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Enzyme Nomenclature
Information on EC 3.4.11.1 - leucyl aminopeptidase
for references in articles please use BRENDA:EC3.4.11.1
Word Map on EC 3.4.11.1
- 3.4.11.1
-
aminopeptidases
- border
- renal
-
brush
- trypsin
- bestatin
-
gamma-glutamyl
- transpeptidase
- maltase
- sucrase
-
histochemical
- lactate
-
carboxypeptidase
- urinary
- urine
-
esterase
- pregnancy
- bile
- mucosa
- chymotrypsin
-
transaminase
-
trim
-
exopeptidase
-
brush-border
-
dipeptidyl
- beta-glucuronidase
-
nephrotoxicity
- gamma-glutamyltransferase
- disaccharidase
-
alanyl
- p-nitroanilide
- bilirubin
- oxytocinase
- amastatin
-
dipeptidase
- trehalase
- cholinesterase
-
canalicular
- gamma-glutamyltranspeptidase
-
3.4.11.2
- n-acetyl-beta-glucosaminidase
- arylamidase
-
jaundice
-
hepatobiliary
- gamma-gtp
- metallopeptidases
-
ankylosing
-
enzymuria
- spondylitis
-
ectoenzyme
- synthesis
- pharmacology
- drug development
- diagnostics
- medicine
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
3.4.11.1
-
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RECOMMENDED NAME
GeneOntology No.
leucyl aminopeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid mides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
-
-
-
-
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
mechanism
-
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
molecular modelling of enzyme-substrate binding
-
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
reaction mechanism, active site structure, conformation models using crystal structure
-
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
exoprotease, preference for N-terminal Leu, Met and Arg residues, low activity when Xaa is Gly, no activity when Xaa is Asp
-
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
exoprotease, preference for N-terminal Leu, Met and Arg residues, low activity when Xaa is Gly or Tyr, no activity when Xaa is Asp
-
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
exoprotease, preference for N-terminal Leu, Met and Arg residues, low activity when Xaa is Gly or Trp, no activity when Xaa is Asp
-
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
catalytic residues are Arg431 and Lys354
-
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
prefers leucine and methionine as N-terminal amino acids
-
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
exopeptidase
-
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
Lys528 is located near the entrance of the substrate pocket and is important for maximal activity by maintaining the appropriate structure of the substrate binding pocket
-
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
mechanism
-
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid mides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
substrate-enzyme complex structure, molecular modeling
-
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid mides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
endopeptidase
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid mides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
endopeptidase
-
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid mides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
solid-state structure and structure of hydrated intermediates of the active site, catalytic mechanism, overview
-
release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid mides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
N-terminal exopeptidase
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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CAS REGISTRY NUMBER
COMMENTARY
9001-61-0
-
90119-07-6
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains NRRL 1988 and NRRL 6271, other strains show low enzyme activity
-
-
Morimus funereus
-
25, 35862, 35908, 650856, 665075, 678587, 95189, 95190, 95192, 95197, 95200, 95201, 95210, 95211, 95212, 95213, 95214, 95216, 95217, 95219, 95220
-
-
-
35908, 651776, 664275, 664276, 664966, 665010, 665075, 681245, 684043, 697396, 700616, 717932, 95178, 95181, 95184, 95187, 95204, 95223, 95227
-
-
-
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
-
regulation of the tick molecules involved in nutrient metabolism for the reproduction, including blood digestion and vitellogenesis, would help in controlling the tick population and tick-borne pathogens
malfunction
-
inhibition of LAP with bestatin does not adversely affect growth of Staphylococcus aureus or biofilm formation; lysates from pepZ mutant cells show leucine aminopeptidase activity comparable to that of the wild-type strain suggesting that the majority of leucine aminopeptidase activity observed in Staphylococcus aureus cells comes from PepS, and not LAP
malfunction
disruption of the LAP-A hexameric structure increases chaperone activity
malfunction
-
disruption of the pepZ gene results in an attenuation of virulence in both localized and systemic models of infection
physiological function
-
the M17 leucine aminopeptidase of the intraerythrocytic stages of the malaria parasite Plasmodium falciparum plays a role in releasing amino acids from host hemoglobin that are used for parasite protein synthesis, growth, and development
physiological function
-
LAP may play regulatory roles in protein biosynthesis and degradation in basophilic cells
physiological function
LAP plays a central role in hatching of the miracidium from the schistosome egg
physiological function
the enzyme is responsible for the catabolism of host hemoglobin
physiological function
-
LAP plays a vital role in the development of oocytes, vitellogenesis
physiological function
lapA is a late wound-response gene of tomato, LapA is involved in protection against Manduca sexta damage
physiological function
-
enzymatic properties to participate in generating or destroying MHC class I-presented peptides
physiological function
-
key roles in senescence, stress response and amino acid turn over
physiological function
LAP-A exhibits chaperone activity which is independant of its peptidase activity; LAP-A exhibits chaperone activity which is independant of its peptidase activity
physiological function
-
LAP is required for survival inside human macrophages
physiological function
rMHJ_0461 binds plasminogen and facilitates plasmin conversion
physiological function
-
immunization with recombinant Fasciola gigantica LAP (FgLAP) elicits high levels of immune responses and protection against Fasciola gigantica in mice
physiological function
-
LAP may play regulatory roles in protein biosynthesis and degradation in basophilic cells
-
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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
(S)-2-amino-N-(6-(dimethylamino)pyridin-3-yl)-4-methylpentanamide + H2O
?
-
-
-
-
?
4-[(E)-2-[4-cyano-5-(dicyanomethylidene)-2,2-dimethyl-2,5-dihydrofuran-3-yl]ethenyl]phenyl L-leucinate + H2O
L-leucine + 4-[(E)-2-(4-aminophenyl)ethenyl-3-cyano-5,5-dimethylfuran-2(5H)-ylidene]propanedinitrile
-
-
-
-
?
Ala-4-nitroanilide + H2O
L-alanine + 4-nitroaniline
-
18.7% of activity towards Leu-4-nitroanilide
-
-
?
alanyl-7-amido-4-methylcoumarin + H2O
alanine + 7-amino-4-methylcoumarin
-
-
-
-
?
angiotensin II + H2O
Asp + angiotensin III
-
i.e. Asp-Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
i.e. Tyr-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
Arg-4-nitroanilide + H2O
L-arginine + 4-nitroaniline
-
52.5% of activity towards Leu-4-nitroanilide
-
-
?
Arg-Ala-Arg + H2O
Arg + Ala-Arg
-
Ala-p-nitroanilide is used as substrate with very low turnover rate
in the assay hydrolysis of Ala-p-nitroanilide is monitored
-
?
Arg-Ser-Arg + H2O
Arg + Ser-Arg
-
Ala-p-nitroanilide is used as substrate with very low turnover rate
in the assay hydrolysis of Ala-p-nitroanilide is monitored
-
?
DL-alpha-amino-acid amide + H2O
D-alpha-amino acid amide + L-alpha-amino acid
-
-
-
-
-
Gly-7-amido-4-methylcoumarin + H2O
glycine + 7-amino-4-methylcoumarin
enzyme shows only weak activity with this substrate
-
-
?
glycine-4-methylcoumaryl-7-amide + H2O
glycine + 7-amino-4-methylcoumarin
-
3.9% activity in comparison to L-leucine-4-methyl-coumaryl-7-amide
-
-
?
hArg-7-amido-4-methylcoumarin + H2O
hArg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-7-amido-4-trifluoro-methylcoumarin + H2O
L-Ala + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
L-alanine-4-methylcoumaryl-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarine
-
-
-
?
L-Arg-7-amido-4-trifluoro-methylcoumarin + H2O
L-Arg + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
L-arginine-4-nitroanilide + H2O
L-arginine + 4-nitroaniline
-
16.5% activity in comparison to L-leucine-4-nitroanilide
-
-
?
L-Ile-7-amido-4-methylcoumarin + H2O
L-isoleucine + 7-amino-4-methylcoumarin
enzyme shows only weak activity with this substrate
-
-
?
L-Leu-4-(phenylazo)phenylamide + H2O
L-Leu + 4-(phenylazo)phenylamine
-
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
7-amino-4-methylcoumarin + L-Leu
-
-
-
-
?
L-Leu-7-amido-4-trifluoro-methylcoumarin + H2O
L-Leu + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
L-lysine-4-nitroanilide + H2O
L-lysine + 4-nitroaniline
-
24.5% activity in comparison to L-leucine-4-nitroanilide
-
-
?
L-lysyl-7-amido-4-methylcoumarin + H2O
L-lysine + 7-amino-4-methylcoumarin
ERAP2 preferentially hydrolyzes Arg-aminomethylcoumarin and Lys-aminomethylcoumarin
-
-
?
L-methionine-4-nitroanilide + H2O
L-methionine + 4-nitroaniline
-
29.6% activity in comparison to L-leucine-4-nitroanilide
-
-
?
L-phenylalanine-4-methylcoumaryl-7-amide + H2O
L-phenylalanine + 7-amino-4-methylcoumarine
-
-
-
?
L-phenylalanine-4-nitroanilide + H2O
L-phenylalanine + 4-nitroaniline
-
38.8% activity in comparison to L-leucine-4-nitroanilide
-
-
?
L-proline-4-methylcoumaryl-7-amide + H2O
L-proline + 7-amino-4-methylcoumarin
-
1.3% activity in comparison to L-leucine-4-methyl-coumaryl-7-amide
-
-
?
L-proline-4-methylcoumaryl-7-amide + H2O
L-proline + 7-amino-4-methylcoumarine
-
-
-
?
L-Tyr-7-amido-4-methylcoumarin + H2O
L-Tyr + 7-amino-4-methylcoumarin
6.4% activity compared to L-Leu-7-amido-4-methylcoumarin
-
-
?
L-tyrosine-4-methylcoumaryl-7-amide + H2O
L-tyrosine + 7-amino-4-methylcoumarin
-
8.5% activity in comparison to L-leucine-4-methyl-coumaryl-7-amide
-
-
?
L-tyrosine-4-methylcoumaryl-7-amide + H2O
L-tyrosine + 7-amino-4-methylcoumarine
20% activity compared to L-leucyl-4-methylcoumaryl-7-amide
-
-
?
L-Val-7-amido-4-methylcoumarin + H2O
L-Val + 7-amino-4-methylcoumarin
enzyme shows only weak activity with this substrate
-
-
?
L-valine-4-methylcoumaryl-7-amide + H2O
L-valine + 7-amino-4-methylcoumarin
-
2.3% activity in comparison to L-leucine-4-methyl-coumaryl-7-amide
-
-
?
Leu-4-methylcoumaryl-7-amide + H2O
Leu + 7-amino-4-methyl-coumarin
-
-
-
-
?
Leu-4-trifluoroomethylcoumarin-7-amide + H2O
Leu + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
Leu-Gly-Arg-Ser-Gly-Gly-Asp-Ile-Ile-Lys-Lys-Met-Gln-Thr-Leu + H2O
Leu + Gly-Arg-Ser-Gly-Gly-Asp-Ile-Ile-Lys-Lys-Met-Gln-Thr-Leu
-
-
-
-
?
Leu-Gly-Tyr-Leu + H2O
Leu + Gly + Tyr + Leu
-
synthetic peptide substrate, successive release of terminal amino acids with descending activity
-
-
?
Leu-Ser-Ile-Ile-Asn-Phe-Glu-Lys-Leu + H2O
? + Ile-Ile-Asn-Phe-Glu-Lys-Leu
-
-
-
-
?
Leu-Ser-Ile-Ile-Asn-Phe-Glu-Lys-Leu + H2O
L-leucine + Ser-Ile-Ile-Asn-Phe-Glu-Lys-Leu
-
trimming of further model epitope precursors to antigenic peptides are also tested
-
-
?
leucyl-7-amido-4-methylcoumarin + H2O
leucine + 7-amino-4-methylcoumarin
-
-
-
?
Lys-4-nitroanilide + H2O
L-lysine + 4-nitroaniline
-
41.9% of activity towards Leu-4-nitroanilide
-
-
?
Met-4-methylcoumaryl-7-amide + H2O
Met + 7-amino-4-methyl-coumarin
-
-
-
-
?
N-(6-methoxy-2-methylpyridin-3-yl),(S)-2-amino-4-methylpentanamide + H2O
?
-
-
-
-
?
N-(6-methoxy-2-methylpyridin-3-yl)-(S)-2-amino-4-methylpentanamide + H2O
?
-
-
-
-
?
Phe-4-methylcoumaryl-7-amide + H2O
Phe + 7-amino-4-methyl-coumarin
-
-
-
-
?
Phg-7-amido-4-methylcoumarin + H2O
Phg + 7-amino-4-methylcoumarin
-
-
-
-
?
Pro-4-nitroanilide + H2O
Pro + 4-nitroaniline
-
30% of the activity with Leu-4-nitroanilide
-
-
?
Ala-4-methylcoumaryl-7-amide + H2O
Ala + 7-amino-4-methylcoumarin
-
-
-
?
Ala-4-methylcoumaryl-7-amide + H2O
Ala + 7-amino-4-methylcoumarin
-
-
-
?
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
-
42% of the activity with Leu-4-nitroanilide
-
-
?
amino acid amides + H2O
amino acid + NH3
-
fast hydrolysis: L-Leu
-
-
?
amino acid amides + H2O
amino acid + NH3
-
fast hydrolysis: L-Leu
-
-
?
amino acid amides + H2O
amino acid + NH3
-
fast hydrolysis: L-Leu
-
-
?
Cys-Gly + H2O
Cys + Gly
the enzyme plays a role in glutathione turnover
-
-
?
Cys-Gly + H2O
Cys + Gly
-
only hydrolyzed by the Mn2+-Zn2+-enzyme, not by the Zn2+-Zn2+-enzyme
-
-
?
cysteinylglycine + H2O
cysteine + glycine
involved in turnover of glutathione
-
?
cysteinylglycine + H2O
cysteine + glycine
-
involved in the metabolism of glutathione and glutathione S-conjugates, major cysteinylglycine-hydrolysing activity
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
low activity
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
Q95V75
low activity
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
low activity
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
?
L-Ala-7-amido-4-methylcoumarin + H2O
L-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
L-alanine 4-nitroanilide + H2O
L-alanine + 4-nitroaniline
-
10.8% of the activity compared to Leu-4-nitroanilide
-
-
?
L-alanine 4-nitroanilide + H2O
L-alanine + 4-nitroaniline
about 20% of the activity compared to Leu-4-nitroanilide
-
-
?
L-alanine 4-nitroanilide + H2O
L-alanine + 4-nitroaniline
about 20% of the activity compared to Leu-4-nitroanilide
-
-
?
L-alanine 4-nitroanilide + H2O
L-alanine + 4-nitroaniline
-
10.8% of the activity compared to Leu-4-nitroanilide
-
-
?
L-alanine-4-methylcoumarin-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-alanine-4-methylcoumarin-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-alanine-4-methylcoumaryl-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
-
-
-
?
L-alanine-4-methylcoumaryl-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
-
-
-
?
L-alanine-4-methylcoumaryl-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
-
32.5% activity in comparison to L-leucine-4-methyl-coumaryl-7-amide
-
-
?
L-alanine-4-methylcoumaryl-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
-
-
-
?
L-alanyl-7-amido-4-methylcoumarin + H2O
L-alanine + 7-amino-4-methylcoumarin
-
20.5% activity compared to L-leucyl-7-amido-4-methylcoumarin
-
-
?
L-alanyl-7-amido-4-methylcoumarin + H2O
L-alanine + 7-amino-4-methylcoumarin
-
-
-
?
L-alanyl-7-amido-4-methylcoumarin + H2O
L-alanine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
best substrate with L-Leu at N-terminal end
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
fast hydrolysis of hydrophobic amino acids in N-terminal position
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
free N-terminal alpha-amino group required
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
no hydrolysis of D-Leu
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
free N-terminal alpha-amino group required
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
fast hydrolysis of hydrophobic amino acids in N-terminal position
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
best substrate with L-Leu at N-terminal end
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
influence of amino acid in penultimate position
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
leucyl-dipeptides
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
free N-terminal alpha-amino group required
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
fast hydrolysis of hydrophobic amino acids in N-terminal position
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
free N-terminal alpha-amino group required
-
-
?
L-amino acid-peptide + H2O
amino acid + peptide
-
fast hydrolysis of hydrophobic amino acids in N-terminal position
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
34.7% activity compared to L-Leu-7-amido-4-methylcoumarin
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-arginine-4-methylcoumarin-7-amide + H2O
L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-arginine-4-methylcoumarin-7-amide + H2O
L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-arginine-4-methylcoumaryl-7-amide + H2O
L-arginine + 7-amino-4-methylcoumarin
-
62.3% activity in comparison to L-leucine-4-methyl-coumaryl-7-amide
-
-
?
L-arginine-4-methylcoumaryl-7-amide + H2O
L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
L-arginine-4-methylcoumaryl-7-amide + H2O
L-arginine + 7-amino-4-methylcoumarine
-
-
-
?
L-arginine-4-methylcoumaryl-7-amide + H2O
L-arginine + 7-amino-4-methylcoumarine
about 2% activity compared to L-leucyl-4-methylcoumaryl-7-amide
-
-
?
L-arginyl-7-amido-4-methylcoumarin + H2O
L-arginine + 7-amino-4-methylcoumarin
ERAP2 preferentially hydrolyzes Arg-aminomethylcoumarin and Lys-aminomethylcoumarin
-
-
?
L-arginyl-7-amido-4-methylcoumarin + H2O
L-arginine + 7-amino-4-methylcoumarin
-
70% activity compared to L-leucyl-7-amido-4-methylcoumarin
-
-
?
L-Cys-7-amido-4-methylcoumarin + H2O
L-Cys + 7-amino-4-methylcoumarin
-
-
?
L-Cys-7-amido-4-methylcoumarin + H2O
L-Cys + 7-amino-4-methylcoumarin
Q95V75
-
-
?
L-Cys-7-amido-4-methylcoumarin + H2O
L-Cys + 7-amino-4-methylcoumarin
-
-
?
L-glutamate 4-nitroanilide + H2O
L-glutamate + 4-nitroaniline
about 20% of the activity compared to Leu-4-nitroanilide
-
-
?
L-glutamate 4-nitroanilide + H2O
L-glutamate + 4-nitroaniline
about 20% of the activity compared to Leu-4-nitroanilide
-
-
?
L-Ile-7-amido-4-methylcoumarin + H2O
L-Ile + 7-amino-4-methylcoumarin
low activity
-
?
L-Ile-7-amido-4-methylcoumarin + H2O
L-Ile + 7-amino-4-methylcoumarin
Q95V75
low activity
-
?
L-Ile-7-amido-4-methylcoumarin + H2O
L-Ile + 7-amino-4-methylcoumarin
low activity
-
?
L-isoleucine 4-nitroanilide + H2O
L-isoleucine + 4-nitroaniline
-
14.3% of the activity compared to Leu-4-nitroanilide
-
-
?
L-isoleucine 4-nitroanilide + H2O
L-isoleucine + 4-nitroaniline
-
14.3% of the activity compared to Leu-4-nitroanilide
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-Leu + 4-nitroaniline
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
best substrate
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
best substrate
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
best synthetic substrate
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
Q95V75
best synthetic substrate
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
best synthetic substrate
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
100% activity, LAP protein demonstrates preferential substrate specificity for Leu-7-amido-4-methylcoumarin
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-Leu + 7-amino-4-methylcoumarin
-
-
-
?
L-Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
very slow hydrolysis
-
-
?
L-Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
-
-
-
?
L-Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
substituted anilides, e.g. o-, m- or p-aminobenzenesulfonic acid, o- or m-anisidine, m- or p-aminobenzenesulfonylfluoride
-
-
?
L-Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
Leu substituted by Ala, Gly, Lys
-
-
?
L-Leu-p-nitroanilide + H2O
L-leucine + p-nitroaniline
-
very slow hydrolysis
-
-
?
L-leucine 4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
-
?
L-leucine 4-nitroanilide + H2O
leucine + 4-nitroaniline
-
-
-
?
L-leucine-4-methylcoumarin-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-leucine-4-methylcoumarin-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarine
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarine
-
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarine
best synthetic substrate
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarine
-
-
-
?
L-leucine-4-methylcoumaryl-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarine
-
-
-
-
?
L-leucine-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-leucine-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-leucine-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
-
L-leucyl-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
?
L-leucyl-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
ERAP1 preferentially hydrolyzes Leu-aminoacyl-aminomethylcoumarin
-
-
?
L-leucyl-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-leucyl-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
preferred substrate
-
-
?
L-leucyl-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-leucyl-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
best substrate
-
-
?
L-leucyl-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
best substrate
-
-
?
L-lysine-4-methylcoumaryl-7-amide + H2O
L-lysine + 7-amino-4-methylcoumarin
-
-
-
?
L-lysine-4-methylcoumaryl-7-amide + H2O
L-lysine + 7-amino-4-methylcoumarin
-
-
-
?
L-lysine-4-methylcoumaryl-7-amide + H2O
L-lysine + 7-amino-4-methylcoumarin
-
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
no activity with Z-Met-7-amido-4-methylcoumarin
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
no activity with Z-Met-7-amido-4-methylcoumarin
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
Q95V75
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
-
?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
-
-
-
?
L-methionine 4-nitroanilide + H2O
L-methionine + 4-nitroaniline
-
26.3% of the activity compared to Leu-4-nitroanilide
-
-
?
L-methionine 4-nitroanilide + H2O
L-methionine + 4-nitroaniline
about 25% of the activity compared to Leu-4-nitroanilide
-
-
?
L-methionine 4-nitroanilide + H2O
L-methionine + 4-nitroaniline
about 25% of the activity compared to Leu-4-nitroanilide
-
-
?
L-methionine 4-nitroanilide + H2O
L-methionine + 4-nitroaniline
-
26.3% of the activity compared to Leu-4-nitroanilide
-
-
?
L-methionine-4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
?
L-methionine-4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
?
L-methionine-4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
low activity
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
low activity
-
-
?
L-Phe-7-amido-4-methylcoumarin + H2O
L-Phe + 7-amino-4-methylcoumarin
-
-
-
?
L-phenylalanine-4-methylcoumarin-7-amide + H2O
L-phenylalanine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-phenylalanine-4-methylcoumarin-7-amide + H2O
L-phenylalanine + 7-amino-4-methylcoumarin
-
-
-
-
?
L-phenylalanine-4-methylcoumaryl-7-amide + H2O
L-phenylalanine + 7-amino-4-methylcoumarin
-
-
-
?
L-phenylalanine-4-methylcoumaryl-7-amide + H2O
L-phenylalanine + 7-amino-4-methylcoumarin
-
-
-
?
L-phenylalanine-4-methylcoumaryl-7-amide + H2O
L-phenylalanine + 7-amino-4-methylcoumarin
-
-
-
?
L-proline-4-methylcoumarin-7-amide + H2O
L-proline + 7-amino-4-methylcoumarin
-
-
-
-
?
L-proline-4-methylcoumarin-7-amide + H2O
L-proline + 7-amino-4-methylcoumarin
-
-
-
-
?
L-prolyl-7-amido-4-methylcoumarin + H2O
L-proline + 7-amino-4-methylcoumarin
-
-
-
?
L-prolyl-7-amido-4-methylcoumarin + H2O
L-proline + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Trp-7-amido-4-methylcoumarin + H2O
L-Trp + 7-amino-4-methylcoumarin
low activity
-
?
L-Trp-7-amido-4-methylcoumarin + H2O
L-Trp + 7-amino-4-methylcoumarin
Q95V75
low activity
-
?
L-Trp-7-amido-4-methylcoumarin + H2O
L-Trp + 7-amino-4-methylcoumarin
low activity
-
?
L-tyrosyl-7-amido-4-methylcoumarin + H2O
L-tyrosine + 7-amino-4-methylcoumarin
-
7.4% activity compared to L-leucyl-7-amido-4-methylcoumarin
-
-
?
L-tyrosyl-7-amido-4-methylcoumarin + H2O
L-tyrosine + 7-amino-4-methylcoumarin
-
-
-
?
L-tyrosyl-7-amido-4-methylcoumarin + H2O
L-tyrosine + 7-amino-4-methylcoumarin
-
-
-
-
?
Leu-2-naphthylamide + H2O
leucine + 2-naphthylamine
-
Leu replaced by Met, Phe
-
-
?
Leu-4-methylcoumaryl-7-amide + H2O
Leu + 7-amino-4-methylcoumarin
-
-
-
?
Leu-4-methylcoumaryl-7-amide + H2O
Leu + 7-amino-4-methylcoumarin
-
-
-
?
Leu-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
-
?
Leu-7-amido-4-methylcoumarin + H2O
leucine + 7-amino-4-methylcoumarin
-
Leu replaced by Arg
-
-
?
Leu-7-amido-4-methylcoumarin + H2O
leucine + 7-amino-4-methylcoumarin
-
Leu replaced by Met
-
-
?
Leu-Gly + H2O
Leu + Gly
-
substrate of the Mn2+-Zn2+-enzyme and the Zn2+-Zn2+-enzyme
-
-
?
Lys-4-nitroanilide + H2O
Lys + 4-nitroaniline