3.4.11.20: aminopeptidase Ey
This is an abbreviated version!
For detailed information about aminopeptidase Ey, go to the full flat file.
Word Map on EC 3.4.11.20
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3.4.11.20
-
plasmodium
-
falciparum
-
antimalarial
-
aminopeptidases
-
bestatin
-
hemoglobin
-
dipeptide
-
malarial
-
subsite
-
metalloaminopeptidases
-
yolk
-
hydroxamic
-
gallus
-
leucyl
-
exopeptidases
-
domesticus
- 3.4.11.20
- plasmodium
- falciparum
-
antimalarial
- aminopeptidases
- bestatin
- hemoglobin
- dipeptide
-
malarial
-
subsite
-
metalloaminopeptidases
- yolk
-
hydroxamic
- gallus
-
leucyl
-
exopeptidases
- domesticus
Reaction
differs from other aminopeptidases in broad specificity for amino acids in the P1 position and the ability to hydrolyse peptides of four or five residues that contain Pro in the P1' position =
Synonyms
aminopeptidase M17, aminopeptidase N, ANPEP, APN1, Leucyl aminopeptidase, M1 aminopeptidase, M1 metalloaminopeptidase, M1-family aminopeptidase, M17 aminopeptidase, M17 leucyl aminopeptidase, malaria M1 metalloaminopeptidase, metallo-aminopeptidase M1, Pf-LAP, PfA-M1, PfA-M1 aminopeptidase, PfA-M17, Xac2987
ECTree
3.4.11.20 aminopeptidase EyAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.11.20 - aminopeptidase Ey
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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-4-cyclohexylbutanoyl-7-amido-4-methylcoumarin + H2O
(S)-2-amino-4-cyclohexylbutanoic acid + 7-amino-4-methylcoumarin
-
-
-
?
Ala-7-amido-4-methylcoumarin + H2O
alanine + 7-amino-4-methylcoumarin
-
-
-
?
Arg-Pro-Pro-Gly-Phe + H2O
Arg + Pro-Pro-Gly-Phe
-
bradikinin fragment 1-5, no hydrolysis of bradikinin
-
?
cholecystokinin octapeptide + H2O
tyrosine sulfate + Asp + Met + Gly + Trp + Met-Asp-Phe-NH2
-
i.e. Asp-tyrosyl sulfate-Met-Gly-Trp-Met-Asp-Phe-NH2
-
-
?
Gly-p-nitroanilide + H2O
Gly + p-nitroaniline
-
58.5% activity compared to L-Pro-p-nitroanilide
-
-
?
homoargininyl-7-amido-4-methylcoumarin + H2O
homoarginine + 7-amino-4-methylcoumarin
-
-
-
?
homophenylalanyl-7-amido-4-methylcoumarin + H2O
homophenylalanine + 7-amino-4-methylcoumarin
-
-
-
?
L-Ala-p-nitroanilide + H2O
L-Ala + p-nitroaniline
-
55.4% activity compared to L-Pro-p-nitroanilide
-
-
?
L-alanyl-2-naphthylamide + H2O
L-alanine + 2-naphthylamine
-
-
-
?
L-arginyl-2-naphthylamide + H2O
L-arginine + 2-naphthylamine
-
-
-
?
L-His-2-naphthylamide + H2O
L-His + 2-naphthylamine
-
31.6% activity compared to L-Pro-p-nitroanilide
-
-
?
L-Ile-2-naphthylamide + H2O
L-Ile + 2-naphthylamine
-
4.6% activity compared to L-Pro-p-nitroanilide
-
-
?
L-Leu-7-amido-4-methyl-coumarin + H2O
L-leucine + 7-amino-4-methyl-coumarin
-
-
-
?
L-Leu-7-amido-4-methylcoumarin + H2O
L-leucine + 7-amino-4-methylcoumarin
-
-
-
?
L-Lys-p-nitroanilide + H2O
L-Lys + p-nitroaniline
-
13% activity compared to L-Pro-p-nitroanilide
-
-
?
L-Met-p-nitroanilide + H2O
L-Met + p-nitroaniline
-
11.5% activity compared to L-Pro-p-nitroanilide
-
-
?
L-methionyl-7-amido-4-methylcoumarin + H2O
L-methionine + 7-amino-4-methylcoumarin
-
-
-
?
L-Phe-p-nitroanilide + H2O
L-Phe + p-nitroaniline
-
1.1% activity compared to L-Pro-p-nitroanilide
-
-
?
L-Pro-2-naphthylamide + H2O
L-Pro + 2-naphthylamine
-
100% activity
-
-
?
L-Pro-p-nitroanilide + H2O
L-Pro + p-nitroaniline
-
100% activity
-
-
?
L-Ser-2-naphthylamide + H2O
L-Ser + 2-naphthylamine
-
64% activity compared to L-Pro-2-naphthylamide
-
-
?
L-Trp-2-naphthylamide + H2O
L-Trp + 2-naphthylamine
-
15.6% activity compared to L-Pro-p-nitroanilide
-
-
?
L-Tyr-2-naphthylamide + H2O
L-Tyr + 2-naphthylamine
-
30.3% activity compared to L-Pro-p-nitroanilide
-
-
?
L-Val-p-nitroanilide + H2O
L-Val + p-nitroaniline
-
5.3% activity compared to L-Pro-p-nitroanilide
-
-
?
Leu-enkephalin + H2O
?
-
i.e. Tyr-Gly-Gly-Phe-Met, stepwise degradation from the N-terminus
-
-
?
Leu-Pro-Leu-Arg-Phe-NH2 + H2O
Leu + Pro-Leu-Arg-Phe-NH2
-
a chicken brain pentapeptide
-
-
?
Leu-Pro-Leu-Arg-PheNH2 + H2O
Leu + Pro-Leu-Arg-PheNH2
-
i.e. chicken brain peptide
resistant to the enzyme
?
Lys-Phe-Ile-Gly-Leu-Met-NH2 + H2O
?
-
eledoisin-related peptide, lysine, phenylalanine, isoleucine, glycine and leucine are liberated from the aminoterminus, methionine is not released from Met-NH2 of the final product
-
-
?
norleucyl-7-amido-4-methylcoumarin + H2O
norleucine + 7-amino-4-methylcoumarin
-
-
-
?
norvalinyl-7-amido-4-methylcoumarin + H2O
norvaline + 7-amino-4-methylcoumarin
-
-
-
?
styryl-Ala-7-amido-4-methylcoumarin + H2O
styryl-alanine + 7-amino-4-methylcoumarin
-
-
-
?
Arg-Pro-Lys-Pro + H2O
Arg + Pro-Lys-Pro
-
i.e. , substance P fragment 1-4, hydrolysis of the N-terminal Xaa-bond, no hydrolysis of substance P
-
?
L-Leu-p-nitroanilide + H2O
L-Leu + p-nitroaniline
-
8.2% activity compared to L-Pro-p-nitroanilide
-
-
?
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
-
-
-
?
additional information
?
-
-
broad specificity for amino acid residues at P1 position, not: Pro-Leu-GlyNH2, schistoFMRF-amide (Pro-Asp-Val-Asp-His-Val-Phe-Leu-Arg-PheNH2), melanocyte-stimulating hormone release-inhibiting factor, Leu-Pro-Thr, Lys-Pro-Arg, Ala-Pro, Gly-Pro, Leu-Pro, Met-Pro, Phe-Pro, alpha-bag cell peptide (Ala-Pro-Arg-Leu-Arg-Phe-Tyr-Ser-Leu)
-
-
?
additional information
?
-
-
the enzyme functiones in regulation of hormone function and thus is involved in diverse biological processes, it offers a biodefense against the infectious microbial product N-formyl-peptide
-
-
?
additional information
?
-
-
the enzyme has a broad specificity for N-terminal amino acids residues at the P1 position of substrates, it degrades hydrophobic, basic, and acidic amino acids including proline, no activity with substance P and melanocyte-stimulating hormone release-inhibiting factor, i.e. Pro-Leu-Gly-NH2
-
-
?
additional information
?
-
-
both S1 and S1' subsite exhibit a preference for basic and hydrophobic side chains over polar and acidic side chains. The relative specificity of the S1 subsite is similar over the pH range 5.5-7.5. Substrate P1 and P1' residues affect both Km and kcat, revealing that side chain-subsite interactions not only drive the formation of the Michaelis complex but also influence the rates of ensuing chemical steps. There is no correlation between S1 and S1' specificities and amino acid abundance in hemoglobin. Interactions between PfA-M1 and the backbone atoms of the P1' and P2' residues as well as the P2' side chain further contribute to the catalytic efficiency of substrate hydrolysis
-
-
?
additional information
?
-
no substrates: Ile-4-nitroanilide, Val-4-nitroanilide, Gly-4-nitroanilide, Pro-4-nitroanilide
-
-
?
