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Information on EC 3.4.11.1 - leucyl aminopeptidase
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3.4.11.1 leucyl aminopeptidaseSpecify your search results
Word Map
- 3.4.11.1
-
aminopeptidases
-
venom
- border
-
crotalus
-
brush
-
durissus
-
terrificus
- bestatin
- transpeptidase
-
gamma-glutamyl
- maltase
- sucrase
-
carboxypeptidase
- pregnancy
-
rattlesnake
- chymotrypsin
-
arachidonic
- bile
-
neurotoxin
-
transaminase
-
trim
-
dipeptidyl
-
exopeptidase
- snake
-
brush-border
-
nephrotoxicity
- p-nitroanilide
-
myotoxic
- gamma-glutamyltransferase
- disaccharidase
-
alanyl
- n-acetyl-beta-glucosaminidase
- amastatin
- arylamidase
-
canalicular
- spondylitis
-
ankylosing
-
3.4.11.2
-
hepatobiliary
- gamma-glutamyltranspeptidase
- trehalase
-
dipeptidase
- gamma-gtp
- oxytocinase
-
enzymuria
- aacocf3
- pharmacology
- diagnostics
- drug development
- medicine
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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
Synonyms
erap2, leucine amino peptidase, leucinaminopeptidase, pilsap, l-leucine aminopeptidase, adipocyte-derived leucine aminopeptidase, phtet2, apdkam589, lap-n, cslap2, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Aminopeptidase A/I
-
-
-
-
aminopeptidase I
aminopeptidase II
Aminopeptidase III
APDkam589
cathepsin III
cytosol aminopeptidase
DR57
-
-
-
-
EC 3.4.1.1
-
-
formerly
-
FrvX
FTBL proteins
-
-
-
-
L-leucine aminopeptidase
LAP
LAP-A
leucinamide aminopeptidase
leucinaminopeptidase
leucine aminopeptidase
leucine aminopeptidase N
leucine aminopeptidase,
Leucyl aminopeptidase
leucyl aminopeptidase (animal)
leucyl aminopeptidase (plant)
leucyl peptidase
leucylpeptidase
M17 leucine aminopeptidase
M42 aminopeptidase
PepA
peptidase S
pepZ
PfLAP
PH1527
PhTET2
proline aminopeptidase
-
-
-
-
Prolyl aminopeptidase
-
-
-
-
proteins, specific or class, FTBL
-
-
-
-
TM0042
additional information
cathepsin III
-
-
-
-
cytosol aminopeptidase
-
-
-
-
L-leucine aminopeptidase
-
-
-
-
LAP
-
-
-
-
LAP-A
stress-induced acidic LAPs, LAP-A exhibits chaperone activity
leucinamide aminopeptidase
-
-
-
-
leucinaminopeptidase
-
-
-
-
leucine aminopeptidase
-
-
-
-
Leucyl aminopeptidase
-
-
-
-
leucyl peptidase
-
-
-
-
peptidase S
-
-
-
-
additional information
the enzyme belongs to the M17 family leucine aminopeptidases
additional information
-
tick midgut leucine aminopeptidase belongs to the clan MF, M17 cytosolic aminopeptidase family
additional information
-
tick midgut leucine aminopeptidase belongs to the clan MF, M17 cytosolic aminopeptidase family
-
additional information
-
enzyme belongs to the peptidase family M17, enzyme belongs to the metallopeptidase family M1
additional information
-
the multifunctional enzyme belongs to the M1 aminopeptidase family
additional information
-
the enzyme belongs to the peptidase family M17
additional information
the enzyme belongs to the M17 family leucine aminopeptidases
additional information
the enzyme belongs to the M17 leucine peptidase family
additional information
-
the enzyme belongs to the M17 leucine peptidase family
additional information
-
the enzyme belongs to the M17 family leucine aminopeptidases
additional information
-
the enzyme belongs to the M17 family leucine aminopeptidases
-
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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 SOURCE
PATHWAYS
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CAS REGISTRY NUMBER
COMMENTARY
9001-61-0
-
90119-07-6
-
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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-lysyl-7-amido-4-methylcoumarin + H2O
L-lysine + 7-amino-4-methylcoumarin
ERAP2 preferentially hydrolyzes Arg-aminomethylcoumarin and Lys-aminomethylcoumarin
-
-
?
L-phenylalanine-4-methylcoumaryl-7-amide + H2O
L-phenylalanine + 7-amino-4-methylcoumarine
-
-
-
?
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-4-nitroanilide + H2O
L-alanine + 4-nitroaniline
-
-
-
?
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-4-nitroanilide + H2O
L-leucine + 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-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
-
-
-
-
?
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-Lys-4-nitroanilide + H2O
L-lysine + 4-nitroaniline
hydrolyzes L-Lys-4-nitroanilide with efficiency comparable to that of L-Leu-4-nitroanilide
-
-
?
L-Lys-4-nitroanilide + H2O
L-lysine + 4-nitroaniline
hydrolyzes L-Lys-4-nitroanilide with efficiency comparable to that of L-Leu-4-nitroanilide
-
-
?
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-lysine-4-nitroanilide + H2O
L-lysine + 4-nitroaniline
-
24.5% activity in comparison to L-leucine-4-nitroanilide
-
-
?
L-lysine-4-nitroanilide + H2O
L-lysine + 4-nitroaniline
-
24.5% activity in comparison to L-leucine-4-nitroanilide
-
-
?
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-methionine-4-nitroanilide + H2O
L-methionine + 4-nitroaniline
-
29.6% activity in comparison to L-leucine-4-nitroanilide
-
-
?
L-methionine-4-nitroanilide + H2O
L-methionine + 4-nitroaniline
-
29.6% activity in comparison to L-leucine-4-nitroanilide
-
-
?
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-phenylalanine-4-nitroanilide + H2O
L-phenylalanine + 4-nitroaniline
-
38.8% activity in comparison to L-leucine-4-nitroanilide
-
-
?
L-phenylalanine-4-nitroanilide + H2O
L-phenylalanine + 4-nitroaniline
-
38.8% activity in comparison to L-leucine-4-nitroanilide
-
-
?
L-Pro-4-nitroanilide + H2O
L-proline + 4-nitroaniline
very low activity
-
-
?
L-Pro-4-nitroanilide + H2O
L-proline + 4-nitroaniline
very low activity
-
-
?
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
-
-
?
N-succinyl-L-Leu-4-nitroanilide + H2O
N-succinyl-L-Leu + 4-nitroaniline
-
-
-
-
?
N-succinyl-L-Leu-4-nitroanilide + H2O
N-succinyl-L-Leu + 4-nitroaniline
-
-
-
-
?
Phe-4-methylcoumaryl-7-amide + H2O
Phe + 7-amino-4-methylcoumarin
-
-
-
?
Phe-4-methylcoumaryl-7-amide + H2O
Phe + 7-amino-4-methylcoumarin
-
-
-
?
phosphatidylinositol-dependent kinase-1 + H2O
?
-
i.e. PDK1, removal of 9 amino acids from the N-terminus of the kinase, which allows S6 kinase to associate with PDK1 and the enzyme upon vascular endothelial growth factor stimulation
-
-
?
phosphatidylinositol-dependent kinase-1 + H2O
?
-
i.e. PDK1, removal of 9 amino acids from the N-terminus of the kinase
-
-
?
Pro-4-methylcoumaryl-7-amide + H2O
Pro + 7-amino-4-methylcoumarin
-
-
-
?
Pro-4-methylcoumaryl-7-amide + H2O
Pro + 7-amino-4-methylcoumarin
-
-
-
?
additional information
?
-
-
not active on Ala-para-nitranilide
-
-
-
additional information
?
-
-
not active on Ala-para-nitranilide
-
-
-
additional information
?
-
molecular modelling of enzyme-substrate conformation, no activity with Asp-Gly
-
?
additional information
?
-
-
the enzyme has tissue-specifici physiological roles, overview, active site structure and zinc-binding, mechanism
-
-
-
additional information
?
-
-
the enzyme prefers peptide substrates with bulky and hydrophobic N-terminal amino acid residues
-
-
-
additional information
?
-
-
the enzyme acts as aminopeptidase and endopeptidase and might be a cysteine type peptidase, no activity with N-blocked substrate, Gly-4-nitroanilide, Arg-4-nitroanilide, and Lys-4-nitroanilide are poor substrates, Glu-4-nitroanilide is no substrate
-
-
-
additional information
?
-
-
enzyme activity is regulated on the transcriptional level
-
?
additional information
?
-
-
substrate specificity study, Asp-Leu, Pro-Gly, Lys-Gly, Ser-Gly, Arg-Lys, Arg-Asp, Gly-Ala, Gly-Val, Gly-Trp, Gly-Gln, Gly-Gly, Gly-Lys, Gly-His, and Leu-Pro are poor substrates, Gly-Asn, Asp-Gly, Gly-Arg, and Gly-Asn are no substrates
-
?
additional information
?
-
-
broad substrate specificity towards naturally occurring peptide hormones, while the enzyme hydrolyzes synthetic substrate in vitro with specificity for leucine, enzyme plays a role in regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney
-
?
additional information
?
-
-
A-LAP plays a key role in the MHC class I antigen-presentation pathway, the enzyme is involved in the renin-angiotensin-system, RAS, and angiotensin II metabolism, and plays a role in blood pressure decrease through inactivation of angiotensin II, overview
-
-
-
additional information
?
-
-
the enzyme has tissue-specifici physiological roles, e.g. trimmíng of the N-terminus of antigenic peptides for presentation or in eye cataract, overview
-
-
-
additional information
?
-
-
the enzyme is involved in peptide trimming, e.g. for the generation of most HLA class I-binding peptide, in the endoplasmic reticulum in concert with other aminopeptidases, overview
-
-
-
additional information
?
-
the enzyme is involved in peptide trimming, e.g. for the generation of most HLA class I-binding peptide, in the endoplasmic reticulum in concert with other aminopeptidases, overview
-
-
-
additional information
?
-
-
the enzyme is involved in processing of precursor peptides, and in destruction of antigenic peptides to limit antigen presentation to MHC class I molecules in the endoplasmic reticulum lumen, pathway overview
-
-
-
additional information
?
-
-
the enzyme hydrolyses with Leu or Met in the P1 position
-
-
-
additional information
?
-
no activity with any other L-amino acid amide, N-carboxybenzyloxy-L-Leu-beta-naphthylamide, and N-carboxybenzyloxy-Gly-Gly-Leu-4-nitroanilide
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additional information
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Q95V75
no activity with any other L-amino acid amide, N-carboxybenzyloxy-L-Leu-beta-naphthylamide, and N-carboxybenzyloxy-Gly-Gly-Leu-4-nitroanilide
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additional information
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no activity with any other L-amino acid amide, N-carboxybenzyloxy-L-Leu-beta-naphthylamide, and N-carboxybenzyloxy-Gly-Gly-Leu-4-nitroanilide
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additional information
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the enzyme is required for DNA synthesis and plays an important role in angiogenesis by regulating the proliferation and migration of endothelial cells, mechanism via vascular endothelial growth factor and stimulation of S6 kinase, overview
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additional information
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PILSAP is required for the development of vascular as well as hematopoietic system in embryoid bodies
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additional information
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the enzyme affects RhoA activation and that influences the proper function of endothelial cells
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additional information
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MHJ_0461 binds heparin and interacts with DNA
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additional information
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MHJ_0461 binds heparin and interacts with DNA
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additional information
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rMHJ_0461 binds plasminogen and facilitates plasmin conversion
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additional information
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rMHJ_0461 binds plasminogen and facilitates plasmin conversion
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additional information
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alterations in intensity and number of isozymes in cold-acclimated plants, bark and leaf
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additional information
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no activity towards L-prolyl-7-amido-4-methylcoumarin, L-valyl-7-amido-4-methylcoumarin, L-glycyl-7-amido-4-methylcoumarin, tert-butyloxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin, tert-butyloxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin, and tert-butyloxycarbonyl-Leu-Lys-Arg-7-amido-4-methylcoumarin
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additional information
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