Substrate Specificity of the Collagenolytic Serine Protease from Uca pugilator. Studies with Noncollagenous Substrates

Gregory A. Grant, Arthur Z. Eisen

Research output: Contribution to journalArticle

41 Scopus citations

Abstract

The collagenolytic serine protease (crab protease) isolated from the hepatopancreas of the fiddler crab, Uca pugilator, has been investigated with respect to its peptide bond specificity and catalytic properties by using noncollagenous substrates. In contrast to vertebrate collagenases, crab protease is a good general protease capable of degrading a variety of polypeptide and synthetic low molecular weight substrates. Crab protease displays a broad range of specificity, cleaving on the carboxyl-terminal side of residues with both positively and negatively charged side chains as well as hydrophobic side chains. The enzyme appears to favor tyrosyl, phenylalanyl, leucyl, and perhaps lysyl residues and, to a lesser extent, arginyl and glutamyl residues. The rate of cleavage of polypeptide substrates is similar to chymotrypsin but is significantly less than trypsin or chymotrypsin for low molecular weight esterase and amidase substrates. Crab protease is effectively inhibited by chymostatin but not by leupeptin or elastatinal. Several common chloromethyl ketone derivatives of phenylalanine and lysine are also ineffective, although crab protease efficiently cleaves at these residues in polypeptide substrates.

Original languageEnglish
Pages (from-to)6089-6095
Number of pages7
JournalBiochemistry
Volume19
Issue number26
DOIs
StatePublished - Feb 1 1980

Fingerprint Dive into the research topics of 'Substrate Specificity of the Collagenolytic Serine Protease from Uca pugilator. Studies with Noncollagenous Substrates'. Together they form a unique fingerprint.

  • Cite this