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Information on EC 3.4.11.20 - aminopeptidase Ey and Organism(s) Gallus gallus and UniProt Accession O57579

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.20 aminopeptidase Ey
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Gallus gallus
UNIPROT: O57579 not found.
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Word Map
The taxonomic range for the selected organisms is: Gallus gallus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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
pfa-m1, pfa-m17, aminopeptidase ey, pf-lap, m1-family aminopeptidase, pfa-m1 aminopeptidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
show the reaction diagram
Glu387 is an essential catalytic residue
-
CAS REGISTRY NUMBER
COMMENTARY hide
9031-94-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Arg-Pro-Lys-Pro + H2O
Arg + Pro-Lys-Pro
show the reaction diagram
Arg-Pro-Pro-Gly-Phe + H2O
Arg + Pro-Pro-Gly-Phe
show the reaction diagram
-
bradikinin fragment 1-5, no hydrolysis of bradikinin
-
?
Arg-Tyr-Leu-Pro-Thr + H2O
?
show the reaction diagram
-
insect neuropeptide
-
-
?
cholecystokinin octapeptide + H2O
tyrosine sulfate + Asp + Met + Gly + Trp + Met-Asp-Phe-NH2
show the reaction diagram
-
i.e. Asp-tyrosyl sulfate-Met-Gly-Trp-Met-Asp-Phe-NH2
-
-
?
L-Leu-4-methylumbelliferyl + H2O
L-leucine + 4-methylumbelliferol
show the reaction diagram
-
-
-
-
?
L-Leu-4-nitroanilide + H2O
L-leucine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Leu 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
Leu 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
?
Leu-enkephalin + H2O
?
show the reaction diagram
-
i.e. Tyr-Gly-Gly-Phe-Met, stepwise degradation from the N-terminus
-
-
?
Leu-Leu-Tyr + H2O
Leu + Leu-Tyr
show the reaction diagram
-
-
-
-
?
Leu-Pro-Leu-Arg-Phe-NH2 + H2O
Leu + Pro-Leu-Arg-Phe-NH2
show the reaction diagram
-
a chicken brain pentapeptide
-
-
?
Leu-Pro-Leu-Arg-PheNH2 + H2O
Leu + Pro-Leu-Arg-PheNH2
show the reaction diagram
-
i.e. chicken brain peptide
resistant to the enzyme
?
Lys-Ala-Met-Cys-Ala + H2O
?
show the reaction diagram
-
-
-
-
?
Lys-Phe-Ile-Gly-Leu-Met-NH2 + H2O
?
show the reaction diagram
-
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
-
-
?
N-Formyl-Met-Leu-Phe + H2O
N-Formyl-Met + Leu-Phe
show the reaction diagram
-
-
-
-
?
Pro-Phe-Gly-Lys + 2 H2O
Pro + Phe + Gly-Lys
show the reaction diagram
-
-
-
-
?
Pro-Phe-Gly-Lys + H2O
Pro + Phe-Gly-Lys
show the reaction diagram
-
-
-
?
proctolin + H2O
?
show the reaction diagram
-
-
-
-
?
tuftsin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-Formyl-Met-Leu-Phe + H2O
N-Formyl-Met + Leu-Phe
show the reaction diagram
-
-
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
activates, required for activity and stability, zinc is bound by residues His386, His390, and Glu409
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
bestatin
-
-
betaine
-
complete inhibition at 2 mM
OF 4949-II
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.8
Leu 4-methylcoumarin 7-amide
0.58
Leu-Pro-Leu-Arg-PheNH2
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
Leu-Pro-Leu-Arg-PheNH2
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3083
-
purified enzyme
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
plasma enzyme
7.8
-
granule enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.8
-
isoelectric focusing, holoenzyme
4.4
-
isoelectric focusing, asialo enzyme form
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
allantoic fluid concentrates proteolytic enzymes assumed to participate in digestive processes: aminopeptidase Ey, dipeptidyl peptidase-4, meprin A, and 72 kDa type IV collagenase preproprotein
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
plasma of egg yolk
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AMPN_CHICK
972
1
109132
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150000
-
2 * 150000
300000
-
low angle laser light scattering-HPLC
360000
-
plasma enzyme, gel filtration
700000
-
granule enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
additional information
-
the native enzyme contains 14% alpha helix and 68% beta-sheet, while the apoenzyme contains only 6% alpha helix, and 70% beta-sheet, tertiary structure
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
10 min, pH 7.5, plasma enzyme stable
60
-
10 min, pH 7.5, 20% loss of plasma enzyme activity, activation of granule enzyme
70
-
10 min, pH 7.5, complete loss of activity of plasma enzyme, 60% loss of activity of granule enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme form from egg yolk plasma fraction and from granule fraction
-
to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene apdE, DNA and amino acid sequence determination and analysis
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ichishima, E.; Yamagata, Y.; Chiba, H.; Sawaguchi, K.; Tanaka, T.
Soluble and bound forms of aminopeptidase in hen's egg yolk
Agric. Biol. Chem.
53
1867-1872
1989
Gallus gallus
-
Manually annotated by BRENDA team
Tanaka, T.; Ichishima, E.
Substrate specificity of aminopeptidase Ey from hens (Gallus domesticus) egg yolk
Comp. Biochem. Physiol. B
105
105-110
1993
Gallus gallus
Manually annotated by BRENDA team
Tanaka, T.; Ichishima, E.
Molecular properties of aminopeptidase Ey as a zinc-metalloenzyme
Int. J. Biochem.
25
1681-1688
1993
Gallus gallus
Manually annotated by BRENDA team
Midorikawa, T.; Abe, R.; Yamagata, Y.; Nakajima, T.; Ichishima, E.
Isolation and characterization of cDNA encoding chicken egg yolk aminopeptidase Ey
Comp. Biochem. Physiol. B
119
513-520
1998
Gallus gallus
Manually annotated by BRENDA team
Ichishima, E.
Aminopeptidase Ey
Handbook of Proteolytic Enzymes (2nd Edition)
1
294-296
2004
Gallus gallus
-
Manually annotated by BRENDA team
Da Silva, M.; Labas, V.; Nys, Y.; Rhault-Godbert, S.
Investigating proteins and proteases composing amniotic and allantoic fluids during chicken embryonic development
Poult. Sci.
96
2931-2941
2017
Gallus gallus (O57579)
Manually annotated by BRENDA team