Analysis of catalytic properties of tripeptidyl peptidase I (TTP-I), a serine carboxyl lysosomal protease, and its detection in tissue extracts using selective FRET peptide substrate.

Marcia Y Kondo,Iuri E Gouvea,Débora N Okamoto,Jorge A N Santos,Caden Souccar,Kohei Oda,Luiz Juliano,Maria A Juliano

Peptides（2016）

引用 3|浏览13

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摘要

•NH2-RWFFIQ-EDDnp is efficient FRET substrate for tripeptidyl peptidase I (TPP-I).•S4 subsite of TPP-I allows electrostatic interaction of with substrate N-terminus amino group.•KCl activated TPP-I in contrast to the inhibition by Ca2+ and NaCl.•Solvent kinetic isotope effects show the role of N-terminus amino group in TPP-I catalytic process.

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关键词

TPP-I,Tripeptidyl amino peptidase,Endopeptidase,FRET peptides

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