Aminopeptidases by Allen Taylor Ph.D. (auth.)

By Allen Taylor Ph.D. (auth.)

This e-book summarizes lately accumulated information about the aminopeptidases. Nomenclature, distributions within the plant and animal kingdoms, structural and compositional info, mechanistic stories, homologies, physiological, clinical and business makes use of, and molecular genetics of aminopeptidases are described.

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Comparison of the amino acid sequences of bovine lens and E. coli am_inopeptidase A (pepA) showing the secondary structure o f biLAP. ( *) tdentlty, ( I ) stmtlanty; structure codes: S, {}strand; H, a-helix; 0, disordered loop or terminus. Z indicates zinc ion binding residues. B indica tes residues involved in binding bestatin. Adapted from Burley et al. 10 55 Structure and Function of Bovine Lens Aminopeptidase (b) IN terminal domain c Fig. 6. Schematics comparing the topology of (a) Aeromonas proteolytica aminopeptidase and (b) the carboxyl terminal domain of b/LAP.

BlLAP is active only when both of these metal-ion binding sites are occupied. 5· 49 Structural data of blLAP in which one of the Zn2 + has been replaced by Mg2+ indicates that this Zn2 +, called the more readily exchangeable ion, is in position number 488. 31 By analogy it would appear that Mn 2+ binds to this site as well. Since replacement of metals affected kcat and was within a hydration radius of the substrate scissile carbonyl, 41 it was assumed that at least one of the metal ions was bound at the active site (see below).

The two-step binding mechanism is also consistent with observations of two presteady-state intermediates in dimetal ion-containing hkLAP and with only one intermediate when hkLAP had one ion. It was proposed that the substrate would bind to both sites in dimetal forms of hkLAP but pass the unoccupied metal ion binding site and bind directly to the analog of Zn2+489 in hkLAP to which only one equivalent of metal was bound. 55 For arginine AP the different binding kinetics and absence of metal content indicate other binding mechanisms exist.

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