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Substrate specificity of pyroglutamylaminopeptidase

descriptionPublicationkeyboard_double_arrow_right Article 01 Jan 1985Publisher:American Chemical Society (ACS)Journal:Journal of Medicinal Chemistry, volume 28, pages 140-143 (issn: 0022-2623, eissn: 1520-4804,

Authors: John T. Capecchi; Gordon Marc Loudon;

doi: 10.1021/jm00379a024

pmid: 2856942

Substrate specificity of pyroglutamylaminopeptidase

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Abstract

Three synthetic peptides (compounds 4-6) were tested as substrates of pyroglutamylaminopeptidase. In addition, inhibition of the hydrolysis of these substrates by compounds 8 and 9 was also examined. The enzyme does not appreciably catalyze the hydrolysis of peptides with six-membered ureido rings at the amino terminus, but it tolerates well a five-membered ureido ring at this position.

Keywords

Pyroglutamyl-Peptidase I, Aminopeptidases, Substrate Specificity

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Fields of Science (3) View all

medical and health sciences

basic medicine

Fields of Science

medical and health sciences

basic medicine

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