Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Aminopeptidase Ey, purified from hen's (Gallus gallus domesticus) egg yolk, was studied for its specificity against N-blocked peptides. Only N-formylmethionyl peptides were hydrolyzed by the enzyme in the tested peptides. N-Formyl-methionyl-leucyl-phenylalanine (fMet-Leu-Phe) lost its chemotactic activity toward human neutrophil after incubation with aminopeptidase Ey.
Comp Biochem Physiol Biochem Mol Biol 1994 Apr
PMID:Inactivation of chemotactic peptides by aminopeptidase Ey from hen's (Gallus gallus domesticus) egg yolk. 820 80

Aminopeptidase Ey (EC 3.4.11.20) from chicken (Gallus gallus domesticus) egg yolk is a homodimeric exopeptidase with a broad specificity for N-terminal amino acid residues at P1 position of the substrate. Aminopeptidase Ey is a 300-k metalloexopeptidase, containing 1.0 g atom of zinc per mole of a subunit with a relative molecular mass of 150 k. A full-length cDNA was cloned from chicken (female) liver cDNA library. Analysis of the 3196-base pairs (bp) nucleotide sequence of the cDNA revealed a single open reading frame coding for 967 amino acid residues. The coding region of aminopeptidase Ey gene, apdE, occupies 2901 bp of the cDNA. The predicted amino acid sequence of the enzyme is 66, 65, 64 and 63% identical with those of aminopeptidases N (EC 3.4.11.2) from human, pig, rabbit and rat, respectively. Aminopeptidase Ey contains the metallo-binding sequence motif, His-Glu-Xaa-His, found in zinc metallopeptidases. Zinc binding sites, His-386, His-390 and Glu-409, and catalytic site, Glu-387, were conserved in the homologous aminopeptidases N.
Comp Biochem Physiol B Biochem Mol Biol 1998 Mar
PMID:Isolation and characterization of cDNA encoding chicken egg yolk aminopeptidase Ey. 973 35