On the active site of elastase: Partial mapping by means of specific peptide substrates

Daphna Atlas*, S. Levit, I. Schechter, A. Berger

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

57 Scopus citations

Abstract

RNase-S peptide as well as some related octa- and hexapeptides were found to be highly, reactive substrates of porcine elastase (e.g. Ala4-Lys-Phe: Km = 4500 M-1, kcat = 32 sec-1, C = 1.4 × 105 M-1 sec-1). Comparison of the various peptides led to the conclusion that the active site of porcine elastase is composed of 6-7 subsites (c.f. [1]). Preliminary mapping shows that subsites S2, S′1 and S′2 have hydrophobic character. Occupation of subsite S4 by the substrate is important for efficient hydrolysis. Binding at this subsite was found to be stereospecific.

Original languageEnglish
Pages (from-to)281-283
Number of pages3
JournalFEBS Letters
Volume11
Issue number4
DOIs
StatePublished - 11 Dec 1970
Externally publishedYes

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