PMID: 8586630May 1, 1995Paper

Cleavage specificity of cucumisin, a plant serine protease

Journal of Biochemistry
T UchikobaM Kaneda

Abstract

Cucumisin was isolated from prince melon sarcocarp by means of a simple purification procedure. Serine protease inhibitors such as soybean trypsin inhibitor, ovomucoid, and aprotinin had no effect on the enzyme activity. alpha 2-Macroglobulin showed 38% inhibition of the original caseinolytic activity of cucumisin. The favorable synthetic substrates for cucumisin were Glt-Ala-Ala-Pro-Leu-pNA and Suc-Ala-Ala-Pro-Phe-pNA. The constant (kcat/Km) for Suc-Ala-Pro-Ala-pNA was found to be 30 times greater than that for Suc-Ala-Ala-Ala-pNA. The substrate specificity of cucumisin for oligopeptides and proteins was shown to be broad.

Citations

Mar 23, 2010·Molecular Biotechnology·Shumi Yoshida-YamamotoYukio Takii
Feb 22, 2005·The New Phytologist·Caroline Pak, Wouter G van Doorn
Jul 20, 2010·The Journal of Biological Chemistry·Masataka NakagawaHiroshi Yamagata
Dec 22, 2010·Allergology International : Official Journal of the Japanese Society of Allergology·Mojtaba SankianAbol-Reza Varasteh
May 11, 2020·Fungal Genetics and Biology : FG & B·Todd A NaumannNeil P J Price
Feb 14, 2021·Bioscience, Biotechnology, and Biochemistry·Kosaku NishimuraKiyoshi Yasukawa
Apr 4, 2000·Phytochemistry·K ArimaM Kaneda
Jul 12, 2005·Plant Physiology and Biochemistry : PPB·Cecília M Antão, F Xavier Malcata
Jul 15, 2006·Phytochemistry·Subhash C YadavM V Jagannadham
Dec 21, 2006·Journal of Agricultural and Food Chemistry·Monu PandeMedicherla V Jagannadham

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