Cleavage specificity of cucumisin, a plant serine protease.

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.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Uchikoba T,Yonezawa H,Kaneda M

doi

10.1093/oxfordjournals.jbchem.a124817

subject

Has Abstract

pub_date

1995-05-01 00:00:00

pages

1126-30

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

117

pub_type

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