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

By Allen Taylor Ph.D. (auth.)

This e-book summarizes lately collected information about the aminopeptidases. Nomenclature, distributions within the plant and animal kingdoms, structural and compositional details, mechanistic reports, homologies, physiological, scientific and commercial makes use of, and molecular genetics of aminopeptidases are described.

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Zn 2+ is involved in substrate liganding and presumably in catalysis of hydrolysis. There is no evidence of an acyl-enzyme intermediate t Abbreviations in this chapter are as follows: AP, aminopeptidase; b, bovine; h, hog; l, lens; k, kidney; LAP, leucine aminopeptidase; LeuP, leucinephosphonic acid; MPD, methylpentanediol; Mel+, generic divalent metal ion; kDa, kilodalton Aminopeptidases, edited by Allen Taylor. G. Landes Company. 22 Aminopeptidases in hydrolysis. Amino acid sequences determined directly or deduced from cDNAs indicate homologies between lens aminopeptidase and APs in organisms as diverse as E.

The inability to label the active site with these inhibitors casts doubt on the presence of an enzyme-bound nucleophile at the active site23•41 (see the metal ions section). These reagents did, however, yield information regarding the active site. 5,t0,3l, 41 •42 Kinetic investigations had predicted comparable relationships decades earlier. 44 Perturbation of the cobalt spectrum upon binding inhibitors suggests that substrates or inhibitors are within the immediate vicinity of metal ions in Aeromonas AP as well.

This water is coordinated to and probably activated by Arg-336. Accordingly, prior claims that Arg-336 is coordinated to the scissile carbonyl and that Arg-336 assumes different conformations in the native and inhibitor-complexed enzyme have been withdrawn. 2 Hydrolysis involves nucleophilic attack at the carbon of the scissile carbonyl. There appear to be no enzyme nucleophiles in the area of the scissile peptide bond in blLAP, although this possibility has some support. 60 The absence of a nucleophile is consistent with an inability to inactivate or label the active site of blLAP using a variety of affinity labels, which required attack by an enzyme-bound nucleophile for covalent attachment.

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