Biochimica et Biophysica Acta 1985-07-01

Mechanistic implications of the inhibition of peptidases by amino aldehydes and bestatin.

L Frick, R Wolfenden

Index: Biochim. Biophys. Acta 829(3) , 311-8, (1985)

Full Text: HTML

Abstract

alpha-Amino aldehydes and bestatin are found to be effective inhibitors of a cytosolic dipeptidase (rat testicular peptidase C), and a cytosolic tripeptidase (rat kidney peptidase B, EC 3.4.11.4), as well as cytosolic leucine aminopeptidase (pig kidney peptidase S, EC 3.4.11.1). Aldehyde hydrates and bestatin share a resemblance to intermediates that might be formed during direct attack by water on peptide substrates, affording a possible explanation for their tight binding. Alternatively, inhibitors of both kinds might form derivatives of an active site nucleophile, resembling intermediates in a double-displacement mechanism. Exchange experiments with H218O suggest that bestatin is bound intact by leucine aminopeptidase, lending support to the first of these two mechanisms.

Related Compounds

Related Articles:

N-tritylprolinal: an efficient building block for the stereoselective synthesis of proline-derived amino alcohols.

2003-12-12

[J. Org. Chem. 68(25) , 9747-52, (2003)]

Synthesis and inhibitory activity of acyl-peptidyl-prolinalderivatives toward post-proline cleaving enzyme as nootropic agents.

1990-01-01

[J. Enzym. Inhib. 3(3) , 163-78, (1990)]

Tyrosine hydroxylase deficiency in three Greek patients with a common ancestral mutation.

2010-06-15

[Mov. Disord 25(8) , 1086-90, (2010)]

New potent prolyl endopeptidase inhibitors: synthesis and structure-activity relationships of indan and tetralin derivatives and their analogues.

1994-06-24

[J. Med. Chem. 37(13) , 2071-8, (1994)]

Secreted trypanosome cyclophilin inactivates lytic insect defense peptides and induces parasite calcineurin activation and infectivity.

2013-03-22

[J. Biol. Chem. 288(12) , 8772-84, (2013)]

More Articles...