmethionine-beta-naphthylamide or Met-Met-Leu-Phe
7.5 - 9
Q7LX61
at 80C
7.5
-
wild-type enzyme
7.5
-
hydrolysis of N-acetyl-Ala p-nitroanilide
7.5
-
-
8
-
activity assay
8
Q973W9
substrate: N-acetyl-Ala-Ala-Ala
8
-
potassium phosphate buffer
8.3
-
hydrolysis of N-acetyl-Ala p-nitroanilide
8.4
-
hydrolysis of N-acetyl-Ala p-nitroanilide
8.8
-
wild-type enzyme
9
-
the rate constants for the D524A and D524N variants increase to about pH 9
9
-
glycine buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
-
about 60% of maximal activity at pH 5 and pH 8
5.8 - 8.8
-
pH 5.8: about% of maximal activity, pH 8.8: about% of maximal activity
6 - 9.5
Q973W9
pH 6.0: about 65% of maximal activity, pH 9.5: about 70% of maximal activity
7 - 9
-
about 55% of maximal activity at pH 7 and at pH 13
7.5 - 8
Q97VD6
pH 7.5: about 55% of maximal activity, pH 8.0: about 75% of maximal activity
7.5 - 9.5
-
pH 7.5: about 50% of maximal activity, pH 9.5: about 65% of maximal activity, wild-type enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
activity assay
70
-
kinetic assay
70
Q973W9
substrate: N-acetyl-Ala-Ala-Ala
74
-
wild-type
75
-
truncated mutant of apAPH that lacks the first short alpha-helix at the N-terminal
77
-
mutant DELTAN21
80
-
activity assay
80
-
wild-type enzyme
90
-
wild-type enzyme
90
-
at pH 5.4
92
-
mutant D15A above 92; mutant R18A above 92
95
-
wild-type enzyme
95
-
heat-activated enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 80
-
60C: about 40% of maximal activity, 80C: optimum
80 - 95
Q97VD6
80C: about 65% of maximal activity, 95C: about 50% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
APH expression in Alzheimers disease brain is lower than in age-matched controls
Manually annotated by BRENDA team
-
mucosal epithelium
Manually annotated by BRENDA team
-
isolated from serum-free conditioned medium
Manually annotated by BRENDA team
-
isolated from serum-free conditioned medium
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
63030
-
-
727876
73230
-
calculated, monomer
696454
81300
-
ion-spray mass spectrometry
95272
125000
Q7LX61
gel filtration
720431
126100
-
calculated, dimer
699850
192000
Q97VD6
gel filtration
720867
230000 - 245000
-
gel filtration
95267
260000
-
heat-activated enzyme, light-scattering photometry
95261
280000
-
gel filtration
95259
280000
-
non-denaturing PAGE
95270
290000 - 320000
-
gel filtration
95251
300000
-
gel filtration
653037
300000
-
gel filtration
95253
300000
-
gel filtration
95263
320000 - 340000
-
gel filtration
29061
350000
Q84LM4
gel filtration
651807
350000
-
gel filtration
651807
360000
-
gel filtration
95254
423000
-
sucrose density gradient ultracentrifugation
95254
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
5 * or 6 * 75000, SDS-PAGE
?
-
x * 812665, calculation from nucleotide sequence
dimer
-
crystallography
dimer
-
symmetric homodimer with each subunit comprised of two domains. The N-terminal domain is a regular seven-propeller, while the C-terminal domain has a canonical alpha/beta hydrolase fold and includes the active site and a conserved Ser445-Asp524-His556 catalytic triad
hexamer
-
hexamers in the crystalline state are formed as trimers of dimers of the monomer enzyme. It is proposed that the mode of multimerization and self-assembly among oligopeptidases is finetuned by a shielding intent of a sticky-edge, insertions, and N- and C-terminal extensions, whereas to maintain the effectiveness of catalysis and selectivity, pliability of the His-loop and the position of the propeller blades are adjusted
hexamer
Pyrococcus horikoshii DSM 12428
-
hexamers in the crystalline state are formed as trimers of dimers of the monomer enzyme. It is proposed that the mode of multimerization and self-assembly among oligopeptidases is finetuned by a shielding intent of a sticky-edge, insertions, and N- and C-terminal extensions, whereas to maintain the effectiveness of catalysis and selectivity, pliability of the His-loop and the position of the propeller blades are adjusted
-
homodimer
-
-
homodimer
Q7LX61
2 * 60000, SDS-PAGE
homodimer
-
the monomer subunit is composed of one hydrolase and one propeller domain. In the homodimeric structures only one subunit displayed the closed form of the enzyme. The other subunit exhibits an open gate to the catalytic site, thus revealing the structural basis that controls the oligopeptidase activity
homodimer
Aeropyrum pernix DSM 11879
-
the monomer subunit is composed of one hydrolase and one propeller domain. In the homodimeric structures only one subunit displayed the closed form of the enzyme. The other subunit exhibits an open gate to the catalytic site, thus revealing the structural basis that controls the oligopeptidase activity
-
homodimer
-
2 * 60000, SDS-PAGE
-
tetramer
-
4 * 70000
tetramer
-
4 * 82000-84000, SDS-PAGE
tetramer
-
4 * 75000, SDS-PAGE
tetramer
-
4 * 75000, SDS-PAGE
tetramer
-
4 * 82000, SDS-PAGE
tetramer
Q84LM4
4 * 82000, SDS-PAGE
tetramer
-
4 * 76000, loss of native tetrameric structure upon citraconylation. This process is reversed at acidic pH. Involvement of all cysteines in disulfide bridges
trimer
-
3 * 76000-80000, SDS-PAGE
homotrimer
Q97VD6
3 * 64000, SDS-PAGE, 3 * 67000, calculated from sequence
additional information
-
structural investigations of the enzyme by mass spectrometric procedures
additional information
-
both monomeric and dimeric species are observed after 24 h dialysis of the enzyme denatured with guanidine-HCl. Both the monomeric and dimeric forms recovered after dialysis are active
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals grown at 17.8C using ammonium phosphate as a precipitant. Crystals belong to space group P1 with unit-cell parameters a = 107.5, b = 109.9, alpha = 108.1, beta = 109.8 and gamma = 91.9
-
crystals of the H367A mutant grown at 20C in hanging drops, to 2.2 A resolution. Belongs to space group P212121
-
hanging drop method, crystal structure determination of the native and two mutant structures (D524N and D524A)
-
hanging-drop vapor-diffusion method. The best crystals were obtained from reservoir of 6% PEG4000, 50 mM/l NaAc (pH 4.6), 15 mM/l DTT, 0.2 mM/l EDTA
-
by hanging drop method. AAP crystallized with the product-like inhibitors Ac-Phe and Gly-Phe, as well as with the substrate Abz-GFEPF(NO2)RA. Mutant S445A crystallized with Abz-GFEPF(NO2)RA. Complexes belong to P212121. Crystal structures of AAPinhibitor complexes reveal the oxyanion-binding site and the specificities of the S1, S2 and S3 subsites. Substrate-binding site extends beyond the S2 subsite, being capable of binding peptides with a longer N-terminus. The S2 subsite displays a non-polar character. The S3 site reveals a hydrophobic region that does not form hydrogen bonds with the inhibitor P3 residue. The enzymeinhibitor complexes reveal that, upon ligand-binding, the S1 subsite undergoes significant conformational changes
-
hanging-drop vapor diffusion method, 2.5 A resolution, space group: P2(1)2(1)2(1), unit cell parameters: a = 63.1 A, b = 102.3 A, c = 163.9 A, truncated mutant of apAPH that lacks the first short alpha-helix at the N-terminal is cloned and expressed in Escherichia coli
-
the crystal structure of the H367A variant of ApAAP is determined and refined to a resolution of 2.2 A
-
crystals are grown at 20C by the hanging drop method
-
crystallized in mother liquor containing 0.1 M TrisHCl pH 7.0, 10%(w/v) polyethylene glycol 8000, 50 mM MgCl2 and 1%(w/v) CHAPS using the hanging-drop vapour-diffusion technique, 3.4 A resolution, space group C222, unit-cell parameters a = 84.8 A, b = 421.1 A, c = 212.0 A, four molecules in the asymmetric unit
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
rapid loss of activity below
95253
5.4
-
0.25 M ammonium sulfate, stable for 6 weeks
95253
6 - 10
Q973W9
25C, 24 h, over 85% activity remaining
724738
6 - 8
-
stable
95253
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 100
-
the major conformation of the enzyme remains stable
95261
50
Q7LX61
72 h, stable
720431
70
Q7LX61
72 h, stable
720431
70
Q97VD6
24 h, 70% loss of activity. Slight increase its relative activity during the first 5 hours of incubation
720867
70
Q973W9
55 h, 70% of the activioty remains
724738
90
-
both the wild-type and the H367A mutant are stable up to 90C but tend to denature at higher temperature, more readily with the mutant. At lower temperature the wild-type has more flexible structural elements, particularly at 25C, but differences diminish with increase of temperature
688698
90
Q97VD6
4 h, 50% loss of activity
720867
90
Q973W9
half-life: 16 h
724738
95
-
24 h, stable
95261
additional information
-
coupling to CNBr-Sepharose and cross-linking with dimethylsuberimidate improve the thermal stability
95260
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
fully resistant to digestion by trypsin, chymotrypsin and elastase
-
loss of activity after freezing and lyophilization
-
stabilized in a 0.1 M solution of ammonium sulfate
-
unstable with organic solvents
-
coupling to CNBr-Sepharose and cross-linking with dimethylsuberimidate improves the thermal stability. This treatment also enhances resistance to inactivation by ionic detergent and the organic solvent N,N-dimethylformamide
-
75% loss of activity in 0.1 M guanidine hydrochloride at 37C after 200 min
-
complete loss of activity upon freezing or lyophilization in the presence of beta-mercaptoethanol. In the absence of thiol the enzyme loses 50% of its activity on lyophilization
-
1 M guanidine-HCl, activity is completely abolished. Dialysis results in 15-20% recovery of enzyme activity. In 1 M guanidine HCl the enzyme loses both its secondary and tertiary structures and dissociates into monomers of 70000 Da. Both monomeric and dimeric species are observed after 24 h dialysis of the enzyme denatured with guanidine-HCl. Both the monomer and dimer forms recovered after dialysis are active
-
8 M urea, 1 h, 25C, 85% loss of activity. Complete recovery on dialysis or 50fold dilution of the denatured enzyme. The enzyme lost its secondary structure at urea concentrations of 2 M and higher, whereas the tertiary structure is minimally perturbed below 4 M urea
-
loss of native tetrameric structure upon citraconylation. This process is reversed at acidic pH
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
guanidine-HCl
Q97VD6
1 M, complete loss of activity, after removal of guanidine-HCl the enzyme recovers 25% of its activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 0.05 mM sodium phosphate, pH 6.9, 2 mM MgCl2, 1 mM EDTA, stable over several months
-
-30C, 20% glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using Hi-Trap Q-Sepharose and HiLoad Sephacryl S-200 columns
-
APH isolated from COS-7 cells purified on a nickel column
-
by gel filtration, to homogeneity
-
by affinity chromatography, more than 95% pure
synthetic construct
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
expression in Escherichia coli of of chimeras of a carboxylesterase (EC 3.1.1.1) from Archaeoglobus fulgidus and an acylpeptide hydrolase (EC 3.4.19.1) from Aeropyrum pernix K1
-
a truncated mutant of apAPH that lacks the first short alpha-helix at the N-terminal is cloned and expressed in Escherichia coli
-
for expression in Escherichia coli BL21-CodonPlus DE3-RIL cells
-
into pET22b vector and transformed into Rozetta DE3 Escherichia coli strain
-
into the vector pET11a for expression in Escherichia coli BL21-CodonPlus DE3-RIL cells
-
expression in Escherichia coli as a functional enzyme
Q84LM4
expression in Escherichia coli as a functional enzyme
-
into the TOPO-V5/His tag mammalian expression vector. Wild-type and mutant APH constructs transfected into COS-7 or SK-N-MC cells
-
expression in Escherichia coli
-
into the vector pET15b for expression in Escherichia coli Rosetta DE3 cells
-
overexpression in Escherichia coli
-
pTrc-PMH overexpressed in Escherichia coli strain JM105
-
expression in Escherichia coli
Q973W9
expression of wild-type and mutant enzymes in Escherichia coli
-
plasmid containing full-length acylpeptide hydrolase used as template to generate pFLAG-CMV1 expression construct. This construct encodes amino acids 2-732 of acylpeptide hydrolase. For protein production, transfection into 293 cells
synthetic construct
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of apeh-3 is down-regulated as an immediate response to stress
Q97VD6
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D524A
-
the mutation affects the closed, active form of the enzyme, disrupting its catalytic triad. The wild-type enzyme exhibits a bell-shaped pH-rate profile (optimum at pH 7.5), whereas the rate constants for the D524A and D524N variants increase to about pH 9. The kcat/Km values is much lower compared with those of the wild-type enzyme
D524N
-
the mutation affects the closed, active form of the enzyme, disrupting its catalytic triad. The wild-type enzyme exhibits a bell-shaped pH-rate profile (optimum at pH 7.5), whereas the rate constants for the D524A and D524N variants increase to about pH 9. The kcat/Km values is much lower compared with those of the wild-type enzyme
F488G/R526V/T560W
-
1.55fold increase in activity with 4-nitrophenyl laurate compared to activity of mutant R526V/T560W
R526 I
-
the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 17.3fold higher than the wild-type ratio
R526A
-
the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 11.7fold higher than the wild-type ratio
R526E
-
the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 115.5fold higher than the wild-type ratio
R526K
-
the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 13.9fold higher than the wild-type ratio
R526L
-
the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 14.8fold higher than the wild-type ratio
R526V
-
the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 22.3fold higher than the wild-type ratio
R526V
-
mutant enzyme with high esterase activity, extreme thermal stability, and high tolerance to organic solvents
R526V/T560W
-
1.5fold increase in activity with 4-nitrophenyl dodecanoate compared to activity of mutant R526V
W474V/F488G/R526V/T560W
-
the mutant enzyme has 7fold higher catalytic efficiency (kcat/Km) for 4-nitrophenyl dodecanoate than the mutant enzyme R526V
W474V/R526V/T560W
-
3.11fold increase in activity with 4-nitrophenyl laurate compared to activity of mutant R526V/T560W
D524A
Aeropyrum pernix DSM 11879
-
the mutation affects the closed, active form of the enzyme, disrupting its catalytic triad. The wild-type enzyme exhibits a bell-shaped pH-rate profile (optimum at pH 7.5), whereas the rate constants for the D524A and D524N variants increase to about pH 9. The kcat/Km values is much lower compared with those of the wild-type enzyme
-
D524N
Aeropyrum pernix DSM 11879
-
the mutation affects the closed, active form of the enzyme, disrupting its catalytic triad. The wild-type enzyme exhibits a bell-shaped pH-rate profile (optimum at pH 7.5), whereas the rate constants for the D524A and D524N variants increase to about pH 9. The kcat/Km values is much lower compared with those of the wild-type enzyme
-
R526V
Aeropyrum pernix DSM 11879
-
mutant enzyme with high esterase activity, extreme thermal stability, and high tolerance to organic solvents
-
R526V/T560W
Aeropyrum pernix DSM 11879
-
1.5fold increase in activity with 4-nitrophenyl dodecanoate compared to activity of mutant R526V
-
W474V/R526V/T560W
Aeropyrum pernix DSM 11879
-
3.11fold increase in activity with 4-nitrophenyl laurate compared to activity of mutant R526V/T560W
-
D15A
-
mutant to determine the effects of the N-terminal region and the salt bridges on the stability and catalytic activity of apAPH
D15A/R18A
-
mutant to determine the effects of the N-terminal region and the salt bridges on the stability and catalytic activity of apAPH
DELTA1-21
-
optimal temperature of a truncated mutant of apAPH that lacks the first short alpha-helix at the N-terminal is decreased by 15C
DELTAN21
-
mutant, N-terminal helix deleted, no longer functional at the optimum temperature, 95C, for the wild-type enzyme, low thermodynamic stability
E88A
-
mutant, lower thermodynamic stability than the wild-type, broken inter-domain salt bridge, catalytic activity almost abolished
E88A/R526E
-
mutant, lower thermodynamic stability than the wild-type
E88A/R526K
-
mutant, lower thermodynamic stability than the wild-type, broken inter-domain salt bridge, positive charge at position 526, catalytic activity almost abolished
E88A/R526V
-
mutant, lower thermodynamic stability than the wild-type
E88D
-
mutant, lower thermodynamic stability than the wild-type
H367A
-
mutant, displays significantly reduced catalytic activity
R18A
-
mutant to determine the effects of the N-terminal region and the salt bridges on the stability and catalytic activity of apAPH
S445A
-
nearly inactive. Remaining activity of the mutant can cause cleavage in the peptide
S587A
-
mutated in the active site
A587S
-
no hydrolytic activity
N675S
-
no hydrolytic activity
Y707H
-
no hydrolytic activity
H367A
-
displays significantly reduced catalytic activity. Unlike the reaction of the wild-type, the reaction of the mutant displays completely linear temperature dependence. Its reaction is associated with unfavourable entropy of activation
additional information
-
construction of chimeras of a carboxylesterase (EC 3.1.1.1) from Archaeoglobus fulgidus and an acylpeptide hydrolase (EC 3.4.19.1) from Aeropyrum pernix K1. Their activities to hydrolyze 4-nitrophenyl esters (pNP) with different acyl chain lengths is explored. The chimeras inherit the thermophilic property of both parents. The substrate-binding domain is the dominant factor on enzyme substrate specificity, and the optimization of the newly formed domain interface is an important guarantee for successful domain swapping of proteins with low-sequence homology
additional information
-
the esterase activity of the mutant R526V (this mutation transforms a promiscuous acylaminoacyl peptidase into a specific carboxylesterase) towards substrates with long acyl chains is enhanced by protein engineering and solvent optimization. The substrate preference of the enzyme can be further changed from 4-nitrophenyl octanoate to 4-nitrophenyl dodecanoate by protein and solvent engineering
F488G/R526V/T560W
Aeropyrum pernix DSM 11879
-
1.55fold increase in activity with 4-nitrophenyl laurate compared to activity of mutant R526V/T560W
-
additional information
Aeropyrum pernix DSM 11879
-
the esterase activity of the mutant R526V (this mutation transforms a promiscuous acylaminoacyl peptidase into a specific carboxylesterase) towards substrates with long acyl chains is enhanced by protein engineering and solvent optimization. The substrate preference of the enzyme can be further changed from 4-nitrophenyl octanoate to 4-nitrophenyl dodecanoate by protein and solvent engineering
-
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
complete recovery of enzyme denatured with 8 M urea on dialysis or 50fold dilution. The enzyme loses its secondary structure at urea concentrations of 2 M and higher, whereas the tertiary structure is minimally perturbed below 4 M urea. Dialysis of the enzyme denatured with 1 M guanidine-HCl results in 15-20% recovery of enzyme activity. In 1 M guanidine HCl the enzyme loses both its secondary and tertiary structures and dissociates into monomers of 70000 Da. Both monomeric and dimeric species are observed after 24 h dialysis of the enzyme denatured with guanidine-HCl. Both the monomeric and dimeric forms recovered after dialysis are active
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
-
AAP displays both exo- and endopeptidase activities
medicine
-
blood acylpeptide hydrolase activity is a sensitive marker for exposure to some organophosphate toxicants
medicine
-
pharmaceutical target for the treatment of Alzheimers disease
medicine
-
reliable biomarker for some organophosphate pesticides that show higher specificity for acylpeptide hydrolase than for cholinesterases
medicine
-
blood acylpeptide hydrolase activity is a sensitive marker for exposure to some organophosphate toxicants
analysis
-
the enzyme is a tool in sequencing blocked peptides and proteins. Useful for unblocking acetylated proteins prior to protein sequence analysis
synthesis
-
the enzyme is a very useful tool for the synthesis and modification of peptides. The stabilized Sepharose-coupled form of the enzyme is used to couple a carboxy-methylated N-formyl amino acid or N-acetyl amino acid to a short pre-existing peptide
analysis
-
enzyme is useful for deblocking of peptides
medicine
Q7LX61
the enzyme may constitute a new therapeutic target for the treatment of a number of pathologies
medicine
-
the enzyme may constitute a new therapeutic target for the treatment of a number of pathologies
-
medicine
-
inhibition of acylpeptide hydrolase activity is related to cognitive improvement. Potential biomarker for organophosphate exposure in the screening for neurotoxicity. Possible participation of acylpeptide hydrolase in processes of synaptic plasticity. May play a predominant role in the control of presynaptic biopeptide concentrations that are contained in synaptic vesicles and released to the synaptic space exerting a neuromodular effect at a postsynaptic level
analysis
-
the enzyme may be useful for the removal of the N-terminal acylamino acid from some N-terminal blocked peptides and proteins in amino acid sequence analysis
additional information
-
amino acid sequence of PMH displays high similarity to that of the Streptomyces acyl-peptide hydrolase. PMH is an aminopeptidase carrying a putative catalytic triad, Ser511-Asp593-His625, with broad substrate specificity
additional information
Streptomyces morookaense JCM4673
-
amino acid sequence of PMH displays high similarity to that of the Streptomyces acyl-peptide hydrolase. PMH is an aminopeptidase carrying a putative catalytic triad, Ser511-Asp593-His625, with broad substrate specificity
-