Specificity of cucumisin in hydrolysis of peptide thiobenzyl esters.

Kaneda, Makoto; Minematsu, Yoshihiro; Powers, James C.; Tominaga, Naotomo

doi:10.1271/bbb1961.50.1075

Cited by 7 publications

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“…The best studied examples are cucumisin from melon and PR‐P69 from tomato. Cucumisin was the first plant SLP to be identified and has been characterized extensively (Kaneda and Tominaga 1975, Kaneda et al. 1986, Yamagata et al.…”

Section: Discussionmentioning

confidence: 99%

“…The best studied examples are cucumisin from melon and PR-P69 from tomato. Cucumisin was the first plant SLP to be identified and has been characterized extensively (Kaneda and Tominaga 1975, Kaneda et al 1986, Yamagata et al 1994. Cucumisin is a thermostable alkaline serine protease found in the juice of melon, and is synthesized as a large inactive precursor of about 78 kDa.…”

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Two subtilisin‐like proteases from soybean

Beilinson

Moskalenko

Livingstone

et al. 2002

Physiologia Plantarum

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Two subtilisin-like proteases (SLP) were identified in soybean (Glycine max [L.] Merr.). The first, SLP-1, was localized in seed coats early in seed development, but became undetectable with anti-SLP-1 antibodies as seed fill progressed. A partial purification of SLP-1 was achieved using a two step chromatographic procedure. NH2-terminal sequence analysis of the partially purified enzyme permitted primers to be designed that were used to amplify cDNA encoding SLP-1. A genomic clone encoding SLP-1 was also obtained. Characterization of the cDNA and partially purified SLP-1 revealed the initial translation product was an 82 694 MW precursor. After removal of a signal peptide, the mature protein was formed by removal of an NH2-terminal propeptide. A COOH-terminal peptide also appeared to be removed from some of the protease molecules. DNA blot analysis suggested that at least one additional SLP gene was present in soybean. The second gene, SLP-2, was subsequently cloned and characterized. Although the coding regions for SLP-1 and SLP-2 were homologous, their promoters were quite divergent. RT-PCR revealed that SLP-2 message was found in the mature plant and in cotyledons of germinating seeds. Although SLP-2 mRNA could be identified in developing seeds, the message was at least an order of magnitude less abundant than that for SLP-1, and it was mis-spliced such that a chain termination event would preclude obtaining a product. As with SLPs from other organisms, the functions of the soybean proteases are unknown. However, SLP-1 is one of only a few proteins from soybean seed coats that have been described.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Two subtilisin‐like proteases from soybean

Beilinson

Moskalenko

Livingstone

et al. 2002

Physiologia Plantarum

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Enzyme Handbook

Schomburg¹,

Salzmann²

1991

Enzyme Handbook

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Milk-clotting activity of cucumisin, a plant serine protease from melon fruit

Uchikoba

Kaneda

1996

Appl Biochem Biotechnol

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Cucumisin (EC 3.4.21.25) isolated from prince melon fruit is a plant serine protease. Its milk-clotting activity was compared with plant cysteine proteases such as papain (EC 3.4.22.2) and ficain (EC 3.4.22.3). Cucumisin was more stable than papain under the condition of pH 7.1, 37 degrees C for 24 h. The milk-clotting activity of cucumisin was the same to that of papain and was half value of that of ficain.

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Specificity of cucumisin in hydrolysis of peptide thiobenzyl esters.

Cited by 7 publications

References 0 publications

Two subtilisin‐like proteases from soybean

Two subtilisin‐like proteases from soybean

Enzyme Handbook

Milk-clotting activity of cucumisin, a plant serine protease from melon fruit

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