3.4.19.1: acylaminoacyl-peptidase
This is an abbreviated version!
For detailed information about acylaminoacyl-peptidase, go to the full flat file.
Word Map on EC 3.4.19.1
-
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
- 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
cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide =
Synonyms
AAP, AARE, AARE/OPH, AAREP, AcpH, acyl aminoacyl peptidase, acyl peptide hydrolase, Acyl-peptide hydrolase, acyl-peptide releasing enzyme, acylamino acid-releasing enzyme, acylamino acid-releasing enzyme/oxidized protein hydrolase, acylamino-acid-releasing enzyme, acylaminoacyl peptidase, Acylaminoacyl-peptidase, acylpeptide hydrolase, acylpeptide hydrolase/esterase, alpha-N-acylpeptide hydrolase, ApAAP, apAPH, APEH, APEH-1, apeH-2, APEH-3, APEH-3Ss, APEHs, APE_1547.1, APH, APHdr, AtAARE, BmAPH, cAARE, DNF15S2 protein, N-acylaminoacyl-peptide hydrolase, N-acylpeptide hydrolase, N-formylmethionine (fMet) aminopeptidase, OP85, PhAAP, pi-APH, PM hydrolase, PMH, SpAAP, sso2141, SSO2693, ST0779, yuxL
ECTree
3.4.19.1 acylaminoacyl-peptidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.19.1 - acylaminoacyl-peptidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala + H2O
2-aminobenzoyl-Ala-Leu-Phe + Gln-Gly-Pro-Phe(NO2)-Ala
2-aminobenzoyl-GFEPF(NO2)RA + H2O
?
good substrate, displays greater kinetic specificity than acetyl-Phe-2-naphthylamide
-
-
?
Ac-Ala-7-amido-4-methylcoumarin + H2O
N-acetyl-L-Ala + 7-amino-4-methylcoumarin
-
-
-
?
Ac-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
-
-
-
?
Ac-Phe-2-naphthylamide + H2O
N-acetyl-L-Phe + 2-naphthylamine
-
-
-
?
Ac-Phe-4-nitroanilide + H2O
N-acetyl-L-Phe + 4-nitroaniline
-
-
-
?
acetyl-Ala-7-amido-4-methylcoumarin + H2O
?
very slow hydrolysis
-
-
?
acetyl-Ala-7-amido-4-methylcoumarin + H2O
acetyl-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O
acetyl-Ala + Ala-Ala-Ala-Ala-Ala
AB009494
-
-
-
?
acetyl-Ala-Met + H2O
acetyl-Ala + Met
-
native enzyme shows 70.4% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Gly-Leu + H2O
acetyl-Gly + Leu
-
native enzyme shows 30.3% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Met-7-amido-4-methylcoumarin + H2O
acetyl-Met + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-Met-Ala-Ala-Ala-Ala-Ala + H2O
acetyl-Met + Ala-Ala-Ala-Ala-Ala
AB009494
-
-
-
?
acetyl-Met-Asn + H2O
acetyl-Met + Asn
-
native enzyme shows 34.1% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Met-Phe + H2O
acetyl-Met + Phe
native enzyme shows 5% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Phe-2-naphthylamide + H2O
?
classical substrate of AAP
-
-
?
acetyl-Phe-2-naphthylamide + H2O
acetyl-Phe + 2-naphthylamine
-
-
-
?
acetyl-Phe-4-nitroanilide + H2O
acetyl-Phe + 4-nitroaniline
specificity rate constant is lower by one order of magnitude for acetyl-Leu-4-nitroanilide than for acetyl-Phe-4-nitroanilide
-
-
?
acetyl-Tyr-4-nitroanilide + H2O
acetyl-Tyr + 4-nitroaniline
AB009494
-
-
-
?
formyl-Ala-Ala-Ala-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala-Ala-Ala-Ala
AB009494
-
-
-
?
formyl-Gly-Val + H2O
formyl-Gly + Val
-
native enzyme shows 30.3% of the activity compared to acetyl-Ala-Ala as substrate
-
?
formyl-Met-Ala-Ala-Ala-Ala-Ala + H2O
formyl-Met + Ala-Ala-Ala-Ala-Ala
AB009494
-
-
-
?
formylmethionine-beta-naphthylamide + H2O
formylmethionine + beta-naphthylamine
-
-
-
-
?
glutaryl-GGF-7-amido-4-methylcoumarin + H2O
?
has a rate constant comparable to that of acetyl-Phe-2-naphthylamide
-
-
?
glycated ribulose-1,5-diphosphate carboxylase/oxygenase protein + H2O
?
-
no degradation of the native protein
-
?
N-acetyl-Ala-beta-naphthylamide + H2O
N-acetyl-Ala + beta-naphthylamine
-
-
-
-
?
N-acetyl-L-alanine 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
-
-
-
-
?
N-acetyl-L-Met-epsilon-L-Lys-Ala-NH2 + H2O
N-acetyl-L-Met + L-Lys-L-Ala-NH2
-
-
-
?
N-acetyl-L-Phe-4-nitroanilide + H2O
N-acetyl-L-Phe + 4-nitroaniline
-
-
-
?
N-acetyl-Leu p-nitroanilide + H2O
N-acetyl-Leu + p-nitroaniline
-
-
-
-
?
N-acetyl-Leu-4-nitroanilide + H2O
N-acetyl-Leu + 4-nitroaniline
-
-
-
-
?
N-acetyl-Leu-p-nitroanilide + H2O
N-acetyl-Leu + p-nitroaniline
esterase activity of wild-type enzyme with p-nitrophenyl caprylate as substrate is 7times higher than peptidase activity with N-acetyl-Leu-p-nitroanilide as substrate, 150fold higher for mutant enzyme R526V, peptidase activity for mutant R526E is abolished
-
-
?
N-acetyl-Phe-2-naphthylamide + H2O
N-acetyl-L-Phe + 2-naphthylamine
kinetic assay
-
-
?
N-acetyl-Tyr p-nitroanilide + H2O
N-acetyl-Tyr + p-nitroaniline
-
-
-
-
?
N-acylpeptide + H2O
?
-
acylpeptide hydrolase catalyzes the hydrolysis of short peptides of the type Nalpha-acyl to form an acyl amino acid and a peptide with a free N-terminus
-
-
?
p-nitrophenyl caprylate + H2O
nitrophenol + caprylate
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
-
-
?
Phe-p-nitroanilide + H2O
Phe + p-nitroaniline
-
prefered substrate for PMH
-
-
?
succinyl-AAA-4-nitroanilide + H2O
succinyl-AAA + 4-nitroaniline
-
-
-
?
succinyl-AAPF-2-naphthylamide + H2O
?
hydrolysed at a significantly slower rate than acetyl-Phe-2-naphthylamide
-
-
?
succinyl-GGF-4-nitroanilide + H2O
succinyl-GGF + 4-nitroaniline
-
-
-
?
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala + H2O
2-aminobenzoyl-Ala-Leu-Phe + Gln-Gly-Pro-Phe(NO2)-Ala
endopeptidase activity
-
-
?
2-aminobenzoyl-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala + H2O
2-aminobenzoyl-Ala-Leu-Phe + Gln-Gly-Pro-Phe(NO2)-Ala
endopeptidase activity
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
high activity
-
-
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
high activity
-
-
?
Ac-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala
high activity
-
-
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
-
-
-
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
-
-
-
?
Ac-Ala-Ala-Ala-Ala + H2O
Ac-Ala + Ala-Ala-Ala
-
-
-
?
Ac-Leu-p-nitroanilide + H2O
Ac-Leu + p-nitroaniline
substrate peptidase assay
-
-
?
Ac-Leu-p-nitroanilide + H2O
Ac-Leu + p-nitroaniline
-
substrate peptidase assay
-
-
?
acetyl-Ala-4-nitroanilide + H2O
acetyl-Ala + 4-nitroaniline
AB009494
the enzyme releases acetyl-Leu better than acetyl-Ala from acetyl-amino acid-4-nitroanilides
-
-
?
acetyl-Ala-4-nitroanilide + H2O
acetyl-Ala + 4-nitroaniline
-
-
-
?
Acetyl-Ala-Ala-Ala + H2O
Acetyl-Ala + Ala-Ala
native enzyme shows 81% of the activity compared to acetyl-Ala-Ala as substrate
-
?
Acetyl-Ala-Ala-Ala + H2O
Acetyl-Ala + Ala-Ala
-
native enzyme shows 147% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Ala-Ala-Ala-Ala + H2O
acetyl-Ala + Ala-Ala-Ala
native enzyme shows 126% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Ala-Ala-Ala-Ala + H2O
acetyl-Ala + Ala-Ala-Ala
-
native enzyme shows 85.6% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Gly-Gly + H2O
acetyl-Gly + Gly
native enzyme shows 4% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Gly-Gly + H2O
acetyl-Gly + Gly
-
native enzyme shows 37% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Leu-4-nitroanilide + H2O
acetyl-Leu + 4-nitroaniline
specificity rate constant is lower by one order of magnitude for acetyl-Leu-4-nitroanilide than for acetyl-Phe-4-nitroanilide
-
-
?
acetyl-Leu-4-nitroanilide + H2O
acetyl-Leu + 4-nitroaniline
AB009494
the enzyme releases acetyl-Leu better than acetyl-Ala from acetyl-amino acid-4-nitroanilides
-
-
?
acetyl-Leu-4-nitroanilide + H2O
acetyl-Leu + 4-nitroaniline
-
-
-
?
acetyl-Met-Ala + H2O
acetyl-Met + Ala
native enzyme shows 45% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Met-Ala + H2O
acetyl-Met + Ala
-
native enzyme shows 4% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Met-Glu + H2O
acetyl-Met + Glu
native enzyme shows 6% of the activity compared to acetyl-Ala-Ala as substrate
-
?
acetyl-Met-Glu + H2O
acetyl-Met + Glu
-
native enzyme shows 4.3% of the activity compared to acetyl-Ala-Ala as substrate
-
?
Ala-beta-naphthylamide + H2O
Ala + 2-naphthylamine
-
-
-
-
?
Ala-p-nitroanilide + H2O
Ala + p-nitroaniline
-
prefered substrate for PMH
-
-
?
Ala-p-nitroanilide + H2O
Ala + p-nitroaniline
-
prefered substrate for PMH
-
-
?
butyryl-Ala-Ala-Ala + H2O
butyryl-Ala + Ala-Ala
native enzyme shows 77% of the activity compared to acetyl-Ala-Ala as substrate
-
?
butyryl-Ala-Ala-Ala + H2O
butyryl-Ala + Ala-Ala
-
native enzyme shows 33.6% of the activity compared to acetyl-Ala-Ala as substrate
-
?
formyl-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala
native enzyme shows 81% of the activity compared to acetyl-Ala-Ala as substrate
-
?
formyl-Ala-Ala-Ala + H2O
formyl-Ala + Ala-Ala
-
native enzyme shows 62.4% of the activity compared to acetyl-Ala-Ala as substrate
-
?
Leu-beta-naphthylamide + H2O
Leu + 2-naphthylamine
-
-
-
-
?
N-acetyl-Ala p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
-
-
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
-
N-acetyl-Ala-Ala-Ala
-
?
N-acetyl-Ala-p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Met-p-nitranilide, N-acetyl-Gly-p-nitranilide
-
?
N-acetyl-Ala-p-nitroanilide + H2O
N-acetyl-Ala + p-nitroaniline
-
substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Gly-p-nitranilide, N-acetyl-Met-p-nitranilide
-
?
N-acetyl-Gly-p-nitroanilide + H2O
N-acetyl-Gly + p-nitroaniline
substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Met-p-nitranilide, N-acetyl-Gly-p-nitranilide
-
?
N-acetyl-Gly-p-nitroanilide + H2O
N-acetyl-Gly + p-nitroaniline
-
substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Gly-p-nitranilide, N-acetyl-Met-p-nitranilide
-
?
N-acetyl-L-Ala-4-nitroanilide + H2O
N-acetyl-L-Ala + 4-nitroaniline
-
-
-
?
N-acetyl-L-Ala-4-nitroanilide + H2O
N-acetyl-L-Ala + 4-nitroaniline
-
-
-
?
N-acetyl-L-alanyl 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
-
-
-
?
N-acetyl-L-alanyl 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
-
-
-
?
N-acetyl-L-alanyl 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
-
-
-
?
N-acetyl-L-alanyl 4-nitroanilide + H2O
N-acetyl-L-alanine + 4-nitroaniline
-
-
-
?
N-acetyl-L-alanyl-p-nitroanilide + H2O
N-acetyl-L-alanine + p-nitroaniline
-
-
-
-
?
N-acetyl-L-alanyl-p-nitroanilide + H2O
N-acetyl-L-alanine + p-nitroaniline
-
-
-
-
?
N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
-
-
-
?
N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
Aeropyrum pernix ATCC 700893
-
-
-
?
N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
-
-
-
?
N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
Aeropyrum pernix JCM 9820
-
-
-
?
N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
Aeropyrum pernix NBRC 100138
-
-
-
?
N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
-
-
-
?
N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
-
-
-
?
N-acetyl-L-leucyl 4-nitroanilide + H2O
N-acetyl-L-leucine + 4-nitroaniline
-
-
-
?
N-acetyl-L-leucyl 4-nitroanilide + H2O
N-acetyl-L-leucine + 4-nitroaniline
preference for N-acetyl-L-leucyl 4-nitroanilide over N-acetyl-L-alanyl 4-nitroanilide
-
-
?
N-acetyl-L-leucyl 4-nitroanilide + H2O
N-acetyl-L-leucine + 4-nitroaniline
preference for N-acetyl-L-leucyl 4-nitroanilide over N-acetyl-L-alanyl 4-nitroanilide
-
-
?
N-acetyl-L-leucyl 4-nitroanilide + H2O
N-acetyl-L-leucine + 4-nitroaniline
-
-
-
?
N-acetyl-L-phenylalanyl 4-nitroanilide + H2O
N-acetyl-L-phenylalanine + 4-nitroaniline
-
-
-
?
N-acetyl-L-phenylalanyl 4-nitroanilide + H2O
N-acetyl-L-phenylalanine + 4-nitroaniline
-
-
-
?
N-acetyl-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
switch of substrate specificity of hyperthermophilic promiscuous acylaminoacyl peptidase by combination of protein and solvent engineering into a specific carboxylesterase
-
-
?
N-acetyl-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
switch of substrate specificity of hyperthermophilic promiscuous acylaminoacyl peptidase by combination of protein and solvent engineering into a specific carboxylesterase
-
-
?
N-acetyl-Met-p-nitroanilide + H2O
N-acetyl-Met + p-nitroaniline
substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Met-p-nitranilide, N-acetyl-Gly-p-nitranilide
-
?
N-acetyl-Met-p-nitroanilide + H2O
N-acetyl-Met + p-nitroaniline
-
substrates in the order of catalytic efficiency: N-acetyl-Ala-p-nitranilide, N-acetyl-Gly-p-nitranilide, N-acetyl-Met-p-nitranilide
-
?
N-acetyl-Phe-2-naphthylamide + H2O
N-acetyl-Phe + 2-naphthylamine
-
-
-
?
N-acetyl-Phe-2-naphthylamide + H2O
N-acetyl-Phe + 2-naphthylamine
-
-
-
?
additional information
?
-
hundreds nanosecond all-atom atomistic molecular dynamics simulations of a representative member of the acylaminoacyl peptidase subfamily (Aeropyrum pernix K1) allow to identify the presence of a tunnel which from the surrounding of the N-terminal alpha1-helix bring to the catalytic site and it is regulated by conformational changes of the N-terminal alpha-helix itself and its surroundings in the native conformational ensemble
-
-
?
additional information
?
-
acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments
-
-
?
additional information
?
-
-
acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments
-
-
?
additional information
?
-
enzyme APH catalyzes the N-terminal hydrolysis of Nalpha-acylpeptides to release Nalpha-acylated amino acids
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
Aeropyrum pernix ATCC 700893
acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments
-
-
?
additional information
?
-
Aeropyrum pernix ATCC 700893
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
-
-
?
additional information
?
-
hundreds nanosecond all-atom atomistic molecular dynamics simulations of a representative member of the acylaminoacyl peptidase subfamily (Aeropyrum pernix K1) allow to identify the presence of a tunnel which from the surrounding of the N-terminal alpha1-helix bring to the catalytic site and it is regulated by conformational changes of the N-terminal alpha-helix itself and its surroundings in the native conformational ensemble
-
-
?
additional information
?
-
acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
Aeropyrum pernix JCM 9820
acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments
-
-
?
additional information
?
-
Aeropyrum pernix JCM 9820
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
-
-
?
additional information
?
-
removal of an N-acylated amino acid from blocked peptides
-
-
?
additional information
?
-
-
removal of an N-acylated amino acid from blocked peptides
-
-
?
additional information
?
-
removal of an N-acylated amino acid from blocked peptides
-
-
?
additional information
?
-
-
removal of an N-acylated amino acid from blocked peptides
-
-
?
additional information
?
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Aeropyrum pernix NBRC 100138
acylaminoacyl peptidase (AAP) is an oligopeptidase that only cleaves short peptides or protein segments
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Aeropyrum pernix NBRC 100138
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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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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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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the trypsin-modified enzyme is able to unblock alphaA-crystallin and displays endoprotease activity unlike the native enzyme
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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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the enzyme may be involved in N-terminal deacylation of nascent polypeptide chains and of bioactive peptides
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APEH interacts with the amino-terminal domain of XRCC1
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APEH interacts with the amino-terminal domain of XRCC1
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acylpeptide hydrolase (APEH) deacetylates N-alpha-acetylated peptides and selectively degrades oxidised protein
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acylpeptide hydrolase (APEH) deacetylates N-alpha-acetylated peptides and selectively degrades oxidised protein
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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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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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cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
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cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
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AB009494
high hydrolytic activity for acylpeptides, no hydrolytic activity for Leu-4-nitroanilide and Ala-4-nitroanilide
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high hydrolytic activity for acylpeptides, no hydrolytic activity for Leu-4-nitroanilide and Ala-4-nitroanilide
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specific for N-terminal acylmethionine residues
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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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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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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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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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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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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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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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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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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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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
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additional information
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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
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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
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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peptidase activity is only exerted on peptides with Gly or Ala at their N-termini
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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
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the enzyme may be involved in regulation of neuropeptide turnover
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His507 of acylaminoacyl peptidase stabilizes the active site conformation, not the catalytic intermediate
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catalyzes the NH2-terminal hydrolysis of N-acylpeptides to release N-acylated amino acids
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