Methionine-preferring broad specificity aminopeptidase from chicken egg-white.
From chicken egg-white a broad specificity aminopeptidase is isolated. The presence of high molecular mass, hydrophobic aminopeptidase is also revealed. Isolated enzyme hydrolysed aliphatic, aromatic and basic aminoacyl-2-naphthylamides, and di- to hexapeptides, with a preference for methionine at the NH2-end, and basic or bulky hydrophobic residue at the penultimate position. The enzyme is a hydrophilic, acidic glycoprotein of M(r) approximately 180,000, optimally active at pH 7.0-7.5 and at a temperature of 50 degrees C. Amastatin, bestatin and o-phenanthroline are strong, and puromycin, EDTA and iodoacetamide less potent, inhibitors. Co2+ activates the enzyme. The isolated enzyme can be classified as a methionine-preferring broad specificity aminopeptidase.
Skrtić
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I
Department of Organic Chemistry and Biochemistry, Ruder Bosković Institute, Zagreb, Croatia.
Vitale
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L
D000626:Aminopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D002645:Chickens; D003035:Cobalt / Q000494:pharmacology; D004529:Egg White / Q000032:analysis*; D004789:Enzyme Activation / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D007930:Leucine / Q000031:analogs & derivatives / Q000494:pharmacology; D008715:Methionine / Q000378:metabolism*; D008970:Molecular Weight; D010455:Peptides; D010618:Phenanthrolines / Q000494:pharmacology; D013379:Substrate Specificity; D013696:Temperature
D000900:Anti-Bacterial Agents; D010455:Peptides; D010618:Phenanthrolines; D003035:Cobalt; C016977:amastatin; D008715:Methionine; D000626:Aminopeptidases; D007930:Leucine; C012211:ubenimex; C025205:1,10-phenanthroline