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Information on EC 3.4.19.1 - acylaminoacyl-peptidase and Organism(s) Homo sapiens and UniProt Accession P13798
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3.4.19.1 acylaminoacyl-peptidaseSpecify your search results
Word Map
- 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
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide
Synonyms
apaap, acylpeptide hydrolase, acylaminoacyl peptidase, acylamino acid-releasing enzyme, acyl-peptide hydrolase, spaap, aphdr, acyl peptide hydrolase, apaph, aare/oph, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Acyl-peptide hydrolase
-
-
-
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acylamino-acid-releasing enzyme
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-
-
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Acylaminoacyl-peptidase
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-
-
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alpha-N-acylpeptide hydrolase
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-
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DNF15S2 protein
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-
-
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N-acylaminoacyl-peptide hydrolase
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-
-
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N-acylpeptide hydrolase
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-
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N-formylmethionine (fMet) aminopeptidase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
CAS REGISTRY NUMBER
COMMENTARY
73562-30-8
-
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
N-acetyl-L-Leu-4-nitroanilide + H2O
N-acetyl-L-Leu + 4-nitroaniline
-
-
-
?
N-acetyl-L-alanyl-p-nitroanilide + H2O
N-acetyl-L-alanine + p-nitroaniline
-
-
-
-
?
N-acetyl-Ala-Ala-Ala + H2O
N-acetyl-Ala + Ala-Ala
-
N-acetyl-Ala-Ala-Ala
-
?
additional information
?
-
APEH interacts with the amino-terminal domain of XRCC1
-
-
?
additional information
?
-
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APEH interacts with the amino-terminal domain of XRCC1
-
-
?
additional information
?
-
acylpeptide hydrolase (APEH) deacetylates N-alpha-acetylated peptides and selectively degrades oxidised protein
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-
?
additional information
?
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acylpeptide hydrolase (APEH) deacetylates N-alpha-acetylated peptides and selectively degrades oxidised protein
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-
?
additional information
?
-
-
the enzyme may be involved in N-terminal deacylation of nascent polypeptide chains and of bioactive peptides
-
-
?
NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
APEH interacts with the amino-terminal domain of XRCC1
-
-
?
additional information
?
-
-
APEH interacts with the amino-terminal domain of XRCC1
-
-
?
additional information
?
-
-
the enzyme may be involved in N-terminal deacylation of nascent polypeptide chains and of bioactive peptides
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-nitrophenyl-N-propyl carbamate
-
potent active site-directed, pseudo-first-order kinetics
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0015
2-(pentylsulfanyl)-4H-1,3,2-benzodioxaphosphinine 2-oxide
Homo sapiens
-
IC50: 0.0015 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.4
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
APH expression in Alzheimers disease brain is lower than in age-matched controls
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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
-
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
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ACPH_HUMAN
732
0
81225
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
structural investigations of the enzyme by mass spectrometric procedures
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the TOPO-V5/His tag mammalian expression vector. Wild-type and mutant APH constructs transfected into COS-7 or SK-N-MC cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
blood acylpeptide hydrolase activity is a sensitive marker for exposure to some organophosphate toxicants
medicine
-
reliable biomarker for some organophosphate pesticides that show higher specificity for acylpeptide hydrolase than for cholinesterases
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
Jones, W.M.; Scaloni, A.; Manning, J.M.
Acylaminoacyl-peptidase
Methods Enzymol.
244
227-231
1994
Homo sapiens
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
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
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
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
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, Rattus norvegicus, Sus scrofa
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
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
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
Homo sapiens, Sus scrofa
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
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
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