Aminopeptidases by Allen Taylor Ph.D. (auth.) PDF
By Allen Taylor Ph.D. (auth.)
ISBN-10: 3662216035
ISBN-13: 9783662216033
ISBN-10: 3662216051
ISBN-13: 9783662216057
This publication summarizes lately accumulated information about the aminopeptidases. Nomenclature, distributions within the plant and animal kingdoms, structural and compositional details, mechanistic stories, homologies, physiological, scientific and commercial makes use of, and molecular genetics of aminopeptidases are described.
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Extra resources for Aminopeptidases
Sample text
9, 22). 30 Aminopeptidases BESTATIN IS A SLOW, RELATIVELY TIGHT-BINDING, COMPETITIVE INHIBITOR OF BLLAP In order to begin to use the available structural data to propose a mechanism of action, it was necessary to determine the type of inhibition of blLAP by bestatin. Three approaches were used to do this: (1) enzyme was added to a solution containing ..... 0 :::> 0 0 a: fl. , 00 _I 0 ::E z 0 50 100 150 MINUTES Fig. 2. 5 mM LeuCiyCiy and 70 8 M bestatin (final concentrations), and samples tested for activity at the times indicated.
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. Circles represent a-helices and triangles represent {Jstrands. Elements with numbers o r /etters indicate structurally equivalent secondary structure elements. Adapted from Chevrier et a/.
61 The LAP used for that work was in the Zn2+Mg2 + form. Assuming that hkLAP and blLAP have the same metal ion distribution, it would appear that Mg2+, and not Zn2+, was in the readily exchanged site. This might explain the unexpected decrease in apparent affinity found for thioamides in the hkLAP, since Mg2+ does not have the same binding affinity for sulfur-containing compounds as Zn2+. This rationale would not appear to explain the lack of binding enhancement in the binding of thiobestatin and brain AP under conditions where zinc might be expected to be retained in the enzyme.
Aminopeptidases by Allen Taylor Ph.D. (auth.)
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