Title : A tyrosine residue essential for catalytic activity in aminopeptidase A.

Pub. Date : 1997 Nov 1

PMID : 9581570






7 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 A tyrosine residue essential for catalytic activity in aminopeptidase A. Tyrosine glutamyl aminopeptidase Mus musculus
2 Treatment of APA with N-acetylimidazole results in a loss of enzymic activity; this is prevented by the competitive aminopeptidase inhibitor amastatin, suggesting the presence of an important tyrosine, lysine or cysteine residue at the active site of APA. Tyrosine glutamyl aminopeptidase Mus musculus
3 Furthermore sequence alignment of mouse APA with other monozinc aminopeptidases indicates the presence of a conserved tyrosine (Tyr-471 in APA). Tyrosine glutamyl aminopeptidase Mus musculus
4 Furthermore sequence alignment of mouse APA with other monozinc aminopeptidases indicates the presence of a conserved tyrosine (Tyr-471 in APA). Tyrosine glutamyl aminopeptidase Mus musculus
5 Furthermore sequence alignment of mouse APA with other monozinc aminopeptidases indicates the presence of a conserved tyrosine (Tyr-471 in APA). Tyrosine glutamyl aminopeptidase Mus musculus
6 Furthermore sequence alignment of mouse APA with other monozinc aminopeptidases indicates the presence of a conserved tyrosine (Tyr-471 in APA). Tyrosine glutamyl aminopeptidase Mus musculus
7 The functional role of Tyr-471 in APA was investigated by replacing this residue with a phenylalanine (Phe-471) or a histidine (His-471) residue by site-directed mutagenesis. Tyrosine glutamyl aminopeptidase Mus musculus