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Information on EC 3.4.19.1 - acylaminoacyl-peptidase
for references in articles please use BRENDA:EC3.4.19.1
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.19 Omega peptidases
3.4.19.1 acylaminoacyl-peptidase
IUBMB Comments
This is a bifunctional serine protease that has exopeptidase activity against Nα-acylated peptides and endopeptidase activity against oxidized and glycated proteins. In its exopeptidase mode the enzyme cleaves an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide. This class of enzymes is evolutionary deeply conserved and is found in bacteria, archaea, animals and plants with different quartenary structures. In humans, malfunction is linked to different types of cancer and sarcoma cell viability. In peptidase family S9 (prolyl oligopeptidase family).
The enzyme appears in viruses and cellular organisms
- 3.4.19.1
- marrow
-
immunocytochemical
-
oligopeptidase
-
anti-alkaline
-
prolyl
-
immunophenotyping
-
hla-dr
-
smear
-
cryosta
-
phosphatase-anti-alkaline
-
cytospins
-
immunoenzymatic
-
moabs
-
aeropyrum
- pernix
- fluorophosphate
-
immunoenzyme
-
immunoalkaline
- medicine
- acylase
-
cytocentrifuge
- analysis
- drug development
- synthesis
- degradation
Reaction Schemes
showcleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
internal cleavage of oxidized and glycated proteins
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
AAH
-
-
-
-
AAP
AARE
acyl peptide enzyme hydrolase
Acyl-peptide hydrolase
-
-
-
-
acyl-peptide releasing enzyme
acylamino acid-releasing enzyme
acylamino-acid-releasing enzyme
-
-
-
-
acylaminoacyl peptidase
Acylaminoacyl-peptidase
acylpeptide hydrolase
alpha-N-acylpeptide hydrolase
-
-
-
-
ApAAP
APEH
apeH-2
APEH-3
APEH-3Ss
APE_1547.1
APH
DNF15S2 protein
-
-
-
-
N-acylaminoacyl-peptide hydrolase
-
-
-
-
N-acylpeptide hydrolase
-
-
-
-
N-formylmethionine (fMet) aminopeptidase
-
-
-
-
OPH
-
-
-
-
oxidized protein hydrolase
-
-
-
-
PhAAP
PM hydrolase
PMH
SpAAP
sso2141
SSO2693
ST0779
yuxL
Acylaminoacyl-peptidase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
internal cleavage of oxidized and glycated proteins
(2)
-
-
-
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
cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
(1)
-
-
-
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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
MetaCyc
Arg/N-end rule pathway (eukaryotic)
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CAS REGISTRY NUMBER
COMMENTARY
73562-30-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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-EALFQGPF(NO2)A + H2O
?
Substrates: very good substrate
Products: -
Products: -
?
2-aminobenzoyl-GFEPF(NO2)RA + H2O
?
Substrates: good substrate, displays greater kinetic specificity than acetyl-Phe-2-naphthylamide
Products: -
Products: -
?
2-aminobenzoyl-KARVLF(NO2)EA-Nle + H2O
?
Substrates: poor substrate
Products: -
Products: -
?
2-aminobenzoyl-RPIITTAGPSF(NO2)A + H2O
?
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-SAVLQSGF(NO2)A + H2O
?
Substrates: good substrate
Products: -
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?
2-naphthyl butyrate + H2O
2-naphthol + butanoate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
Substrates: -
Products: -
Products: -
?
Ac-Ala-4-nitroanilide + H2O
acetyl-Ala + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
Ac-Ala-7-amido-4-methylcoumarin + H2O
N-acetyl-L-Ala + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
Ac-Leu-4-nitroanilide + H2O
Ac-Leu + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
Ac-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
Ac-Phe-2-naphthylamide + H2O
N-acetyl-L-Phe + 2-naphthylamine
Substrates: -
Products: -
Products: -
?
Ac-Phe-4-nitroanilide + H2O
N-acetyl-L-Phe + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
acetyl-Ala-7-amido-4-methylcoumarin + H2O
?
Substrates: very slow hydrolysis
Products: -
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?
acetyl-Ala-7-amido-4-methylcoumarin + H2O
acetyl-Ala + 7-amino-4-methylcoumarin
-
Substrates: -
Products: -
Products: -
?
acetyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O
acetyl-Ala + Ala-Ala-Ala-Ala-Ala
AB009494
Substrates: -
Products: -
Products: -
?
acetyl-Ala-Met + H2O
acetyl-Ala + Met
-
Substrates: native enzyme shows 70.4% of the activity compared to acetyl-Ala-Ala as substrate
Products: -
Products: -
?
acetyl-Gly-Leu + H2O
acetyl-Gly + Leu
-
Substrates: native enzyme shows 30.3% of the activity compared to acetyl-Ala-Ala as substrate
Products: -
Products: -
?
acetyl-Met-7-amido-4-methylcoumarin + H2O
acetyl-Met + 7-amino-4-methylcoumarin
Substrates: -
Products: -
Products: -
?
acetyl-Met-Ala-Ala-Ala-Ala-Ala + H2O
acetyl-Met + Ala-Ala-Ala-Ala-Ala
AB009494
Substrates: -
Products: -
Products: -
?
acetyl-Met-Asn + H2O
acetyl-Met + Asn
-
Substrates: native enzyme shows 34.1% of the activity compared to acetyl-Ala-Ala as substrate
Products: -
Products: -
?
acetyl-Met-Phe + H2O
acetyl-Met + Phe
Substrates: native enzyme shows 5% of the activity compared to acetyl-Ala-Ala as substrate
Products: -
Products: -
?
acetyl-Phe-2-naphthylamide + H2O
?
Substrates: classical substrate of AAP
Products: -
Products: -
?
acetyl-Phe-2-naphthylamide + H2O
acetyl-Phe + 2-naphthylamine
Substrates: -
Products: -
Products: -
?
acetyl-Phe-4-nitroanilide + H2O
acetyl-Phe + 4-nitroaniline
Substrates: specificity rate constant is lower by one order of magnitude for acetyl-Leu-4-nitroanilide than for acetyl-Phe-4-nitroanilide
Products: -
Products: -
?
acetyl-Tyr-4-nitroanilide + H2O
acetyl-Tyr + 4-nitroaniline
AB009494
Substrates: -
Products: -
Products: -
?
Ala-p-nitroanilide + H2O
Ala + p-nitroaniline
-
Substrates: prefered substrate for PMH
Products: -
Products: -
?
formyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala-Ala-Ala-Ala
AB009494
Substrates: -
Products: -
Products: -
?
formyl-Gly-Val + H2O
formyl-Gly + Val
-
Substrates: native enzyme shows 30.3% of the activity compared to acetyl-Ala-Ala as substrate
Products: -
Products: -
?
formyl-Met-Ala + H2O
formyl-Met + Ala
AB009494
Substrates: -
Products: -
Products: -
?
formyl-Met-Ala-Ala-Ala-Ala-Ala + H2O
formyl-Met + Ala-Ala-Ala-Ala-Ala
AB009494
Substrates: -
Products: -
Products: -
?
formyl-Met-Ala-Ser + H2O
formyl-Met + Ala-Ser
AB009494
Substrates: -
Products: -
Products: -
?
formyl-Met-Leu-Gly + H2O
formyl-Met + Leu-Gly
AB009494
Substrates: -
Products: -
Products: -
?
formylmethionine p-nitroanilide + H2O
formylmethionine + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
formylmethionine-beta-naphthylamide + H2O
formylmethionine + beta-naphthylamine
-
Substrates: -
Products: -
Products: -
?
formylmethionine-Leu + H2O
formylmethionine + Leu
-
Substrates: -
Products: -
Products: -
?
formylmethionine-Phe + H2O
formylmethionine + Phe
-
Substrates: -
Products: -
Products: -
?
formylmethionine-Trp + H2O
formylmethionine + Trp
-
Substrates: -
Products: -
Products: -
?
formylmethionine-Val + H2O
formylmethionine + Val
-
Substrates: -
Products: -
Products: -
?
glutaryl-GGF-7-amido-4-methylcoumarin + H2O
?
Substrates: has a rate constant comparable to that of acetyl-Phe-2-naphthylamide
Products: -
Products: -
?
Gly-Phe-2-naphthylamide + H2O
Gly-Phe + 2-naphthylamine
Substrates: -
Products: -
Products: -
?
glycated ribulose-1,5-diphosphate carboxylase/oxygenase protein + H2O
?
-
Substrates: no degradation of the native protein
Products: -
Products: -
?
N-acetyl-Ala ethyl ester + H2O
N-acetyl-Ala + ethanol
-
Substrates: -
Products: -
Products: -
?
N-acetyl-Ala-Ala-Arg-Gly + H2O
N-acetyl-Ala + Ala-Arg-Gly
-
Substrates: -
Products: -
Products: -
?
N-acetyl-Ala-Ala-Gln-Nepsilon-acetyl-Lys + H2O
?
-
Substrates: -
Products: -
Products: -
?
N-acetyl-Ala-Ala-Gln-Nepsilon-succinyl-Lys + H2O
?
-
Substrates: -
Products: -
Products: -
?
N-acetyl-Ala-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu + H2O
?
-
Substrates: -
Products: -
Products: -
?
N-acetyl-Ala-Ala-Phe-Gly + H2O
N-acetyl-Ala + Ala-Phe-Gly
-
Substrates: -
Products: -
Products: -
?
N-acetyl-Ala-Ala-Pro-Ala + H2O
N-acetyl-Ala + Ala-Pro-Ala
-
Substrates: -
Products: -
Products: -
?
N-acetyl-Ala-beta-naphthylamide + H2O
N-acetyl-Ala + beta-naphthylamine
-
Substrates: -
Products: -
Products: -
?
N-acetyl-alanyl-4-nitroanilide + H2O
N-acetyl-L-Ala + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
N-acetyl-Glu p-nitroanilide + H2O
N-acetyl-Glu + p-nitroaniline
-
Substrates: -
Products: -
Products: -
?
N-acetyl-Gly-Ala + H2O
N-acetyl-Gly + Ala
-
Substrates: weak activity
Products: -
Products: -
?
N-acetyl-L-alanine 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
N-acetyl-L-Met-alpha-L-Lys-Ala-NH2 + H2O
N-acetyl-L-Met + L-Lys-Ala-NH2
-
Substrates: -
Products: -
Products: -
?
N-acetyl-L-Met-epsilon-L-Lys-Ala-NH2 + H2O
N-acetyl-L-Met + L-Lys-L-Ala-NH2
-
Substrates: -
Products: -
Products: -
?
N-acetyl-L-Phe-4-nitroanilide + H2O
N-acetyl-L-Phe + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
N-acetyl-Leu-4-nitroanilide + H2O
N-acetyl-Leu + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
N-acetyl-Leu-p-nitroanilide + H2O
N-acetyl-Leu + p-nitroaniline
Substrates: 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
Products: -
Products: -
?
N-acetyl-Met-Ala-Gly-Gly-Asp-Ala-Ser-Gly-Glu + H2O
?
-
Substrates: -
Products: -
Products: -
?
N-acetyl-Met-Asp-Glu-Thr-Gly-Asp-Thr-Ala-Leu-Val-Ala + H2O
?
-
Substrates: -
Products: -
Products: -
?
N-acetyl-Phe-2-naphthylamide + H2O
N-acetyl-L-Phe + 2-naphthylamine
Substrates: kinetic assay
Products: -
Products: -
?
N-acetyl-Phe-Ala + H2O
N-acetyl-Phe + Ala
-
Substrates: weak activity
Products: -
Products: -
?
N-acetyl-Tyr-Ala + H2O
N-acetyl-Tyr + Ala
-
Substrates: weak activity
Products: -
Products: -
?
N-acylpeptide + H2O
?
-
Substrates: 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
Products: -
Products: -
?
p-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl caprylate + H2O
nitrophenol + caprylate
Substrates: 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
Products: -
Products: -
?
p-nitrophenyl hexanoate + H2O
p-nitrophenol + hexanoate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl propionate + H2O
p-nitrophenol + propionate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl valerate + H2O
p-nitrophenol + pentanoate
-
Substrates: -
Products: -
Products: -
?
Phe-p-nitroanilide + H2O
Phe + p-nitroaniline
-
Substrates: prefered substrate for PMH
Products: -
Products: -
?
Pro-beta-naphthylamide + H2O
Pro + 2-naphthylamine
-
Substrates: -
Products: -
Products: -
?
succinyl-AAA-4-nitroanilide + H2O
succinyl-AAA + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
succinyl-AAPF-2-naphthylamide + H2O
?
Substrates: hydrolysed at a significantly slower rate than acetyl-Phe-2-naphthylamide
Products: -
Products: -
?
succinyl-GGF-4-nitroanilide + H2O
succinyl-GGF + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
Z-GGL-4-nitroanilide + H2O
Z-GGL + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala + H2O
2-aminobenzoyl-Ala-Leu-Phe + Gln-Gly-Pro-Phe(NO2)-Ala
Substrates: endopeptidase activity
Products: -
Products: -
?
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala + H2O
2-aminobenzoyl-Ala-Leu-Phe + Gln-Gly-Pro-Phe(NO2)-Ala
Substrates: endopeptidase activity
Products: -
Products: -
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
Aeropyrum pernix ATCC 700893
Substrates: -
Products: -
Products: -
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
Aeropyrum pernix JCM 9820
Substrates: -
Products: -
Products: -
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
Aeropyrum pernix NBRC 100138
Substrates: -
Products: -
Products: -
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
Substrates: -
Products: -
Products: -
?
Ac-Ala-Ala + H2O
Ac-Ala + Ala
Substrates: -
Products: -
Products: -
?
Ac-Ala-Ala + H2O
Ac-Ala + Ala
Substrates: -
Products: -
Products: -
?
Ac-Ala-Ala + H2O
Ac-Ala + Ala
Substrates: -
Products: -
Products: -
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
Substrates: -
Products: -
Products: -
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
Substrates: high activity
Products: -
Products: -
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
Substrates: high activity
Products: -
Products: -
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
Substrates: high activity
Products: -
Products: -
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
Substrates: high activity
Products: -
Products: -
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
Substrates: high activity
Products: -
Products: -
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
Substrates: -
Products: -
Products: -
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
Aeropyrum pernix ATCC 700893
Substrates: -
Products: -
Products: -
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
Substrates: -
Products: -
Products: -
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
Aeropyrum pernix NBRC 100138
Substrates: -
Products: -
Products: -
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
Substrates: -
Products: -
Products: -
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
Substrates: -
Products: -
Products: -
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
Substrates: -
Products: -
Products: -
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
Substrates: -
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Products: -
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
Substrates: -
Products: -
Products: -
?
Ac-Leu-p-nitroanilide + H2O
Ac-Leu + p-nitroaniline
Substrates: substrate peptidase assay
Products: -
Products: -
?
Ac-Leu-p-nitroanilide + H2O
Ac-Leu + p-nitroaniline
-
Substrates: substrate peptidase assay
Products: -
Products: -
?
acetyl-Ala-4-nitroanilide + H2O
acetyl-Ala + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
acetyl-Ala-4-nitroanilide + H2O
acetyl-Ala + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
acetyl-Ala-4-nitroanilide + H2O
acetyl-Ala + 4-nitroaniline
AB009494
Substrates: the enzyme releases acetyl-Leu better than acetyl-Ala from acetyl-amino acid-4-nitroanilides
Products: -
Products: -
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acetyl-Ala-4-nitroanilide + H2O
acetyl-Ala + 4-nitroaniline
Substrates: the activity of the cold-active acylaminoacyl peptidase relies on its dimerization by domain swapping
Products: -
Products: -
?
acetyl-Ala-4-nitroanilide + H2O
acetyl-Ala + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
acetyl-Ala-4-nitroanilide + H2O
acetyl-Ala + 4-nitroaniline
Substrates: cryo-EM structure of acylpeptide hydrolase reveals substrate selection by multimerization and a multistate serine-protease triad
Products: -
Products: -
?
acetyl-Ala-4-nitroanilide + H2O
acetyl-Ala + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
acetyl-Ala-4-nitroanilide + H2O
acetyl-Ala + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
acetyl-Ala-Ala + H2O
acetyl-Ala + Ala
Substrates: -
Products: -
Products: -
?
acetyl-Ala-Ala + H2O
acetyl-Ala + Ala
AB009494
Substrates: -
Products: -
Products: -
?
Acetyl-Ala-Ala-Ala + H2O
Acetyl-Ala + Ala-Ala
Substrates: native enzyme shows 81% of the activity compared to acetyl-Ala-Ala as substrate
Products: -
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Acetyl-Ala-Ala-Ala + H2O
Acetyl-Ala + Ala-Ala
-
Substrates: native enzyme shows 147% of the activity compared to acetyl-Ala-Ala as substrate
Products: -
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?
acetyl-Ala-Ala-Ala-Ala + H2O
acetyl-Ala + Ala-Ala-Ala
Substrates: native enzyme shows 126% of the activity compared to acetyl-Ala-Ala as substrate
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acetyl-Ala-Ala-Ala-Ala + H2O
acetyl-Ala + Ala-Ala-Ala
-
Substrates: native enzyme shows 85.6% of the activity compared to acetyl-Ala-Ala as substrate
Products: -
Products: -
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acetyl-Ala-Ala-Ala-Ala + H2O
acetyl-Ala + Ala-Ala-Ala
AB009494
Substrates: -
Products: -
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acetyl-Gly-Gly + H2O
acetyl-Gly + Gly
Substrates: native enzyme shows 4% of the activity compared to acetyl-Ala-Ala as substrate
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acetyl-Gly-Gly + H2O
acetyl-Gly + Gly
-
Substrates: native enzyme shows 37% of the activity compared to acetyl-Ala-Ala as substrate
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acetyl-Leu-4-nitroanilide + H2O
acetyl-Leu + 4-nitroaniline
Substrates: 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-Leu-4-nitroanilide + H2O
acetyl-Leu + 4-nitroaniline
AB009494
Substrates: the enzyme releases acetyl-Leu better than acetyl-Ala from acetyl-amino acid-4-nitroanilides
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acetyl-Leu-4-nitroanilide + H2O
acetyl-Leu + 4-nitroaniline
Substrates: -
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acetyl-Met-Ala + H2O
acetyl-Met + Ala
Substrates: native enzyme shows 45% of the activity compared to acetyl-Ala-Ala as substrate
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acetyl-Met-Ala + H2O
acetyl-Met + Ala
-
Substrates: native enzyme shows 4% of the activity compared to acetyl-Ala-Ala as substrate
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acetyl-Met-Ala + H2O
acetyl-Met + Ala
AB009494
Substrates: -
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acetyl-Met-Glu + H2O
acetyl-Met + Glu
Substrates: native enzyme shows 6% of the activity compared to acetyl-Ala-Ala as substrate
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acetyl-Met-Glu + H2O
acetyl-Met + Glu
-
Substrates: native enzyme shows 4.3% of the activity compared to acetyl-Ala-Ala as substrate
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Ala-Ala-Ala-Ala + H2O
Ala + Ala-Ala-Ala
Substrates: -
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Ala-Ala-Ala-Ala + H2O
Ala + Ala-Ala-Ala
Substrates: -
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Ala-beta-naphthylamide + H2O
Ala + 2-naphthylamine
-
Substrates: -
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Ala-beta-naphthylamide + H2O
Ala + 2-naphthylamine
-
Substrates: -
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butyryl-Ala-Ala-Ala + H2O
butyryl-Ala + Ala-Ala
Substrates: native enzyme shows 77% of the activity compared to acetyl-Ala-Ala as substrate
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butyryl-Ala-Ala-Ala + H2O
butyryl-Ala + Ala-Ala
-
Substrates: native enzyme shows 33.6% of the activity compared to acetyl-Ala-Ala as substrate
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formyl-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala
Substrates: native enzyme shows 81% of the activity compared to acetyl-Ala-Ala as substrate
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formyl-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala
-
Substrates: native enzyme shows 62.4% of the activity compared to acetyl-Ala-Ala as substrate
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formyl-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala
AB009494
Substrates: -
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formyl-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala
Substrates: -
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Leu-beta-naphthylamide + H2O
Leu + 2-naphthylamine
-
Substrates: -
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Leu-beta-naphthylamide + H2O
Leu + 2-naphthylamine
-
Substrates: -
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N-acetyl-Ala p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
-
Substrates: -
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N-acetyl-Ala p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
-
Substrates: -
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N-acetyl-Ala p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
-
Substrates: -
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N-acetyl-Ala p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
-
Substrates: -
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N-acetyl-Ala-Ala + H2O
N-acetyl-Ala + Ala
-
Substrates: N-acetyl-Ala-Ala
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N-acetyl-Ala-Ala + H2O
N-acetyl-Ala + Ala
Substrates: -
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N-acetyl-Ala-Ala + H2O
N-acetyl-Ala + Ala
Substrates: -
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N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
-
Substrates: N-acetyl-Ala-Ala-Ala
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N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
-
Substrates: -
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N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
-
Substrates: -
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N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
Substrates: -
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N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
Substrates: -
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N-acetyl-Ala-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala-Ala
-
Substrates: -
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N-acetyl-Ala-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala-Ala
-
Substrates: -
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N-acetyl-Ala-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala-Ala
-
Substrates: -
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N-acetyl-Ala-p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
Substrates: substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Met-p-nitranilide, N-acetyl-Gly-p-nitranilide
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N-acetyl-Ala-p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
-
Substrates: substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Gly-p-nitranilide, N-acetyl-Met-p-nitranilide
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N-acetyl-Ala-p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
-
Substrates: -
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N-acetyl-Gly-p-nitroanilide + H2O
N-acetyl-Gly + p-nitroaniline
Substrates: substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Met-p-nitranilide, N-acetyl-Gly-p-nitranilide
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N-acetyl-Gly-p-nitroanilide + H2O
N-acetyl-Gly + p-nitroaniline
-
Substrates: substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Gly-p-nitranilide, N-acetyl-Met-p-nitranilide
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N-acetyl-L-Ala-4-nitroanilide + H2O
N-acetyl-L-Ala + 4-nitroaniline
Substrates: -
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N-acetyl-L-Ala-4-nitroanilide + H2O
N-acetyl-L-Ala + 4-nitroaniline
Substrates: -
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N-acetyl-L-alanyl 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
Substrates: -
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N-acetyl-L-alanyl 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
Substrates: -
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N-acetyl-L-alanyl 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
Substrates: -
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N-acetyl-L-alanyl 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
Substrates: -
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N-acetyl-L-alanyl-p-nitroanilide + H2O
N-acetyl-L-alanine + p-nitroaniline
-
Substrates: -
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N-acetyl-L-alanyl-p-nitroanilide + H2O
N-acetyl-L-alanine + p-nitroaniline
-
Substrates: -
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N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
Substrates: -
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N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
Aeropyrum pernix ATCC 700893
Substrates: -
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N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
Substrates: -
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N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
Aeropyrum pernix JCM 9820
Substrates: -
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N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
Aeropyrum pernix NBRC 100138
Substrates: -
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N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
Substrates: -
Products: -
Products: -
?
N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
Substrates: -
Products: -
Products: -
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N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
Substrates: -
Products: -
Products: -
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N-acetyl-L-leucyl 4-nitroanilide + H2O
N-acetyl-L-leucine + 4-nitroaniline
Substrates: preference for N-acetyl-L-leucyl 4-nitroanilide over N-acetyl-L-alanyl 4-nitroanilide
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N-acetyl-L-leucyl 4-nitroanilide + H2O
N-acetyl-L-leucine + 4-nitroaniline
Substrates: -
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Products: -
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N-acetyl-L-leucyl 4-nitroanilide + H2O
N-acetyl-L-leucine + 4-nitroaniline
Substrates: preference for N-acetyl-L-leucyl 4-nitroanilide over N-acetyl-L-alanyl 4-nitroanilide
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N-acetyl-L-leucyl 4-nitroanilide + H2O
N-acetyl-L-leucine + 4-nitroaniline
Substrates: -
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N-acetyl-L-phenylalanyl 4-nitroanilide + H2O
N-acetyl-L-phenylalanine + 4-nitroaniline
Substrates: -
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N-acetyl-L-phenylalanyl 4-nitroanilide + H2O
N-acetyl-L-phenylalanine + 4-nitroaniline
Substrates: -
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N-acetyl-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
Substrates: switch of substrate specificity of hyperthermophilic promiscuous acylaminoacyl peptidase by combination of protein and solvent engineering into a specific carboxylesterase
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N-acetyl-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
Substrates: switch of substrate specificity of hyperthermophilic promiscuous acylaminoacyl peptidase by combination of protein and solvent engineering into a specific carboxylesterase
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N-acetyl-Met-p-nitroanilide + H2O
N-acetyl-Met + p-nitroaniline
Substrates: substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Met-p-nitranilide, N-acetyl-Gly-p-nitranilide
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N-acetyl-Met-p-nitroanilide + H2O
N-acetyl-Met + p-nitroaniline
-
Substrates: substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Gly-p-nitranilide, N-acetyl-Met-p-nitranilide
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N-acetyl-Phe-2-naphthylamide + H2O
N-acetyl-Phe + 2-naphthylamine
Substrates: -
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N-acetyl-Phe-2-naphthylamide + H2O
N-acetyl-Phe + 2-naphthylamine
Substrates: -
Products: -
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?
Phe-beta-naphthylamide + H2O
Phe + 2-naphthylamine
-
Substrates: -
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Phe-beta-naphthylamide + H2O
Phe + 2-naphthylamine
-
Substrates: -
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Tyr-beta-naphthylamide + H2O
Tyr + 2-naphthylamine
-
Substrates: -
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?
Tyr-beta-naphthylamide + H2O
Tyr + 2-naphthylamine
-
Substrates: -
Products: -
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additional information
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Substrates: 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
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additional information
?
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Substrates: the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview
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additional information
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Substrates: the enzyme is also active with fatty acid esters, e.g. with 4-nitrophenyl caprylate. Substrate binding mechanism analysis, and random acceleration and steered molecular dynamics simulations of ligands unbinding pathways from APH. 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. Overview
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additional information
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Substrates: acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments
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additional information
?
-
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Substrates: acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments
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additional information
?
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Substrates: enzyme APH catalyzes the N-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids
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additional information
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Aeropyrum pernix ATCC 700893
Substrates: the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview
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additional information
?
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Aeropyrum pernix ATCC 700893
Substrates: acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments
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additional information
?
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Substrates: 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
Products: -
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additional information
?
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Substrates: the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview
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additional information
?
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Substrates: acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments
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additional information
?
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Aeropyrum pernix JCM 9820
Substrates: the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview
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additional information
?
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Aeropyrum pernix JCM 9820
Substrates: acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments
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additional information
?
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Substrates: removal of an N-acylated amino acid from blocked peptides
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additional information
?
-
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Substrates: removal of an N-acylated amino acid from blocked peptides
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additional information
?
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Substrates: removal of an N-acylated amino acid from blocked peptides
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additional information
?
-
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Substrates: removal of an N-acylated amino acid from blocked peptides
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additional information
?
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Aeropyrum pernix NBRC 100138
Substrates: the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview
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additional information
?
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Aeropyrum pernix NBRC 100138
Substrates: acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments
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additional information
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Substrates: the acylaminoacyl peptidase from Bacillus subtilis strain 168 catalyzes the removal of an acylated amino acid from Nalpha-acylpeptides, but it also catalyzes the aldol reaction with high enantioselectivity providing optically active secondary alcohols with satisfying enantioselectivity of 84.6% enantiomeric excess
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additional information
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Substrates: the acylaminoacyl peptidase from Bacillus subtilis strain 168 catalyzes the removal of an acylated amino acid from Nalpha-acylpeptides, but it also catalyzes the aldol reaction with high enantioselectivity providing optically active secondary alcohols with satisfying enantioselectivity of 84.6% enantiomeric excess
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additional information
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Substrates: the trypsin-modified enzyme is able to unblock alphaA-crystallin and displays endoprotease activity unlike the native enzyme
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additional information
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Substrates: the enzyme might be involved in not only catalysis of the N-terminal hydrolysis of Nalpha-acylpeptides but also the elimination of glycated proteins
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additional information
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Substrates: the enzyme may be involved in N-terminal deacylation of nascent polypeptide chains and of bioactive peptides
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additional information
?
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Substrates: APEH interacts with the amino-terminal domain of XRCC1
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additional information
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Substrates: APEH interacts with the amino-terminal domain of XRCC1
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additional information
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Substrates: acylpeptide hydrolase (APEH) deacetylates N-alpha-acetylated peptides and selectively degrades oxidised protein
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additional information
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Substrates: acylpeptide hydrolase (APEH) deacetylates N-alpha-acetylated peptides and selectively degrades oxidised protein
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
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additional information
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Substrates: cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
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additional information
?
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AB009494
Substrates: high hydrolytic activity for acylpeptides, no hydrolytic activity for Leu-4-nitroanilide and Ala-4-nitroanilide
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additional information
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Substrates: high hydrolytic activity for acylpeptides, no hydrolytic activity for Leu-4-nitroanilide and Ala-4-nitroanilide
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additional information
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Substrates: specific for N-terminal acylmethionine residues
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additional information
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Substrates: 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
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additional information
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Substrates: 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
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additional information
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Substrates: no activity with L-leucyl 4-nitroanilide, L-alanyl 4-nitroanilide or L-phenylalanyl 4-nitroanilide. The enzyme also shows endopeptidase activity
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additional information
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Substrates: no activity with L-leucyl 4-nitroanilide, L-alanyl 4-nitroanilide or L-phenylalanyl 4-nitroanilide. The enzyme also shows endopeptidase activity
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additional information
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Substrates: no activity with L-Leu-4-nitroanilide, L-Ala-4-nitroanilide, or L-Phe-4-nitroanilide, succinyl-AAPF-4-nitroanilide, and succinyl-AAVA-4-nitroanilide
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additional information
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Substrates: no activity with L-Leu-4-nitroanilide, L-Ala-4-nitroanilide, or L-Phe-4-nitroanilide, succinyl-AAPF-4-nitroanilide, and succinyl-AAVA-4-nitroanilide
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additional information
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Substrates: 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
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additional information
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Substrates: no activity with L-leucyl 4-nitroanilide, L-alanyl 4-nitroanilide or L-phenylalanyl 4-nitroanilide. The enzyme also shows endopeptidase activity
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additional information
?
-
Substrates: promiscuous activity of the ST0779 mutant in aldol addition, overview. ST0779 displays superior catalytic efficiency kcat/Km (6-8fold higher) and enantioselectivity with enantiomeric excess of 90-99% compared to porcine pancreatic lipase. The catalytic versatility of ST0779 is validated as the enzyme displays activity towards a broad scope of substituted benzaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the NH2-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids, but it also exhibits esterase activity and catalyzes the aldol reaction between acetone and 4-nitrobenzaldehyde. Comparison of kinetic parameters of ST0779- and porcine pancreatic lipase (PPL)-mediated aldol reaction between acetone and 4-nitrobenzaldehyde, catalytic reaction mechanism, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme catalyzes the NH2-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids, but it also exhibits esterase activity and catalyzes the aldol reaction between acetone and 4-nitrobenzaldehyde. Comparison of kinetic parameters of ST0779- and porcine pancreatic lipase (PPL)-mediated aldol reaction between acetone and 4-nitrobenzaldehyde, catalytic reaction mechanism, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition
Products: -
Products: -
?
additional information
?
-
Substrates: promiscuous activity of the ST0779 mutant in aldol addition, overview. ST0779 displays superior catalytic efficiency kcat/Km (6-8fold higher) and enantioselectivity with enantiomeric excess of 90-99% compared to porcine pancreatic lipase. The catalytic versatility of ST0779 is validated as the enzyme displays activity towards a broad scope of substituted benzaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the NH2-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids, but it also exhibits esterase activity and catalyzes the aldol reaction between acetone and 4-nitrobenzaldehyde. Comparison of kinetic parameters of ST0779- and porcine pancreatic lipase (PPL)-mediated aldol reaction between acetone and 4-nitrobenzaldehyde, catalytic reaction mechanism, overview
Products: -
Products: -
?
additional information
?
-
Substrates: promiscuous activity of the ST0779 mutant in aldol addition, overview. ST0779 displays superior catalytic efficiency kcat/Km (6-8fold higher) and enantioselectivity with enantiomeric excess of 90-99% compared to porcine pancreatic lipase. The catalytic versatility of ST0779 is validated as the enzyme displays activity towards a broad scope of substituted benzaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition
Products: -
Products: -
?
additional information
?
-
Substrates: promiscuous activity of the ST0779 mutant in aldol addition, overview. ST0779 displays superior catalytic efficiency kcat/Km (6-8fold higher) and enantioselectivity with enantiomeric excess of 90-99% compared to porcine pancreatic lipase. The catalytic versatility of ST0779 is validated as the enzyme displays activity towards a broad scope of substituted benzaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme catalyzes the NH2-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids, but it also exhibits esterase activity and catalyzes the aldol reaction between acetone and 4-nitrobenzaldehyde. Comparison of kinetic parameters of ST0779- and porcine pancreatic lipase (PPL)-mediated aldol reaction between acetone and 4-nitrobenzaldehyde, catalytic reaction mechanism, overview
Products: -
Products: -
?
additional information
?
-
Substrates: the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition
Products: -
Products: -
?
additional information
?
-
Substrates: promiscuous activity of the ST0779 mutant in aldol addition, overview. ST0779 displays superior catalytic efficiency kcat/Km (6-8fold higher) and enantioselectivity with enantiomeric excess of 90-99% compared to porcine pancreatic lipase. The catalytic versatility of ST0779 is validated as the enzyme displays activity towards a broad scope of substituted benzaldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition
Products: -
Products: -
?
additional information
?
-
-
Substrates: peptidase activity is only exerted on peptides with Gly or Ala at their N-termini
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme may be involved in regulation of neuropeptide turnover
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: His507 of acylaminoacyl peptidase stabilizes the active site conformation, not the catalytic intermediate
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzes the NH2-terminal hydrolysis of N-acylpeptides to release N-acylated amino acids
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Substrates: removal of an N-acylated amino acid from blocked peptides
Products: -
Products: -
?
additional information
?
-
-
Substrates: removal of an N-acylated amino acid from blocked peptides
Products: -
Products: -
?
additional information
?
-
Substrates: removal of an N-acylated amino acid from blocked peptides
Products: -
Products: -
?
additional information
?
-
-
Substrates: removal of an N-acylated amino acid from blocked peptides
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme might be involved in not only catalysis of the N-terminal hydrolysis of Nalpha-acylpeptides but also the elimination of glycated proteins
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme may be involved in N-terminal deacylation of nascent polypeptide chains and of bioactive peptides
Products: -
Products: -
?
additional information
?
-
Substrates: APEH interacts with the amino-terminal domain of XRCC1
Products: -
Products: -
?
additional information
?
-
-
Substrates: APEH interacts with the amino-terminal domain of XRCC1
Products: -
Products: -
?
additional information
?
-
Substrates: cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
Products: -
Products: -
?
additional information
?
-
-
Substrates: cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme may be involved in regulation of neuropeptide turnover
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzes the NH2-terminal hydrolysis of N-acylpeptides to release N-acylated amino acids
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cl-
SCN-
-
0.1-0.5 M, activates towards N-acetyl-Ala p-nitroanilide and N-acetyl-Ala beta-naphthylamide
Cl-
-
0.1-0.5 M, activates activity towards N-acetyl-Ala p-nitroanilide and N-acetyl-Ala beta-naphthylamide
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(10E,12Z)-octadeca-10,12-dienoic acid
-
non-competitive inhibition mechanism
15-deoxy-DELTA12,14-prostaglandin J2
0.1 mM, inhibition to 44.5% of control, HeLa lysate
15-oxo-11Z,13E-eicosadienoate
0.1 mM, inhibition to 50.7% of control, HeLa lysate. 0.1 mM, inhibition to 29.5% of control, purified enzyme
-
24-hydroxycholesterol
0.1 mM, inhibition to 65.2% of control, HeLa lysate. 0.1 mM, inhibition to 68.8% of control, purified enzyme
4-hydroxyphenyl 4-methoxyphenyl (1-acetamidoethyl)phosphonate
-
0.25 or 0.05 mM, 34% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol); 0.25 or 0.05 mM, 99% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
7-ketocholesterol
0.1 mM, inhibition to 59.8% of control, HeLa lysate. 0.1 mM, inhibition to 51.4% of control, purified enzyme
9-oxo-10E,12Z-octadecadienoic acid
0.1 mM, inhibition to 45-5% of control, HeLa lysate. 0.1 mM, inhibition to 19.7% of control, purified enzyme
acetyl-Gly-prolineboronic acid
-
selectivity for APH 25fold higher than for fibroblast activation protein
benzyloxycarbonyl-Gly-Gly-Phe-chloromethyl ketone
CMK, chloromethyl ketone inhibitor, enzyme binding structure analysis, molecular dynamics studies, overview
bis(4-butylphenyl) (1-acetamidoethyl)phosphonate
-
0.25 or 0.05 mM, 33% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis(4-butylphenyl) (1-[[(benzyloxy)carbonyl]amino]ethyl)phosphonate
-
0.25 or 0.05 mM, 30% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis(4-chlorophenyl) (1-acetamidoethyl)phosphonate
-
0.25 or 0.05 mM, 48% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis(4-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]ethyl)phosphonate
-
0.25 or 0.05 mM, 50% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis(4-ethylphenyl) (1-acetamidoethyl)phosphonate
-
0.25 or 0.05 mM, 22% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis(4-ethylphenyl) (1-[[(benzyloxy)carbonyl]amino]ethyl)phosphonate
-
0.25 or 0.05 mM, 34% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis(4-methoxyphenyl) (1-[[(benzyloxy)carbonyl]amino]ethyl)phosphonate
-
0.25 or 0.05 mM, 65% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis[4-(methylsulfanyl)phenyl] (1-[4-[(tert-butoxycarbonyl)amino]butanamido]ethyl)phosphonate
-
0.25 or 0.05 mM, 32% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis[4-(methylsulfanyl)phenyl] (1-[[(benzyloxy)carbonyl]amino]ethyl)phosphonate
-
0.25 or 0.05 mM, 47% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis[4-(methylsulfanyl)phenyl] [1-(2-cyclohexylacetamido)ethyl]phosphonate
-
0.25 or 0.05 mM, 39% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis[4-(methylsulfanyl)phenyl] [1-(2-phenylacetamido)ethyl]phosphonate
-
0.25 or 0.05 mM, 46% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis[4-(methylsulfanyl)phenyl] [1-(3-cyclohexylpropanamido)ethyl]phosphonate
-
0.25 or 0.05 mM, 36% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis[4-(methylsulfanyl)phenyl] [1-(4-methoxybenzamido)ethyl]phosphonate
-
0.25 or 0.05 mM, 49% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis[4-(methylsulfanyl)phenyl] [1-(4-phenylbutanamido)ethyl]phosphonate
-
0.25 or 0.05 mM, 39% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis[4-(methylsulfanyl)phenyl] [1-[(pyrazine-2-carbonyl)amino]ethyl]phosphonate
-
0.25 or 0.05 mM, 49% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis[4-(methylsulfanyl)phenyl] [1-[3-(3,4-dimethoxyphenyl)propanamido]ethyl]phosphonate
-
0.25 or 0.05 mM, 37% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis[4-(methylsulfanyl)phenyl] [1-[3-(4-methoxyphenyl)propanamido]ethyl]phosphonate
-
0.25 or 0.05 mM, 46% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis[4-(methylsulfanyl)phenyl] [1-[3-(pyridin-2-yl)propanamido]ethyl]phosphonate
-
0.25 or 0.05 mM, 40% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis[4-(propan-2-yl)phenyl] (1-acetamidoethyl)phosphonate
-
0.25 or 0.05 mM, 37% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
bis[4-(propan-2-yl)phenyl] (1-[[(benzyloxy)carbonyl]amino]ethyl)phosphonate
-
0.25 or 0.05 mM, 23% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
DELTA12-prostaglandin J2
0.1 mM, inhibition to 52.1% of control, HeLa lysate
diphenyl (1-acetamidoethyl)phosphonate
-
0.25 or 0.05 mM, 21% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
diphenyl (1-[[(benzyloxy)carbonyl]amino]ethyl)phosphonate
-
0.25 or 0.05 mM, 29% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
diphenyl [1-(2-cyclohexylacetamido)ethyl]phosphonate
-
0.25 or 0.05 mM, 36% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
diphenyl [1-(2-phenylacetamido)ethyl]phosphonate
-
0.25 or 0.05 mM, 40% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
diphenyl [1-(3-cyclohexylpropanamido)ethyl]phosphonate
-
0.25 or 0.05 mM, 57% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
diphenyl [1-(4-methoxybenzamido)ethyl]phosphonate
-
0.25 or 0.05 mM, 43% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
diphenyl [1-(4-phenylbutanamido)ethyl]phosphonate
-
0.25 or 0.05 mM, 34% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
diphenyl [1-[(pyrazine-2-carbonyl)amino]ethyl]phosphonate
-
0.25 or 0.05 mM, 48% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
diphenyl [1-[3-(4-hydroxyphenyl)propanamido]ethyl]phosphonate
-
0.25 or 0.05 mM, 69% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
Glyoxal
0.1 mM, inhibition to 92% of control, HeLa lysate. 0.1 mM, inhibition to 65.9% of control, purified enzyme
Guanidine-HCl
1 M, complete loss of activity, after removal of guanidine-HCl the enzyme recovers 25% of its activity
linoleic acid
0.1 mM, inhibition to 46.3% of control, HeLa lysate. 0.1 mM, inhibition to 58.9% of control, purified enzyme
malathion
significantly inhibits the activity of enzyme APH both in vitro and in vivo
meropenem
the active form of the enzyme binds four meropenem molecules covalently linked to the catalytic Ser587 of the serineprotease triad, in an acyl-enzyme state. the enzyme is hindered from fully processing the antibiotic by the displacement and protonation of His707 of the catalytic triad. The enzyme is made susceptible to the association by its unusually sheltered active pockets and flexible catalytic triads
methyl glyoxal
0.1 mM, inhibition to 97% of control, HeLa lysate. 0.1 mM, inhibition to % of control, purified enzyme
N-acetyl-Ala chloromethyl ketone
-
inactivation follows first order kinetics, acetyl-Ala protects
p-nitrophenyl-N-propyl carbamate
-
potent active site-directed, pseudo-first-order kinetics
peptide SsCEI 2
-
specific and efficient inhibition. No inhibition in presence of peptide SsCEI 3 and peptide SsCEI 4
-
phoxim
significantly inhibits the activity of enzyme APH both in vitro and in vivo
prostaglandin A1
0.1 mM, inhibition to 50.7% of control, HeLa lysate. 0.1 mM, inhibition to 41.6% of control, purified enzyme
prostaglandin E1
0.1 mM, inhibition to 62.2% of control, HeLa lysate. 0.1 mM, inhibition to 76.3% of control, purified enzyme
Sulfolobus solfataricus chymotrypsin-elastase inhibitor
specific inhibition
-
tert-butyl 4-[(1-[bis[4-(methylsulfanyl)phenoxy]phosphoryl]ethyl)carbamoyl]piperidine-1-carboxylate
-
0.25 or 0.05 mM, 44% inhibition, enzyme from U937 cells, percentage of inhibition after 15 min incubation of APH with tested inhibitor (250 or 50 micromol)
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
chlorpyrifos
binding structure, docking study, and molecular dynamics simulations using structure PDB ID 1VE7 as search model, and umbrella sampling calculations, molecular mechanical/GBSA calculations, enzyme-inhibitor complex structure, overview
chlorpyrifos
significantly inhibits the activity of enzyme APH both in vitro and in vivo
dichlorvos
-
exhibits high affinity for acylpeptide hydrolase, possibly blocks its activity toward N-acylpeptide
phosphatidylethanolamine-binding protein inhibitor SsCEI
-
-
phosphatidylethanolamine-binding protein inhibitor SsCEI
-
-
Urea
6 M, about 70% loss of activity, regains activity at almost all urea concentrations upon removal of the denaturinf agent
additional information
different organophosphorous compounds bind to the enzyme inducing conformational changes in two domains, namely, alpha/beta hydrolase and beta-propeller, computational study of APH bound to chlorpyrifosmethyl oxon and dichlorvos, and molecular dynamics simulations of enzyme bound to the inhibitors, the starting model of APH is derived from 2.7 A resolution crystal structure of acylpeptide hydrolase/esterase from Aeropyrum pernix K1 (PDB ID 1VE7), overview. The docking study reveals that Val471 and Gly368 are important residues for chlorpyrifosmethyl oxon and dichlorvos binding
-
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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6
N-acetyl-L-Leu-4-nitroanilide
in 25 mM Tris-HCl buffer pH 7.5, at 90°C
0.04
N-acetyl-L-Phe-4-nitroanilide
in 25 mM Tris-HCl buffer pH 7.5, at 90°C
0.00129
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala
pH 7.0, 70°C, wild-type enzyme
0.00281
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala
pH 7.0, 70°C, mutant enzyme D524N
0.0071
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala
pH 7.0, 70°C, mutant enzyme D524A
0.467
Ac-Leu-p-nitroanilide
mutant R526V, in the presence of 1 M sodium chloride
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
1.76
Ac-Leu-p-nitroanilide
mutant E88A, in the presence of 1 M sodium chloride
20.2
acetyl-Ala-4-nitroanilide
AB009494
pH 5.4, 85°C, heat-activated enzyme
15.2
Acetyl-Ala-Ala-Ala-Ala
AB009494
pH 5.4, 85°C, heat-activated enzyme
12.9
acetyl-Leu-4-nitroanilide
AB009494
pH 5.4, 85°C, heat-activated enzyme
0.8
N-acetyl-L-Ala-4-nitroanilide
in 25 mM Tris-HCl buffer pH 7.5, at 90°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17.5
N-acetyl-L-Ala-4-nitroanilide
in 25 mM Tris-HCl buffer pH 7.5, at 90°C
18
N-acetyl-L-Leu-4-nitroanilide
in 25 mM Tris-HCl buffer pH 7.5, at 90°C
2
N-acetyl-L-Phe-4-nitroanilide
in 25 mM Tris-HCl buffer pH 7.5, at 90°C
0.000917
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala
pH 7.0, 70°C, mutant enzyme D524A
0.00525
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala
pH 7.0, 70°C, mutant enzyme D524N
8.2
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala
pH 7.0, 70°C, wild-type enzyme
10.5
Ac-Leu-p-nitroanilide
mutant R526V, in the presence of 1 M sodium chloride
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
144
acetyl-Ala-4-nitroanilide
AB009494
pH 5.4, 85°C, heat-activated enzyme
2090
Acetyl-Ala-Ala-Ala-Ala
AB009494
pH 5.4, 85°C, heat-activated enzyme
3200
acetyl-Leu-4-nitroanilide
AB009494
pH 5.4, 85°C, heat-activated enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
17.5
N-acetyl-L-Ala-4-nitroanilide
in 25 mM Tris-HCl buffer pH 7.5, at 90°C
32.7
N-acetyl-L-Leu-4-nitroanilide
in 25 mM Tris-HCl buffer pH 7.5, at 90°C
2
N-acetyl-L-Phe-4-nitroanilide
in 25 mM Tris-HCl buffer pH 7.5, at 90°C
0.2
succinyl-AAA-4-nitroanilide
in 25 mM Tris-HCl buffer pH 7.5, at 90°C
1.3
succinyl-GGF-4-nitroanilide
in 25 mM Tris-HCl buffer pH 7.5, at 90°C
0.7
Z-GGL-4-nitroanilide
in 25 mM Tris-HCl buffer pH 7.5, at 90°C
0.129
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala
pH 7.0, 70°C, mutant enzyme D524A
1.87
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala
pH 7.0, 70°C, mutant enzyme D524N
6347
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala
pH 7.0, 70°C, wild-type enzyme
0.414
N-acetyl-Phe-2-naphthylamide
pH 7.0, 70°C, mutant enzyme D524A, measured under first-order conditions
1.31
N-acetyl-Phe-2-naphthylamide
pH 7.0, 70°C, mutant enzyme D524N, measured under first-order conditions
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00002
phosphatidylethanolamine-binding protein inhibitor SsCEI
pH 7.5, 80°C, substrate: N-acetyl-L-leucyl 4-nitroanilide
-
0.008
phosphatidylethanolamine-binding protein inhibitor SsCEI
pH 7.5, 90°C, substrate: acetyl-Leu-4-nitroanilide
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
4-hydroxyphenyl 4-methoxyphenyl (1-acetamidoethyl)phosphonate
Sus scrofa
-
pH 7.4, temperature not specified in the publication
0.25
bis(4-chlorophenyl) (1-[[(benzyloxy)carbonyl]amino]ethyl)phosphonate
Sus scrofa
-
pH 7.4, temperature not specified in the publication
0.19
bis(4-methoxyphenyl) (1-[[(benzyloxy)carbonyl]amino]ethyl)phosphonate
Sus scrofa
-
pH 7.4, temperature not specified in the publication
0.219
diphenyl [1-(3-cyclohexylpropanamido)ethyl]phosphonate
Sus scrofa
-
pH 7.4, temperature not specified in the publication
0.18
diphenyl [1-[3-(4-hydroxyphenyl)propanamido]ethyl]phosphonate
Sus scrofa
-
pH 7.4, temperature not specified in the publication
0.00000002
phosphatidylethanolamine-binding protein inhibitor SsCEI
Saccharolobus solfataricus
pH 7.5, 80°C, substrate: N-acetyl-L-leucyl 4-nitroanilide
-
0.0011
2-(pentylsulfanyl)-4H-1,3,2-benzodioxaphosphinine 2-oxide
Mus musculus
-
IC50: 0.0011 mM
0.0015
2-(pentylsulfanyl)-4H-1,3,2-benzodioxaphosphinine 2-oxide
Homo sapiens
-
IC50: 0.0015 mM
additional information
additional information
Bombyx mori
the IC50 values of chlorpyrifos, phoxim, and malathion with recombinant enzyme are 1.60, 7.90, and 7.62 mg/l, respectively, pH 7.5, 25°C
-
additional information
additional information
Bombyx mori
-
the IC50 values of chlorpyrifos, phoxim, and malathion with recombinant enzyme are 1.60, 7.90, and 7.62 mg/l, respectively, pH 7.5, 25°C
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0007
cellular extract, using N-acetyl-L-Leu-4-nitroanilide as substrate, at pH 7.5 and 90°C
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
1.9
118
AB009494
substrate: acetyl-Ala-Ala-Ala-Ala-Ala-Ala, pH 5.4, 85°C, heat-activated enzyme
15
AB009494
substrate: acetyl-Tyr-4-nitroanilide, pH 5.4, 85°C, heat-activated enzyme
1513
AB009494
substrate: formyl-Met-Ala, pH 5.4, 85°C, heat-activated enzyme
17026
AB009494
substrate: formyl-Met-Ala-Ser, pH 5.4, 85°C, heat-activated enzyme
1830
AB009494
substrate: acetyl-Ala-Ala-Ala-Ala, pH 5.4, 85°C, heat-activated enzyme
4.8
51
AB009494
substrate: acetyl-Ala-4-nitroanilide, pH 5.4, 85°C, heat-activated enzyme
5120
AB009494
substrate: acetyl-Met-Ala, pH 5.4, 85°C, heat-activated enzyme
5363
AB009494
substrate: formyl-Ala-Ala-Ala, pH 5.4, 85°C, heat-activated enzyme
66.8
AB009494
substrate: formyl-Met-Ala-Ala-Ala-Ala-Ala, pH 5.4, 85°C, heat-activated enzyme
7060
AB009494
substrate: acetyl-Ala-Ala, pH 5.4, 85°C, heat-activated enzyme
7064
AB009494
substrate: formyl-Met-Leu-Gly, pH 5.4, 85°C, heat-activated enzyme
750
AB009494
substrate: acetyl-Leu-4-nitroanilide, pH 5.4, 85°C, heat-activated enzyme
77
AB009494
substrate: acetyl-Met-Ala-Ala-Ala-Ala-Ala, pH 5.4, 85°C, heat-activated enzyme
77.3
AB009494
substrate: formyl-Ala-Ala-Ala-Ala-Ala-Ala, pH 5.4, 85°C, heat-activated enzyme
additional information
4.8
after 6857fold purification, using N-acetyl-L-Leu-4-nitroanilide as substrate, at pH 7.5 and 90°C
additional information
AB009494
the specific activity of the enzyme increases 714fold with heat treatment, suggesting the modification of the structure of the enzyme for optimal hydrolytic activity by heating
additional information
-
the specific activity of the enzyme increases 714fold with heat treatment, suggesting the modification of the structure of the enzyme for optimal hydrolytic activity by heating
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5 - 9
8.4
7.5 - 9
-
hydrolysis of formylmethionine-beta-naphthylamide or Met-Met-Leu-Phe
9
the rate constants for the D524A and D524N variants increase to about pH 9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8 - 8.8
pH 5.8: about% of maximal activity, pH 8.8: about% of maximal activity
6 - 9.5
pH 6.0: about 65% of maximal activity, pH 9.5: about 70% of maximal activity
7.5 - 8
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
50
70
75
-
truncated mutant of apAPH that lacks the first short alpha-helix at the N-terminal
80
90
92
95
additional information
additional information
AB009494
the specific activity of the enzyme increases 714fold with heat treatment, suggesting the modification of the structure of the enzyme for optimal hydrolytic activity by heating
additional information
-
the specific activity of the enzyme increases 714fold with heat treatment, suggesting the modification of the structure of the enzyme for optimal hydrolytic activity by heating
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80 - 95
80°C: about 65% of maximal activity, 95°C: about 50% of maximal activity
additional information
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
APH expression in Alzheimers disease brain is lower than in age-matched controls
brenda
Plasmodium falciparum internalizes and accumulates the erythrocyte enzyme (APEH) during its growth in the host cell. Internalization of erythrocyte acylpeptide hydrolase is required for asexual replication of Plasmodium falciparum
brenda
additional information
enzyme BmAPH is expressed in all tested tissues and developmental stages of the silkworm, immunohistochemistry analysis. BmAPH protein is localized in the basement membranes
brenda
additional information
-
enzyme BmAPH is expressed in all tested tissues and developmental stages of the silkworm, immunohistochemistry analysis. BmAPH protein is localized in the basement membranes
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
ACPH is preferentially located at the pre-synaptic side
brenda
additional information
additional information
APEH is primarily localised in the cytoplasm, but a subfraction of the enzyme is sequestered at sites of nuclear damage following UVA irradiation or following oxidative stress
-
brenda
additional information
-
APEH is primarily localised in the cytoplasm, but a subfraction of the enzyme is sequestered at sites of nuclear damage following UVA irradiation or following oxidative stress
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
-
the enzyme is proposed as a target for the development of potential anticancer agents
evolution
malfunction
metabolism
physiological function
additional information
evolution
the enzyme belongs to a class of serine-type protease belonging to the prolyl oligopeptidase (POP) family. The members of the POP family are involved in numerous metabolic processes
evolution
enzyme AAP belongs to alpha/beta-hydrolase enzyme superfamily
evolution
acylaminoacyl peptidase is a member of the prolyl oligopeptidase protein family
evolution
the enzyme belongs to the prolyl oligopeptidase family of serine proteases
evolution
-
enzyme AAP belongs to alpha/beta-hydrolase enzyme superfamily
-
evolution
-
acylaminoacyl peptidase is a member of the prolyl oligopeptidase protein family
-
evolution
Aeropyrum pernix ATCC 700893
-
enzyme AAP belongs to alpha/beta-hydrolase enzyme superfamily
-
evolution
Aeropyrum pernix ATCC 700893
-
acylaminoacyl peptidase is a member of the prolyl oligopeptidase protein family
-
evolution
Aeropyrum pernix JCM 9820
-
enzyme AAP belongs to alpha/beta-hydrolase enzyme superfamily
-
evolution
Aeropyrum pernix JCM 9820
-
acylaminoacyl peptidase is a member of the prolyl oligopeptidase protein family
-
evolution
Aeropyrum pernix NBRC 100138
-
enzyme AAP belongs to alpha/beta-hydrolase enzyme superfamily
-
evolution
Aeropyrum pernix NBRC 100138
-
acylaminoacyl peptidase is a member of the prolyl oligopeptidase protein family
-
malfunction
-
overexpression of AARE/OPH exhibits no apparent effect on the level of oxidized proteins because wild types have inherently high AARE/OPH activity
malfunction
-
the AtAARE-suppressed plants using RNAi became susceptible to oxidative stress corresponding to enhanced accumulation of oxidized proteins
malfunction
-
transgenic overexpression of APH results in crystallin cleavage, impaired lens development, and cataract
metabolism
AB009494
the existence of the acylamino acid-releasing enzyme in archaea suggests that the mechanisms of protein degradation or initiation of protein synthesis or both in archaea may be similar to those in eukaryotes
metabolism
the enzyme (APEH) participates in the metabolism of the antiepileptic drug valproic acid (2-propylpentanoic acid, VPA) by catalyzing the hydrolysis of the VPA metabolite valproylglucuronide (VPA-G) to its aglycon. The inhibition of APEH by carbapenem antibiotics decreases therapeutic VPA levels by enhancing the urinary elimination of VPA in form of VPA-G. APEH sequence variants may have pharmacogenetic implications for the treatment of patients with the antiepileptic drug valproic acid. Therefore, APEH mutation analysis is recommended in patients who do not achieve usually reached therapeutic valproic acid levels or need particularly high drug doses to do so
physiological function
-
AtAARE contributes to eliminate oxidized proteins to sustain the antioxidant system in the cytoplasm
physiological function
-
APH is involved in the generation of peptides that have the potential to induce protein aggregation
physiological function
enzyme APEH is a component of the cellular response to DNA damage. APEH is primarily localised in the cytoplasm, but a subfraction of the enzyme is sequestered at sites of nuclear damage following UVA irradiation or following oxidative stress. Localization of APEH at sites of nuclear damage is mediated by direct interaction with XRCC1, a scaffold protein that accelerates the repair of DNA single-strand breaks. APEH interacts with the amino-terminal domain of XRCC1, and APEH facilitates both single-strand break repair and cell survival following exposure to H2O2 in human cells
physiological function
enzyme BmAPHmay be involved in enhancing silkworm tolerance to organophosphorus (OP) insecticides
physiological function
acylpeptide hydrolases (APHs) catalyze the removal of N-acylated amino acids from blocked peptides
physiological function
-
the enzyme participates in various events including oxidized proteins degradation, amyloid beta-peptide cleavage, and response to DNA damage
physiological function
the enzyme functions as an upstream regulator of the proteasome through the removal of terminal N-acetylated residues from its protein substrates
physiological function
the enzyme is involved in the recycling of amino acids from acylated peptides
additional information
enzyme structure modeling and comparison with the enzyme structure from Sulfurisphaera tokodaii, overview. Both enzymes share a high structural homology
additional information
molecular docking and molecular dynamics simulations using the structure with PDB ID 1VE7, substrate binding structures, overview
additional information
substrate binding structures of wild-type and mutant R526V enzymes, docking study and molecular dynamics simulations, overview. Molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) calculations
additional information
-
substrate binding structures of wild-type and mutant R526V enzymes, docking study and molecular dynamics simulations, overview. Molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) calculations
additional information
substrate binding structures of wild-type and mutant enzymes, docking study and molecular dynamics simulations, overview. Molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) calculations
additional information
the closed form of the enzyme is catalytically active, while opening deactivates the catalytic triad. Molecular-dynamics simulations are used to investigate the structure of the complexes formed with longer peptide substrates showing that their binding within the large crevice of the closed form of ApAAP leaves the enzyme structure unperturbed. Their accessing the binding site seems more probable when assisted by opening of the enzyme. Thus, the open form of ApAAP corresponds to a scavenger of possible substrates, the actual cleavage of which only takes place if the enzyme is able to re-close. Structure analysis, detailed overview
additional information
-
the closed form of the enzyme is catalytically active, while opening deactivates the catalytic triad. Molecular-dynamics simulations are used to investigate the structure of the complexes formed with longer peptide substrates showing that their binding within the large crevice of the closed form of ApAAP leaves the enzyme structure unperturbed. Their accessing the binding site seems more probable when assisted by opening of the enzyme. Thus, the open form of ApAAP corresponds to a scavenger of possible substrates, the actual cleavage of which only takes place if the enzyme is able to re-close. Structure analysis, detailed overview
additional information
the three-dimensional structure of the psychrophilic acyl aminoacyl peptidase from Sporosarcina psychrophila (SpAAP) highlights adaptive molecular changes resulting in a fine-tuned trade-off between flexibility and stability. A feature of SpAAP cold adaptation is the enlargement of the tunnel connecting the exterior of the protein with the active site. Such a wide channel might compensate for the reduced molecular motions occurring in the cold and allow easy and direct access of substrates to the catalytic site, rendering transient movements between domains unnecessary. Thus, cold-adapted SpAAP has developed a molecular strategy unique within this group of proteins: it is able to enhance the flexibility of each functional unit while still preserving sufficient stability. The Ser-Asp-His catalytic triad in SpAAP (Ser458, Asp540 and His572) matches that of the canonical alpha/beta hydrolase fold
additional information
-
the three-dimensional structure of the psychrophilic acyl aminoacyl peptidase from Sporosarcina psychrophila (SpAAP) highlights adaptive molecular changes resulting in a fine-tuned trade-off between flexibility and stability. A feature of SpAAP cold adaptation is the enlargement of the tunnel connecting the exterior of the protein with the active site. Such a wide channel might compensate for the reduced molecular motions occurring in the cold and allow easy and direct access of substrates to the catalytic site, rendering transient movements between domains unnecessary. Thus, cold-adapted SpAAP has developed a molecular strategy unique within this group of proteins: it is able to enhance the flexibility of each functional unit while still preserving sufficient stability. The Ser-Asp-His catalytic triad in SpAAP (Ser458, Asp540 and His572) matches that of the canonical alpha/beta hydrolase fold
additional information
the catalytic triad is composed by catalytic residues Ser566, Asp654, and His686
additional information
-
the catalytic triad is composed by catalytic residues Ser566, Asp654, and His686
additional information
exploration of the chlorpyrifos escape pathway from acylpeptide hydrolases using steered molecular dynamics simulations, overview
additional information
enzyme structure modeling and comparison with the enzyme structure from Aeropyrum pernix, overview. Both enzymes share a high structural homology
additional information
Plasmodium falciparum internalizes and accumulates the erythrocyte enzyme (APEH) during its growth in the host cell. Internalization of erythrocyte acylpeptide hydrolase is required for asexual replication of Plasmodium falciparum
additional information
-
enzyme structure modeling and comparison with the enzyme structure from Aeropyrum pernix, overview. Both enzymes share a high structural homology
-
additional information
-
enzyme structure modeling and comparison with the enzyme structure from Aeropyrum pernix, overview. Both enzymes share a high structural homology
-
additional information
-
enzyme structure modeling and comparison with the enzyme structure from Sulfurisphaera tokodaii, overview. Both enzymes share a high structural homology
-
additional information
-
substrate binding structures of wild-type and mutant enzymes, docking study and molecular dynamics simulations, overview. Molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) calculations
-
additional information
-
the closed form of the enzyme is catalytically active, while opening deactivates the catalytic triad. Molecular-dynamics simulations are used to investigate the structure of the complexes formed with longer peptide substrates showing that their binding within the large crevice of the closed form of ApAAP leaves the enzyme structure unperturbed. Their accessing the binding site seems more probable when assisted by opening of the enzyme. Thus, the open form of ApAAP corresponds to a scavenger of possible substrates, the actual cleavage of which only takes place if the enzyme is able to re-close. Structure analysis, detailed overview
-
additional information
Aeropyrum pernix ATCC 700893
-
enzyme structure modeling and comparison with the enzyme structure from Sulfurisphaera tokodaii, overview. Both enzymes share a high structural homology
-
additional information
Aeropyrum pernix ATCC 700893
-
substrate binding structures of wild-type and mutant enzymes, docking study and molecular dynamics simulations, overview. Molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) calculations
-
additional information
Aeropyrum pernix ATCC 700893
-
the closed form of the enzyme is catalytically active, while opening deactivates the catalytic triad. Molecular-dynamics simulations are used to investigate the structure of the complexes formed with longer peptide substrates showing that their binding within the large crevice of the closed form of ApAAP leaves the enzyme structure unperturbed. Their accessing the binding site seems more probable when assisted by opening of the enzyme. Thus, the open form of ApAAP corresponds to a scavenger of possible substrates, the actual cleavage of which only takes place if the enzyme is able to re-close. Structure analysis, detailed overview
-
additional information
-
enzyme structure modeling and comparison with the enzyme structure from Aeropyrum pernix, overview. Both enzymes share a high structural homology
-
additional information
-
enzyme structure modeling and comparison with the enzyme structure from Aeropyrum pernix, overview. Both enzymes share a high structural homology
-
additional information
Aeropyrum pernix JCM 9820
-
enzyme structure modeling and comparison with the enzyme structure from Sulfurisphaera tokodaii, overview. Both enzymes share a high structural homology
-
additional information
Aeropyrum pernix JCM 9820
-
substrate binding structures of wild-type and mutant enzymes, docking study and molecular dynamics simulations, overview. Molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) calculations
-
additional information
Aeropyrum pernix JCM 9820
-
the closed form of the enzyme is catalytically active, while opening deactivates the catalytic triad. Molecular-dynamics simulations are used to investigate the structure of the complexes formed with longer peptide substrates showing that their binding within the large crevice of the closed form of ApAAP leaves the enzyme structure unperturbed. Their accessing the binding site seems more probable when assisted by opening of the enzyme. Thus, the open form of ApAAP corresponds to a scavenger of possible substrates, the actual cleavage of which only takes place if the enzyme is able to re-close. Structure analysis, detailed overview
-
additional information
Aeropyrum pernix NBRC 100138
-
enzyme structure modeling and comparison with the enzyme structure from Sulfurisphaera tokodaii, overview. Both enzymes share a high structural homology
-
additional information
Aeropyrum pernix NBRC 100138
-
substrate binding structures of wild-type and mutant enzymes, docking study and molecular dynamics simulations, overview. Molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) calculations
-
additional information
Aeropyrum pernix NBRC 100138
-
the closed form of the enzyme is catalytically active, while opening deactivates the catalytic triad. Molecular-dynamics simulations are used to investigate the structure of the complexes formed with longer peptide substrates showing that their binding within the large crevice of the closed form of ApAAP leaves the enzyme structure unperturbed. Their accessing the binding site seems more probable when assisted by opening of the enzyme. Thus, the open form of ApAAP corresponds to a scavenger of possible substrates, the actual cleavage of which only takes place if the enzyme is able to re-close. Structure analysis, detailed overview
-
Show AA Sequence and Transmembrane Helices (3343 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
280000
300000
350000
64000
67000
70000
75000
76000
-
4 * 76000, loss of native tetrameric structure upon citraconylation. This process is reversed at acidic pH. Involvement of all cysteines in disulfide bridges
82000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
homodimer
homotrimer
tetramer
additional information
?
x * 78500, about, sequence calculation, x * 80000, recombinant His-tagged enzyme, SDS-PAGE
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
-
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
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
-
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
release of subunits from the quaternary structure is hindered by an arm exchange mechanism, in which a tiny structural element at the N-terminus of one subunit inserts into the other subunit. Mutants lacking the arm are monomeric, inactive and highly prone to aggregation
tetramer
-
4 * 76000, loss of native tetrameric structure upon citraconylation. This process is reversed at acidic pH. Involvement of all cysteines in disulfide bridges
additional information
APH family is composed of a beta-propeller domain in N-terminus and a catalytic domain in C-terminus. These domains are structurally connected by bridge regions. One is the N-terminus region that stretches into the C-terminal catalytic domain. The other is the linker that directly connects the beta-propeller domain to the catalytic domain. N-terminus region forms a unique alpha-helix 1 (alpha1), which deviates from the beta-propeller domain. Nevertheless, it connects with the surface of the catalytic domain. The structure of alpha1 is conserved and affects conformational flexibility
additional information
Aeropyrum pernix ATCC 700893
-
APH family is composed of a beta-propeller domain in N-terminus and a catalytic domain in C-terminus. These domains are structurally connected by bridge regions. One is the N-terminus region that stretches into the C-terminal catalytic domain. The other is the linker that directly connects the beta-propeller domain to the catalytic domain. N-terminus region forms a unique alpha-helix 1 (alpha1), which deviates from the beta-propeller domain. Nevertheless, it connects with the surface of the catalytic domain. The structure of alpha1 is conserved and affects conformational flexibility
-
additional information
-
APH family is composed of a beta-propeller domain in N-terminus and a catalytic domain in C-terminus. These domains are structurally connected by bridge regions. One is the N-terminus region that stretches into the C-terminal catalytic domain. The other is the linker that directly connects the beta-propeller domain to the catalytic domain. N-terminus region forms a unique alpha-helix 1 (alpha1), which deviates from the beta-propeller domain. Nevertheless, it connects with the surface of the catalytic domain. The structure of alpha1 is conserved and affects conformational flexibility
-
additional information
Aeropyrum pernix JCM 9820
-
APH family is composed of a beta-propeller domain in N-terminus and a catalytic domain in C-terminus. These domains are structurally connected by bridge regions. One is the N-terminus region that stretches into the C-terminal catalytic domain. The other is the linker that directly connects the beta-propeller domain to the catalytic domain. N-terminus region forms a unique alpha-helix 1 (alpha1), which deviates from the beta-propeller domain. Nevertheless, it connects with the surface of the catalytic domain. The structure of alpha1 is conserved and affects conformational flexibility
-
additional information
Aeropyrum pernix NBRC 100138
-
APH family is composed of a beta-propeller domain in N-terminus and a catalytic domain in C-terminus. These domains are structurally connected by bridge regions. One is the N-terminus region that stretches into the C-terminal catalytic domain. The other is the linker that directly connects the beta-propeller domain to the catalytic domain. N-terminus region forms a unique alpha-helix 1 (alpha1), which deviates from the beta-propeller domain. Nevertheless, it connects with the surface of the catalytic domain. The structure of alpha1 is conserved and affects conformational flexibility
-
additional information
enzyme peptide mapping, mass spectrometric analysis, overview
additional information
-
enzyme peptide mapping, mass spectrometric analysis, overview
additional information
-
structural investigations of the enzyme by mass spectrometric procedures
additional information
tertiary and quarternary structure analysis and tructure comparisons, overview
additional information
-
tertiary and quarternary structure analysis and tructure comparisons, overview
additional information
APH family is composed of a beta-propeller domain in N-terminus and a catalytic domain in C-terminus. These domains are structurally connected by bridge regions. One is the N-terminus region that stretches into the C-terminal catalytic domain. The other is the linker that directly connects the beta-propeller domain to the catalytic domain. N-terminus region forms a unique alpha-helix 1 (alpha1), which deviates from the beta-propeller domain. Nevertheless, it connects with the surface of the catalytic domain. The structure of alpha1 is conserved and affects conformational flexibility
additional information
-
APH family is composed of a beta-propeller domain in N-terminus and a catalytic domain in C-terminus. These domains are structurally connected by bridge regions. One is the N-terminus region that stretches into the C-terminal catalytic domain. The other is the linker that directly connects the beta-propeller domain to the catalytic domain. N-terminus region forms a unique alpha-helix 1 (alpha1), which deviates from the beta-propeller domain. Nevertheless, it connects with the surface of the catalytic domain. The structure of alpha1 is conserved and affects conformational flexibility
-
additional information
-
APH family is composed of a beta-propeller domain in N-terminus and a catalytic domain in C-terminus. These domains are structurally connected by bridge regions. One is the N-terminus region that stretches into the C-terminal catalytic domain. The other is the linker that directly connects the beta-propeller domain to the catalytic domain. N-terminus region forms a unique alpha-helix 1 (alpha1), which deviates from the beta-propeller domain. Nevertheless, it connects with the surface of the catalytic domain. The structure of alpha1 is conserved and affects conformational flexibility
-
additional information
-
APH family is composed of a beta-propeller domain in N-terminus and a catalytic domain in C-terminus. These domains are structurally connected by bridge regions. One is the N-terminus region that stretches into the C-terminal catalytic domain. The other is the linker that directly connects the beta-propeller domain to the catalytic domain. N-terminus region forms a unique alpha-helix 1 (alpha1), which deviates from the beta-propeller domain. Nevertheless, it connects with the surface of the catalytic domain. The structure of alpha1 is conserved and affects conformational flexibility
-
additional information
-
APH family is composed of a beta-propeller domain in N-terminus and a catalytic domain in C-terminus. These domains are structurally connected by bridge regions. One is the N-terminus region that stretches into the C-terminal catalytic domain. The other is the linker that directly connects the beta-propeller domain to the catalytic domain. N-terminus region forms a unique alpha-helix 1 (alpha1), which deviates from the beta-propeller domain. Nevertheless, it connects with the surface of the catalytic domain. The structure of alpha1 is conserved and affects conformational flexibility
-
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals grown at 17.8°C 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 20°C 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
purified enzyme in complex with chloromethyl ketone inhibitor, hanging drop vapour diffusion method, for the complex crystal form: mixing of 0.003 ml of protein solution containing 0.221 mM ApAAP protein, and 0.56 mM inhibitor CMK in 20 mM Tris pH 7.5 buffer, with 0.003 ml of reservoir solution containing 78 mM sodium acetate, pH 4.5, 2.4% w/v PEG 4000, 6.7 mM dithiothreitol, and 0.44 mM EDTA, for apoenzyme crystal form: mixing of 0.003 ml of protein solution containing 0.158 mM ApAAP protein in 20 mM Tris pH 7.5 buffer, with 0.003 ml of reservoir solution containing 78 mM sodium acetate, pH 5.0, 2.2% w/v PEG 4000, 5.2 mM dithiothreitol, and 0.34 mM EDTA, 20°C, X-ray diffraction structure determination and analysis at 1.90A and 2.55A resolution, modeling
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
crystallized using microbatch-under-oil employing the random microseed matrix screening method. The protein crystallizes in space group P2(1)1, with unit-cell parameters a: 77.6, b: 189.6, c: 120.4 A, beta: 108.4
-
purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 50 mM sodium phosphate, 100 mM NaCl, pH 7.5, with 0.001 ml reservoir solution containing 30% PEG 400, 0.1 M Na-HEPES, pH 7.5, 0.2 M MgCl2, and 0.1 M (NH4)2SO4, 4°C, X-ray diffraction structure determination and analysis at 2.5 A resolution
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
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PROTEIN VARIANTS
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
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
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
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
-
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
-
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 15°C
DELTAN21
mutant, N-terminal helix deleted, no longer functional at the optimum temperature, 95°C, 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
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
R526V
Ac-Leu-4-nitroanilide bound to R526V AAP to form a more disordered loop (residues 552-562) in the alpha/beta-hydrolase fold like of AAP, which causes an open and inactive AAP domain form, secondly, binding 4-nitrophenylcaprylate and Ac-Leu-4-nitroanilide to AAP can decrease the flexibility of residues 225-250, 260-270 and 425-450, in which the ordered secondary structures may contain the suitable geometrical structure and so it is useful to serine attack
E10A
-
a 20-min pre-incubation at 50°C leads to a residual of 65% (wild-type: 70%)
K6A
-
a 20-min pre-incubation at 50°C leads to a residual of 70% similar to wild-type
K6A/E10A
-
a 20-min pre-incubation at 50°C leads to a residual of 45% (wild-type: 70%)
N3A
-
a 20-min pre-incubation at 50°C leads to a residual of 70% similar to wild-type
R14A
-
a 20-min pre-incubation at 50°C leads to a residual of 70% similar to wild-type
additional information
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
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
additional information
construction of mutant APE-DELTAEG by deletion of two residues E316 and G317, and of mutant APE-2G by inserted two Gly residues between residues L315 and E316 deleted residues F395 and V396. The catalytic activity of the APE-DELTAEG mutant toward 4-nitrophenyl butyrate (pNPC4) is 2.8fold more active compared to wild-type, whose preferred substrate is 4-nitrophenyl caprylate (pNPC8)
additional information
Aeropyrum pernix ATCC 700893
-
construction of mutant APE-DELTAEG by deletion of two residues E316 and G317, and of mutant APE-2G by inserted two Gly residues between residues L315 and E316 deleted residues F395 and V396. The catalytic activity of the APE-DELTAEG mutant toward 4-nitrophenyl butyrate (pNPC4) is 2.8fold more active compared to wild-type, whose preferred substrate is 4-nitrophenyl caprylate (pNPC8)
-
additional information
-
construction of mutant APE-DELTAEG by deletion of two residues E316 and G317, and of mutant APE-2G by inserted two Gly residues between residues L315 and E316 deleted residues F395 and V396. The catalytic activity of the APE-DELTAEG mutant toward 4-nitrophenyl butyrate (pNPC4) is 2.8fold more active compared to wild-type, whose preferred substrate is 4-nitrophenyl caprylate (pNPC8)
-
additional information
Aeropyrum pernix JCM 9820
-
construction of mutant APE-DELTAEG by deletion of two residues E316 and G317, and of mutant APE-2G by inserted two Gly residues between residues L315 and E316 deleted residues F395 and V396. The catalytic activity of the APE-DELTAEG mutant toward 4-nitrophenyl butyrate (pNPC4) is 2.8fold more active compared to wild-type, whose preferred substrate is 4-nitrophenyl caprylate (pNPC8)
-
additional information
Aeropyrum pernix NBRC 100138
-
construction of mutant APE-DELTAEG by deletion of two residues E316 and G317, and of mutant APE-2G by inserted two Gly residues between residues L315 and E316 deleted residues F395 and V396. The catalytic activity of the APE-DELTAEG mutant toward 4-nitrophenyl butyrate (pNPC4) is 2.8fold more active compared to wild-type, whose preferred substrate is 4-nitrophenyl caprylate (pNPC8)
-
additional information
enzyme mutants lacking the arm in the quarternary structure are monomeric, inactive and highly prone to aggregation
additional information
-
enzyme mutants lacking the arm in the quarternary structure are monomeric, inactive and highly prone to aggregation
additional information
construction of N-terminus deletion mutants DELTAN21 and DELTAN21-4 A, which can be obviously discriminated from the wild-type in terms of activity in various pH values. Mutant ST-4 A exhibits higher activity toward substrate Ac-Ala-Ala-Ala at 70°C compared with the wild-type enzyme. ST-4 A enzymatic activity is 2fold more active than wild-type at 95°C and ST-6 A enzymatic activity is 1.7fold more active than wild-type at 95°C. Construction of mutants ST-DELTAGL by deletion of residues G332 and L333, of mutant ST-2 A by insertion of four Ala residues between residues G331 and G332, of mutant ST-6 A by removal of N-terminal 21 residues and linker insertion with four Ala residues between residues G331 and G332, and of mutant DELTAN21, overview
additional information
-
construction of N-terminus deletion mutants DELTAN21 and DELTAN21-4 A, which can be obviously discriminated from the wild-type in terms of activity in various pH values. Mutant ST-4 A exhibits higher activity toward substrate Ac-Ala-Ala-Ala at 70°C compared with the wild-type enzyme. ST-4 A enzymatic activity is 2fold more active than wild-type at 95°C and ST-6 A enzymatic activity is 1.7fold more active than wild-type at 95°C. Construction of mutants ST-DELTAGL by deletion of residues G332 and L333, of mutant ST-2 A by insertion of four Ala residues between residues G331 and G332, of mutant ST-6 A by removal of N-terminal 21 residues and linker insertion with four Ala residues between residues G331 and G332, and of mutant DELTAN21, overview
-
additional information
-
construction of N-terminus deletion mutants DELTAN21 and DELTAN21-4 A, which can be obviously discriminated from the wild-type in terms of activity in various pH values. Mutant ST-4 A exhibits higher activity toward substrate Ac-Ala-Ala-Ala at 70°C compared with the wild-type enzyme. ST-4 A enzymatic activity is 2fold more active than wild-type at 95°C and ST-6 A enzymatic activity is 1.7fold more active than wild-type at 95°C. Construction of mutants ST-DELTAGL by deletion of residues G332 and L333, of mutant ST-2 A by insertion of four Ala residues between residues G331 and G332, of mutant ST-6 A by removal of N-terminal 21 residues and linker insertion with four Ala residues between residues G331 and G332, and of mutant DELTAN21, overview
-
additional information
-
construction of N-terminus deletion mutants DELTAN21 and DELTAN21-4 A, which can be obviously discriminated from the wild-type in terms of activity in various pH values. Mutant ST-4 A exhibits higher activity toward substrate Ac-Ala-Ala-Ala at 70°C compared with the wild-type enzyme. ST-4 A enzymatic activity is 2fold more active than wild-type at 95°C and ST-6 A enzymatic activity is 1.7fold more active than wild-type at 95°C. Construction of mutants ST-DELTAGL by deletion of residues G332 and L333, of mutant ST-2 A by insertion of four Ala residues between residues G331 and G332, of mutant ST-6 A by removal of N-terminal 21 residues and linker insertion with four Ala residues between residues G331 and G332, and of mutant DELTAN21, overview
-
additional information
-
construction of N-terminus deletion mutants DELTAN21 and DELTAN21-4 A, which can be obviously discriminated from the wild-type in terms of activity in various pH values. Mutant ST-4 A exhibits higher activity toward substrate Ac-Ala-Ala-Ala at 70°C compared with the wild-type enzyme. ST-4 A enzymatic activity is 2fold more active than wild-type at 95°C and ST-6 A enzymatic activity is 1.7fold more active than wild-type at 95°C. Construction of mutants ST-DELTAGL by deletion of residues G332 and L333, of mutant ST-2 A by insertion of four Ala residues between residues G331 and G332, of mutant ST-6 A by removal of N-terminal 21 residues and linker insertion with four Ala residues between residues G331 and G332, and of mutant DELTAN21, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
50
70
70 - 90
the enzyme retains 30% activity following the incubation for 24 h at 70°C while the residual activity of the enzyme is halved after 4 h incubation at 90°C
90
additional information
70
24 h, 70% loss of activity. Slight increase its relative activity during the first 5 hours of incubation
70
purified recombinant enzyme, 55 h, 70% acylpeptide releasing activity remaining
90
both the wild-type and the H367A mutant are stable up to 90°C 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 25°C, but differences diminish with increase of temperature
additional information
-
thermal stability of the multi-domain SpAAP is investigated by intrinsic fluorescence spectroscopy. This technique suggests a cooperative and apparently two-state unfolding process with a Tm of 50°C, which is consistent with the results previously observed by CD spectroscopy
additional information
-
coupling to CNBr-Sepharose and cross-linking with dimethylsuberimidate improve the thermal stability
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
75% loss of activity in 0.1 M guanidine hydrochloride at 37°C after 200 min
-
8 M urea, 1 h, 25°C, 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
-
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
-
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
-
loss of native tetrameric structure upon citraconylation. This process is reversed at acidic pH
-
stability of the cold-active acylaminoacyl peptidase relies on its dimerization by domain swapping
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
guanidine-HCl
guanidine-HCl
1 M, complete loss of activity, after removal of guanidine-HCl the enzyme recovers 25% of its activity
guanidine-HCl
-
1 M, complete loss of activity, after removal of guanidine-HCl the enzyme recovers 25% of its activity
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.05 mM sodium phosphate, pH 6.9, 2 mM MgCl2, 1 mM EDTA, stable over several months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Q Sepharose column chromatography, phenyl Sepharose column chromatography, Mono Q column chromatography, and Mono S column chromatography
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21 Transetta (DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) Codon plus by ammonium sulfate fractionation and nickel affinity chromatography
recombinant wild-type and mutant His-tagged enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a truncated mutant of apAPH that lacks the first short alpha-helix at the N-terminal is cloned and expressed in Escherichia coli
-
APEH sequence variants predicted to affect enzyme activity are selected from databases, and overexpressed in HEK293 cells
expression in Escherichia coli
expression in Escherichia coli as a functional enzyme
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
gene APE_1547.1, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene APH, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21 Transetta (DE3)
gene aph, sequence comparisons, recombinant expression of N-terminally His-tagged enzyme SpAAP in Escherichia coli
gene ST0779, sequence comparisons, recombinant expression of wild-type and mutant His-tagged enzymes in Escherichia coli strain BL21(DE3)
gene yuxL, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)Codon plus
into pET22b vector and transformed into Rozetta DE3 Escherichia coli strain
into the TOPO-V5/His tag mammalian expression vector. Wild-type and mutant APH constructs transfected into COS-7 or SK-N-MC cells
-
into the vector pET11a for expression in Escherichia coli BL21-CodonPlus DE3-RIL cells
into the vector pET15b for expression in Escherichia coli Rosetta DE3 cells
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
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
decreased activity in the brains of mice exposed to e-cigarette vapor
expression of apeh-3 is down-regulated as an immediate response to stress
expression of apeh-3 is down-regulated as an immediate response to stress
expression of apeh-3 is down-regulated as an immediate response to stress
-
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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
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
diagnostics
drug development
enzyme APH is believed to be an important target for drug design
medicine
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
additional information
analysis
-
the enzyme is a tool in sequencing blocked peptides and proteins. Useful for unblocking acetylated proteins prior to protein sequence analysis
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
analysis
AB009494
the enzyme is expected to be useful for the removal of Nalpha-acylated residues in short peptide sequence analysis at high temperatures
diagnostics
enzyme inhibition may contribute to disease development and progression in pathologies associated with redox imbalances and can potentially act as biomarker for oxidative stress in disease
diagnostics
enzyme inhibition may contribute to disease development and progression in pathologies associated with redox imbalances and can potentially act as biomarker for oxidative stress in disease
medicine
-
blood acylpeptide hydrolase activity is a sensitive marker for exposure to some organophosphate toxicants
medicine
-
blood acylpeptide hydrolase activity is a sensitive marker for exposure to some organophosphate toxicants
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
medicine
-
reliable biomarker for some organophosphate pesticides that show higher specificity for acylpeptide hydrolase than for cholinesterases
medicine
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
-
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
-
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sherriff, R.M.; Broom, M.F.; Chadwick, V.S.
Isolation and purification of N-formylmethionine aminopeptidase from rat intestine
Biochim. Biophys. Acta
1119
275-280
1992
Rattus norvegicus
brenda
Kobayashi, K.; Smith, J.A.
Acyl-peptide hydrolase from rat liver. Characterization of enzyme reaction
J. Biol. Chem.
262
11435-11445
1987
Rattus norvegicus
brenda
Tsunasawa, S.; Imanaka, T.; Nakazawa, T.
Apparent dipeptidyl peptidase activities of acylamino acid-releasing enzymes
J. Biochem.
93
1217-1220
1983
Sus scrofa
brenda
Schoenberger, O.L.; Tschesche, H.
N-Acetylalanine aminopeptidase. A new enzyme from human erythrocytes
Hoppe-Seyler's Z. Physiol. Chem.
362
865-873
1981
Homo sapiens
brenda
Tsunasawa, S.; Narita, K.; Ogata, K.
Purification and properties of acylamino acid-releasing enzyme from rat liver
J. Biochem.
77
89-102
1975
Escherichia coli, Escherichia coli B / ATCC 11303, Gallus gallus, Oryctolagus cuniculus, Rattus norvegicus
brenda
Scaloni, A.; Ingallinella, P.; Andolfo, A.; Jones, W.; Marino, G.; Manning, J.M.
Structural investigations on human erythrocyte acylpeptide hydrolase by mass spectrometric procedures
J. Protein Chem.
18
349-360
1999
Homo sapiens
brenda
Jones, W.M.; Scaloni, A.; Manning, J.M.
Acylaminoacyl-peptidase
Methods Enzymol.
244
227-231
1994
Homo sapiens
brenda
Farries, T.C.; Auffret, A.D.; Aitken, A.
Enzyme-mediated peptide synthesis using acylpeptide hydrolase
Eur. J. Biochem.
196
687-692
1991
Ovis aries
brenda
Raphel, V.; Giardina, T.; Guevel, L.; Perrier, J.; Dupuis, L.; Guo, X.J.; Puigserver, A.
Cloning, sequencing and further characterization of acylpeptide hydrolase from porcine intestinal mucosa
Biochim. Biophys. Acta
1432
371-381
1999
Sus scrofa
brenda
Farries, T.C.; Harris, A.; Auffret, A.D.; Aitken, A.
Removal of N-acetyl groups from blocked peptides with acylpeptide hydrolase
Eur. J. Biochem.
196
679-685
1991
Ovis aries
brenda
Scaloni, A.; Jones, W.M.; Barra, D.; Pospischil, M.; Sassa, S.; Popowicz, A.; Manning, L.R.; Schneewind, O.; Manning, J.M.
Acylpeptide hydrolase: inhibitors and some active site residues of the human enzyme
J. Biol. Chem.
267
3811-3818
1992
Homo sapiens
brenda
Sharma, K.K.; Orthwerth, B.J.
Bovine lens acylpeptide hydrolase. Purification and characterization of a tetrameric enzyme resistant to urea denaturation and proteolytic inactivation
Eur. J. Biochem.
216
631-637
1993
Bos taurus
brenda
Scaloni, A.; Barra, D.; Jones, W.M.; Manning, J.M.
Human acylpeptide hydrolase. Studies on its thiol groups and mechanism of action
J. Biol. Chem.
269
15076-15084
1994
Homo sapiens
brenda
Sharma, K.K.; Kester, K.
Peptide hydrolysis in lens: role of leucine aminopeptidase, aminopeptidase III, prolyloligopeptidase and acylpeptidehydrolase
Curr. Eye Res.
15
363-369
1996
Bos taurus
brenda
Jones, W.M.; Scaloni, A.; Bossa, F.; Popowicz, A.M.; Schneewind, O.; Manning, J.M.
Genetic relationship between acylpeptide hydrolase and acylase, two hydrolytic enzymes with similar binding but different catalytic specificities
Proc. Natl. Acad. Sci. USA
88
2194-2198
1991
Homo sapiens
brenda
Radhakrishna, G.; Wold, F.
Purification and characterization of an N-acylaminoacyl-peptide hydrolase from rabbit muscle
J. Biol. Chem.
264
11076-11081
1989
Oryctolagus cuniculus
brenda
Chongcharoen, K.; Sharma, K.K.
Characterization of trypsin: modified bovine lens acylpeptide hydrolase
Biochem. Biophys. Res. Commun.
247
136-141
1998
Bos taurus
brenda
Krishna, R.G.; Wold, F.
Specificity determinants of acylaminoacyl-peptide hydrolase
Protein Sci.
1
582-589
1992
Oryctolagus cuniculus
brenda
Raphel, V.; Lupi, N.; Dupuis, L.; Puigserver, A.
The N-acylpeptide hydrolase from porcine intestine: isolation, subcellular localization and comparative hydrolysis of peptide and isopeptide bonds
Biochimie
75
891-897
1993
Sus scrofa
brenda
Mitta, M.; Miyagi, M.; Kato, I.; Tsunasawa, S.
Identification of the catalytic triad residues of porcine liver acylamino acid-releasing enzyme
J. Biochem.
123
924-931
1998
Sus scrofa
brenda
Miyagi, M.; Sakiyama, F.; Kato, I.; Tsunasawa, S.
Complete covalent structure of porcine liver acylamino acid-releasing enzyme and identification of its active site serine residue
J. Biochem.
118
771-779
1995
Sus scrofa
brenda
Feese, M.; Scaloni, A.; Jones, W.M.; Manning, J.M.; Remington, S.J.
Crystallization and preliminary X-ray studies of human erythrocyte acylpeptide hydrolase
J. Mol. Biol.
233
546-549
1993
Homo sapiens
brenda
Wang, G.; Gao, R.; Ding, Y.; Yang, H.; Cao, S.; Feng, Y.; Rao, Z.
Crystallization and preliminary crystallographic analysis of acylamino-acid releasing enzyme from the hyperthermophilic archaeon Aeropyrum pernix
Acta Crystallogr. Sect. D
58
1054-1055
2002
Aeropyrum pernix
brenda
Yamauchi, Y.; Ejiri, Y.; Toyoda, Y.; Tanaka, K.
Identification and biochemical characterization of plant acylamino acid-releasing enzyme
J. Biochem.
134
251-257
2003
Arabidopsis thaliana (Q84LM4), Arabidopsis thaliana, Cucumis sativus
brenda
Senthilkumar, R.; Sharma, K.K.
Effect of chaotropic agents on the structure-function of recombinant acylpeptide hydrolase
J. Protein Chem.
21
323-332
2002
Sus scrofa
brenda
Durand, A.; Villard, C.; Giardina, T.; Perrier, J.; Juge, N.; Puigserver, A.
Structural properties of porcine intestine acylpeptide hydrolase
J. Protein Chem.
22
183-191
2003
Sus scrofa
brenda
Richards, P.G.; Johnson, M.K.; Ray, D.E.
Identification of acylpeptide hydrolase as a sensitive site for reaction with organophosphorus compounds and a potential target for cognitive enhancing drugs
Mol. Pharmacol.
58
577-583
2000
Sus scrofa
brenda
Zhang, H.F.; Zheng, B.S.; Peng, Y.; Lou, Z.Y.; Feng, Y.; Rao, Z.H.
Expression, purification and crystal structure of a truncated acylpeptide hydrolase from Aeropyrum pernix K1
Acta Biochim. Biophys. Sin.
37
613-617
2005
Aeropyrum pernix K1
brenda
Wright, H.; Kiss, A.L.; Szeltner, Z.; Polgar, L.; Fueloep, V.
Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase
Acta Crystallogr. Sect. F
F61
942-944
2005
Sus scrofa
brenda
Perrier, J.; Durand, A.; Giardina, T.; Puigserver, A.
Catabolism of intracellular N-terminal acetylated proteins: involvement of acylpeptide hydrolase and acylase
Biochimie
87
673-685
2005
Homo sapiens, Sus scrofa, Rattus norvegicus
brenda
Kiss, A.L.; Szeltner, Z.; Fueloep, V.; Polgar, L.
His507 of acylaminoacyl peptidase stabilizes the active site conformation, not the catalytic intermediate
FEBS Lett.
571
17-20
2004
Sus scrofa
brenda
Wang, Q.; Yang, G.; Liu, Y.; Feng, Y.
Discrimination of esterase and peptidase activities of acylaminoacyl peptidase from hyperthermophilic Aeropyrum pernix K1 by a single mutation
J. Biol. Chem.
281
18618-18625
2006
Aeropyrum pernix (Q9YBQ2)
brenda
Bartlam, M.; Wang, G.; Yang, H.; Gao, R.; Zhao, X.; Xie, G.; Cao, S.; Feng, Y.; Rao, Z.
Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1
Structure
12
1481-1488
2004
Aeropyrum pernix (Q9YBQ2)
brenda
Quistad, G.B.; Klintenberg, R.; Casida, J.E.
Blood acylpeptide hydrolase activity is a sensitive marker for exposure to some organophosphate toxicants
Toxicol. Sci.
86
291-299
2005
Homo sapiens, Mus musculus
brenda
Edosada, C.Y.; Quan, C.; Wiesmann, C.; Tran, T.; Sutherlin, D.; Reynolds, M.; Elliott, J.M.; Raab, H.; Fairbrother, W.; Wolf, B.B.
Selective inhibition of fibroblast activation protein protease based on dipeptide substrate specificity
J. Biol. Chem.
281
7437-7444
2006
synthetic construct
brenda
Nishimura, M.; Ikeda, K.; Sugiyama, M.
Molecular cloning and characterization of gene encoding novel puromycin-inactivating enzyme from blasticidin S-producing Streptomyces morookaensis
J. Biosci. Bioeng.
101
63-69
2006
Streptomyces morookaense, Streptomyces morookaense JCM 4673
brenda
Kiss, A.L.; Hornung, B.; Radi, K.; Gengeliczki, Z.; Sztaray, B.; Juhasz, T.; Szeltner, Z.; Harmat, V.; Polgar, L.
The acylaminoacyl peptidase from Aeropyrum pernix K1 thought to be an exopeptidase displays endopeptidase activity
J. Mol. Biol.
368
509-520
2007
Aeropyrum pernix K1 (Q9YBQ2), Aeropyrum pernix K1
brenda
Yamin, R.; Bagchi, S.; Hildebrant, R.; Scaloni, A.; Widom, R.L.; Abraham, C.R.
Acyl peptide hydrolase, a serine proteinase isolated from conditioned medium of neuroblastoma cells, degrades the amyloid-beta peptide
J. Neurochem.
100
458-467
2007
Homo sapiens
brenda
Kiss, A.L.; Pallo, A.; Naray-Szabo, G.; Harmat, V.; Polgar, L.
Structural and kinetic contributions of the oxyanion binding site to the catalytic activity of acylaminoacyl peptidase
J. Struct. Biol.
162
312-323
2008
Aeropyrum pernix (Q9YBQ2), Aeropyrum pernix, Aeropyrum pernix K1 (Q9YBQ2)
brenda
Pancetti, F.; Olmos, C.; Dagnino-Subiabre, A.; Rozas, C.; Morales, B.
Noncholinesterase effects induced by organophosphate pesticides and their relationship to cognitive processes: implication for the action of acylpeptide hydrolase
J. Toxicol. Environ. Health B Crit. Rev.
10
623-630
2007
Sus scrofa, Homo sapiens
brenda
Zhang, Z.; Zheng, B.; Wang, Y.; Chen, Y.; Manco, G.; Feng, Y.
The conserved N-terminal helix of acylpeptide hydrolase from archaeon Aeropyrum pernix K1 is important for its hyperthermophilic activity
Biochim. Biophys. Acta
1784
1176-1183
2008
Aeropyrum pernix K1 (Q9YBQ2), Aeropyrum pernix K1
brenda
Szeltner, Z.; Kiss, A.L.; Domokos, K.; Harmat, V.; Naray-Szabo, G.; Polgar, L.
Characterization of a novel acylaminoacyl peptidase with hexameric structure and endopeptidase activity
Biochim. Biophys. Acta
1794
1204-1210
2009
Pyrococcus horikoshii (O58323), Pyrococcus horikoshii
brenda
Yang, G.; Bai, A.; Gao, L.; Zhang, Z.; Zheng, B.; Feng, Y.
Glu88 in the non-catalytic domain of acylpeptide hydrolase plays dual roles: charge neutralization for enzymatic activity and formation of salt bridge for thermodynamic stability
Biochim. Biophys. Acta
1794
94-102
2009
Aeropyrum pernix K1 (Q9YBQ2), Aeropyrum pernix K1
brenda
Boehme, L.; Baer, J.W.; Hoffmann, T.; Manhart, S.; Ludwig, H.H.; Rosche, F.; Demuth, H.U.
Isoaspartate residues dramatically influence substrate recognition and turnover by proteases
Biol. Chem.
389
1043-1053
2008
Sus scrofa
brenda
Olmos, C.; Sandoval, R.; Rozas, C.; Navarro, S.; Wyneken, U.; Zeise, M.; Morales, B.; Pancetti, F.
Effect of short-term exposure to dichlorvos on synaptic plasticity of rat hippocampal slices: involvement of acylpeptide hydrolase and alpha(7) nicotinic receptors
Toxicol. Appl. Pharmacol.
238
37-46
2009
Rattus norvegicus
brenda
Palmieri, G.; Langella, E.; Gogliettino, M.; Saviano, M.; Pocsfalvi, G.; Rossi, M.
A novel class of protease targets of phosphatidylethanolamine-binding proteins (PEBP): a study of the acylpeptide hydrolase and the PEBP inhibitor from the archaeon Sulfolobus solfataricus
Mol. Biosyst.
6
2498-2507
2010
Saccharolobus solfataricus (Q7LX61), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q7LX61)
brenda
Gogliettino, M.; Balestrieri, M.; Cocca, E.; Mucerino, S.; Rossi, M.; Petrillo, M.; Mazzella, E.; Palmieri, G.
Identification and characterisation of a novel acylpeptide hydrolase from Sulfolobus solfataricus: structural and functional insights
PLoS One
7
e37921
2012
Saccharolobus solfataricus (Q97VD6), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97VD6)
brenda
Zhou, X.; Wang, H.; Zhang, Y.; Gao, L.; Feng, Y.
Alteration of substrate specificities of thermophilic alpha/beta hydrolases through domain swapping and domain interface optimization
Acta Biochim. Biophys. Sin.
44
965-973
2012
Aeropyrum pernix (Q9YBQ2)
brenda
Li, R.; Zhang, F.; Cao, S.-G.; Xie, G.-Q.; Gao, R.J.
Expression and characterization of a thermostable acyl-peptide releasing enzyme ST0779 from Sulfolobus tokodaii
Chem. Res. Chin. Univ.
28
851-855
2012
Sulfurisphaera tokodaii (Q973W9), Sulfurisphaera tokodaii 7 (Q973W9)
-
brenda
Menyhard, D.K.; Kiss-Szeman A.; Tichy-Racs, E.; Hornung, B.; Radi, K.; Szeltner, Z.; Domokos, K., Szamosi, I.; Naray-Szabo, G.; Polgar, L.; Harmat, V.
A self-compartmentalizing hexamer serine protease from Pyrococcus horikoshii: substrate selection achieved through multimerization
J. Biol. Chem.
288
17884-17894
2013
Pyrococcus horikoshii (O58323), Pyrococcus horikoshii DSM 12428 (O58323)
brenda
Palmieri, G.; Bergamo, P.; Luini, A.; Ruvo, M.; Gogliettino, M.; Langella, E.; Saviano, M.; Hegde, R.N.; Sandomenico, A.; Rossi, M.
Acylpeptide hydrolase inhibition as targeted strategy to induce proteasomal down-regulation
PLoS One
6
e25888
2011
Saccharolobus solfataricus
brenda
Harmat, V.; Domokos, K.; Menyhard, D.K.; Pallo, A.; Szeltner, Z.; Szamosi, I.; Beke-Somfai, T.; Naray-Szabo, G., Polgar, L.
Structure and catalysis of acylaminoacyl peptidase: closed and open subunits of a dimer oligopeptidase
J. Biol. Chem.
286
1987-1998
2011
Aeropyrum pernix (Q9YBQ2), Aeropyrum pernix, Aeropyrum pernix DSM 11879 (Q9YBQ2)
brenda
Papaleo, E.; Renzetti, G.
Coupled motions during dynamics reveal a tunnel toward the active site regulated by the N-terminal alpha-helix in an acylaminoacyl peptidase
J. Mol. Graph. Model.
38
226-234
2012
Aeropyrum pernix (Q9YBQ2), Aeropyrum pernix DSM 11879 (Q9YBQ2)
brenda
Liu, C.; Yang, G.; Wu, L.; Tian, G.; Zhang, Z.; Feng, Y.
Switch of substrate specificity of hyperthermophilic acylaminoacyl peptidase by combination of protein and solvent engineering
Protein Cell
2
497-506
2011
Aeropyrum pernix (Q9YBQ2), Aeropyrum pernix DSM 11879 (Q9YBQ2)
brenda
Are, V.; Ghosh, B.; Kumar, A.; Yadav, P.; Bhatnagar, D.; Jamdar, S.; Makde, R.
Expression, purification, crystallization and preliminary X-ray diffraction analysis of acylpeptide hydrolase from Deinococcus radiodurans
Acta Crystallogr. Sect. F
70
1292-1295
2014
Deinococcus radiodurans
brenda
Papaleo, E.; Parravicini, F.; Grandori, R.; De Gioia, L.; Brocca, S.
Structural investigation of the cold-adapted acylaminoacyl peptidase from Sporosarcina psychrophila by atomistic simulations and biophysical methods
Biochim. Biophys. Acta
1844
2203-2213
2014
Deinococcus radiodurans
brenda
Gogliettino, M.; Riccio, A.; Balestrieri, M.; Cocca, E.; Facchiano, A.; DArco, T.M.; Tesoro, C.; Rossi, M.; Palmieri, G.
A novel class of bifunctional acylpeptide hydrolases--potential role in the antioxidant defense systems of the Antarctic fish Trematomus bernacchii
FEBS J.
281
401-415
2014
Trematomus bernacchii, Trematomus bernacchii (V5QZ74)
brenda
Santhoshkumar, P.; Xie, L.; Raju, M.; Reneker, L.; Sharma, K.K.
Lens crystallin modifications and cataract in transgenic mice overexpressing acylpeptide hydrolase
J. Biol. Chem.
289
9039-9052
2014
Mus musculus
brenda
Sandoval, R.; Navarro, S.; Garcia-Rojo, G.; Calderon, R.; Pedrero, A.; Sandoval, S.; Wyneken, U.; Pancetti, F.
Synaptic localization of acylpeptide hydrolase in adult rat telencephalon
Neurosci. Lett.
520
98-103
2012
Rattus norvegicus
brenda
Nakai, A.; Yamauchi, Y.; Sumi, S.; Tanaka, K.
Role of acylamino acid-releasing enzyme/oxidized protein hydrolase in sustaining homeostasis of the cytoplasmic antioxidative system
Planta
236
427-436
2012
Arabidopsis thaliana
brenda
Papaleo, E.; Renzetti, G.; Tiberti, M.
Mechanisms of intramolecular communication in a hyperthermophilic acylaminoacyl peptidase: a molecular dynamics investigation
PLoS ONE
7
e35686
2012
Sporosarcina psychrophila
brenda
Yu, X.; Prez, B.; Zhang, Z.; Gao, R.; Guo, Z.
Mining catalytic promiscuity from thermophilic archaea: an acyl-peptide releasing enzyme from Sulfolobus tokodaii (ST0779) for nitroaldol reactions
Green Chem.
18
2753-2761
2016
Sulfurisphaera tokodaii (Q973W9), Sulfurisphaera tokodaii 7 (Q973W9), Sulfurisphaera tokodaii DSM 16993 (Q973W9), Sulfurisphaera tokodaii JCM 10545 (Q973W9), Sulfurisphaera tokodaii NBRC 100140 (Q973W9)
-
brenda
Ishikawa, K.; Ishida, H.; Koyama, Y.; Kawarabayasi, Y.; Kawahara, J.; Matsui, E.; Matsui, I.
Acylamino acid-releasing enzyme from the thermophilic archaeon Pyrococcus horikoshii
J. Biol. Chem.
273
17726-17731
1998
Pyrococcus horikoshii (AB009494), Pyrococcus horikoshii
brenda
Menyhard, D.K.; Orgovan, Z.; Szeltner, Z.; Szamosi, I.; Harmat, V.
Catalytically distinct states captured in a crystal lattice the substrate-bound and scavenger states of acylaminoacyl peptidase and their implications for functionality
Acta Crystallogr. Sect. D
71
461-472
2015
Aeropyrum pernix (Q9YBQ2), Aeropyrum pernix, Aeropyrum pernix ATCC 700893 (Q9YBQ2), Aeropyrum pernix DSM 11879 (Q9YBQ2), Aeropyrum pernix JCM 9820 (Q9YBQ2), Aeropyrum pernix NBRC 100138 (Q9YBQ2)
brenda
Li, R.; Perez, B.; Jian, H.; Jensen, M.M.; Gao, R.; Dong, M.; Glasius, M.; Guo, Z.
Characterization and mechanism insight of accelerated catalytic promiscuity of Sulfolobus tokodaii (ST0779) peptidase for aldol addition reaction
Appl. Microbiol. Biotechnol.
99
9625-9634
2015
Sulfurisphaera tokodaii (Q973W9), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7T (Q973W9), Sulfurisphaera tokodaii JCM 10545 (Q973W9)
brenda
Liu, D.; Deng, L.; Wang, D.; Li, W.; Gao, R.
"Bridge regions" regulate catalysis and protein stability of acylpeptide hydrolase
Biochem. Eng. J.
145
42-52
2019
Aeropyrum pernix (Q9YBQ2), Aeropyrum pernix ATCC 700893 (Q9YBQ2), Aeropyrum pernix DSM 11879 (Q9YBQ2), Aeropyrum pernix JCM 9820 (Q9YBQ2), Aeropyrum pernix NBRC 100138 (Q9YBQ2), Sulfurisphaera tokodaii (Q973W9), Sulfurisphaera tokodaii 7 (Q973W9), Sulfurisphaera tokodaii DSM 16993 (Q973W9), Sulfurisphaera tokodaii JCM 10545 (Q973W9), Sulfurisphaera tokodaii NBRC 100140 (Q973W9)
-
brenda
Yu, X.; Wang, Q.; Zhou, Y.; Gao, R.; Wang, Y.
Cloning and application of a new acylaminoacyl peptidase from Bacillus subtilis 168 for aldol reaction
Chem. J. Chin. Univ.
36
2454-2460
2015
Bacillus subtilis (A8CWI2), Bacillus subtilis 168 (A8CWI2)
-
brenda
Zeng, Z.; Rulten, S.; Breslin, C.; Zlatanou, A.; Coulthard, V.; Caldecott, K.
Acylpeptide hydrolase is a component of the cellular response to DNA damage
DNA Repair
58
52-61
2017
Homo sapiens (P13798), Homo sapiens
brenda
Brocca, S.; Ferrari, C.; Barbiroli, A.; Pesce, A.; Lotti, M.; Nardini, M.
A bacterial acyl aminoacyl peptidase couples flexibility and stability as a result of cold adaptation
FEBS J.
283
4310-4324
2016
Sporosarcina psychrophila (E1VFE0), Sporosarcina psychrophila
brenda
Fu, P.; Sun, W.; Zhang, Z.
Molecular cloning, expression and characterization of acylpeptide hydrolase in the silkworm, Bombyx mori
Gene
580
8-16
2016
Bombyx mori (A0A0X9PFK4), Bombyx mori
brenda
Jin, H.; Zhou, Z.; Wang, D.; Guan, S.; Han, W.
Molecular dynamics simulations of acylpeptide hydrolase bound to chlorpyrifosmethyl oxon and dichlorvos
Int. J. Mol. Sci.
16
6217-6234
2015
Aeropyrum pernix (Q9YBQ2)
brenda
Wang, D.; Jin, H.; Wang, J.; Guan, S.; Zhang, Z.; Han, W.
Exploration of the chlorpyrifos escape pathway from acylpeptide hydrolases using steered molecular dynamics simulations
J. Biomol. Struct. Dyn.
34
749-761
2016
Aeropyrum pernix (Q9YBQ2)
brenda
Zhu, J.; Wang, Y.; Li, X.; Han, W.; Zhao, L.
Understanding the interactions of different substrates with wild-type and mutant acylaminoacyl peptidase using molecular dynamics simulations
J. Biomol. Struct. Dyn.
36
4285-4302
2018
Aeropyrum pernix (Q9YBQ2), Aeropyrum pernix ATCC 700893 (Q9YBQ2), Aeropyrum pernix DSM 11879 (Q9YBQ2), Aeropyrum pernix JCM 9820 (Q9YBQ2), Aeropyrum pernix NBRC 100138 (Q9YBQ2), Homo sapiens (P13798), Homo sapiens
brenda
Jin, H.; Zhu, J.; Dong, Y.; Han, W.
Exploring the different ligand escape pathways in acylaminoacyl peptidase by random acceleration and steered molecular dynamics simulations
RSC Adv.
6
10987-10996
2016
Aeropyrum pernix (Q9YBQ2)
-
brenda
Walczak, M.; Chryplewicz, A.; Olewinska, S.; Psurski, M.; Winiarski, L.; Torzyk, K.; Oleksyszyn, J.; Sienczyk, M.
Phosphonic analogs of alanine as acylpeptide hydrolase inhibitors
Chem. Biodivers.
18
e2001004
2021
Sus scrofa
brenda
Tyler, K.; Geilman, S.; Bell, D.M.; Taylor, N.; Honeycutt, S.C.; Garrett, P.I.; Hillhouse, T.M.; Covey, T.M.
Acyl peptide enzyme hydrolase (APEH) activity is inhibited by lipid metabolites and peroxidation products
Chem. Biol. Interact.
348
109639
2021
Mus musculus (Q8R146), Homo sapiens (P13798)
brenda
Kiss-Szeman, A.J.; Takacs, L.; Orgovan, Z.; Straner, P.; Jakli, I.; Schlosser, G.; Masiulis, S.; Harmat, V.; Menyhard, D.K.; Perczel, A.
A carbapenem antibiotic inhibiting a mammalian serine protease structure of the acylaminoacyl peptidase-meropenem complex
Chem. Sci.
13
14264-14276
2022
Sus scrofa (P19205)
brenda
Kiss-Szeman, A.J.; Straner, P.; Jakli, I.; Hosogi, N.; Harmat, V.; Menyhard, D.K.; Perczel, A.
Cryo-EM structure of acylpeptide hydrolase reveals substrate selection by multimerization and a multi-state serine-protease triad
Chem. Sci.
13
7132-7142
2022
Sus scrofa (P19205)
brenda
Mangiagalli, M.; Barbiroli, A.; Santambrogio, C.; Ferrari, C.; Nardini, M.; Lotti, M.; Brocca, S.
The activity and stability of a cold-active acylaminoacyl peptidase rely on its dimerization by domain swapping
Int. J. Biol. Macromol.
181
263-274
2021
Sporosarcina psychrophila (E1VFE0)
brenda
Tsortouktzidis, D.; Grundke, K.; Till, C.; Korwitz-Reichelt, A.; Sass, J.O.
Acylpeptide hydrolase (APEH) sequence variants with potential impact on the metabolism of the antiepileptic drug valproic acid
Metab. Brain Dis.
34
1629-1634
2019
Homo sapiens (P13798)
brenda
Elahi, R.; Dapper, C.; Klemba, M.
Internalization of erythrocyte acylpeptide hydrolase is required for asexual replication of Plasmodium falciparum
mSphere
4
e00077-19
2019
Homo sapiens (P13798)
brenda
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