Fluorescence of human liver alanine aminopeptidase.
Fluorescence of human liver alanine aminopeptidase has been attributed to tryptophan fluorescence. The fluorescence maximum is at 330 nm, 20 nm lower than that for free tryptophan, suggesting that most of the enzyme tryptophans are in a nonpolar environment and are shielded from solvent. Quenching of enzyme fluorescence by iodide, pyridine, and N-methyl nicotinamide also demonstrates that enzyme tryptophan residues are largely buried and inaccessible to solvent. Those accessible are in negatively charged environments. 8-(1'-dimethylaminonaphthalene-5'-sulfonylamido-octanoic acid (8-DNS-octanoic acid) and epsilon-DNS-L-Lys inhibit aminopeptidase. One molecule of inhibitor when bound to the enzyme quenched 57% and 63% of enzyme fluorescence, respectively. Such efficient quenching may indicate a degree of segregation of tryptophan toward the active center.
D000626:Aminopeptidases / Q000037:antagonists & inhibitors; D001665:Binding Sites; D002210:Caprylates / Q000494:pharmacology; D003619:Dansyl Compounds / Q000494:pharmacology; D004735:Energy Transfer; D005453:Fluorescence; D006801:Humans; D007454:Iodides / Q000494:pharmacology; D008099:Liver / Q000201:enzymology*; D008239:Lysine / Q000031:analogs & derivatives; D009536:Niacinamide / Q000031:analogs & derivatives / Q000494:pharmacology; D011725:Pyridines / Q000494:pharmacology; D014364:Tryptophan
D002210:Caprylates; D003619:Dansyl Compounds; D007454:Iodides; D011725:Pyridines; D009536:Niacinamide; D014364:Tryptophan; D000626:Aminopeptidases; D008239:Lysine