Download PDF by Allen Taylor Ph.D. (auth.): Aminopeptidases

By Allen Taylor Ph.D. (auth.)

This ebook summarizes lately collected information about the aminopeptidases. Nomenclature, distributions within the plant and animal kingdoms, structural and compositional info, mechanistic reports, homologies, physiological, scientific and business makes use of, and molecular genetics of aminopeptidases are described.

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It is bound less tightly to blLAP but more tightly to other APs. 23 ~ to hkLAP) more tightly than peptides but less tightly than some "statins". The availability of a relatively tightly-bound LAP inhibitor such as bestatin and the atomic coordinates obtained from the single crystal structure determination of this transition state analog inhibitor46 provided further details with respect to identification of the active site. Conversion of bestatin to [3H]p-azidobestatin resulted in an effective photoaffinity label for blLAP.

5 5 It is interesting to speculate that of the 8% amino acid sequence difference between hklAP and bllAP, there are differences in residues which alter metal binding. 13 Other than bllAP, there is no other example in which Lys is used to coordinate the metal ion (see section V). A new observation is that of a third metal ion binding site in bllAP. 2 While unremarkable in a structural context, this is surprising since no prior compositional analyses indicated more than two Zn 2+ per protomer. 5•42 •49 •56 This metal is coordinated by Structure and Function of Bovine Lens Aminopeptidase 49 Leu-170, Met-171, Thr-173, Arg-271, a water and possibly Met-274, and is 12 A away from Zn2 +489.

13 The mass of LAP is 52,989Da, whereas the mass of the proprotein would be 55,562Da. 1 Trypsinization of the enzyme resulted in formation of only two polypeptides, one with a mass of 37 kDa (residues 138-487) and Structure and Function of Bovine Lens Aminopeptidase 29 the other with a mass of 18 kDa (residues 1-137) (Fig. 1d). A unique cleavage between residues 322 and 323 by hydroxylamine results in similarly sized but different polypeptides {1-322 and 323-487) from those obtained with trypsin.

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