PMID: 2500950May 1, 1989Paper

The thiol proteinases from the latex of Carica papaya L. III. The primary structure of chymopapain

Biological Chemistry Hoppe-Seyler
A JacquetG Braunitzer

Abstract

The amino-acid sequence of chymopapain is presented. It was isolated from the latex of the fruits from the tropical species Carica papaya L. and is, besides papain and papaya proteinase omega, the third thiol proteinase from this source. The primary structure contains 218 amino-acid residues. It was deduced from sequence analysis of the native enzyme and of peptides obtained by tryptic, chymotryptic, peptic, thermolysinolytic and mild acidic hydrolysis. Out of a total of eight cysteine residues, six are involved in the formation of three disulfide bonds, the location of which has been established with the help of peptic and thermolysinolytic peptides and fragments, obtained by mild acidic hydrolysis. Chymopapain shares 126 identical amino-acid residues (58%) with papain and 141 (65%) with papaya proteinase omega, including the three disulfide bridges and the free cysteine in position 25, required for activity. Except some amino-acid residues in the substrate-binding site, all residues involved in the catalytic mechanism are conserved. The homology between papaya proteinases is discussed.

Citations

Jan 11, 2002·European Journal of Biochemistry·Soghra Khatun HaqRizwan Hasan Khan
May 15, 1993·European Journal of Biochemistry·I G SumnerP W Goodenough
Nov 20, 1989·FEBS Letters·A RitonjaA J Barrett
May 28, 2003·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Mohamed AzarkanYvan Looze
Dec 17, 1996·Biochemistry·D MaesY Looze

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