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 reviews, homologies, physiological, clinical and business makes use of, and molecular genetics of aminopeptidases are described.
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There is a long loop connecting an alpha-helix and the fifth strand of the beta sheet. This long loop contains the peptide bond between residues Arg-137 and Lys-138, where trypsin cleaves each protomer within the hexameric enzyme but leaves the hexamer intact, fully active, 19 and crystallizable (Carpenter, unpublished). Monomers of blLAP have not been isolated. The effective stabilization of hexamers in the native and, presumably, in the trypsin-treated enzyme is achieved via an extensive network of hydrogen bonds and van der Waals' interactions.
Their amino terminus might not have been anticipated, since in each of the "statins," the aNH2-residue is in the D-configuration, and LAP does not hydrolyze peptides or peptide analogs with aNH2-terminal residues which are of the D-configuration. 36-38 In addition there seems to either be insufficient precision in the structural data and/or enough flexibility in the enzyme such that the extra structure present in the "statin" inhibitors is easily modeled in the active site. Thus, there is sufficient overlap of the scissile peptide bond in substrates and the peptide bond in these inhibitors to allow mechanistic extrapolation (see mechanism of action section).
9 •34 Complete occupancy of each binding site in the enzyme-inhibitor complex has been corroborated by kinetic studies with p-azidobestatin22 and by structural studies of blLAP complexed with bestatin, 10 am as tatin 20 36 Aminopeptidases and leucinephosphonic acid. 3 5 This information is in contrast with data which indicate that there is 80% inhibition of hkLAP when only one bestatin is bound per hexamer. 33 IDENTIFICATION OF ACTIVE SITE AND MODE OF INHIBITOR BINDING Compendia of kinetic data obtained with many peptides, esters, and amino acid analogs are found in prior reviews.