Autoproteolytic processing of aspartic proteinase from sunflower seeds

Bioscience, Biotechnology, and Biochemistry
H ParkH Kobayashi

Abstract

The autoproteolytic processing of mature aspartic proteinase from sunflower seeds was investigated. The mature aspartic proteinase (48 kDa) was processed at N65s-D66s in the plant-specific region of the enzyme to form 34-kDa and 14-kDa subunits. The next step was the hydrolysis of the A25s-Q26s and N97s-E98s bonds to form a 39-kDa enzyme that consisted of 29-kDa and 9-kDa disulfide-bonded subunits. Finally, bonds including V1s-M2s, M2s-S3s, C100s-D101s, and D101s-R102s were cleaved to form non-covalently bound subunits (29 kDa and 9 kDa) by eliminating the disulfide bonds in the plant-specific region of the protein.

References

Jul 31, 1979·Molecular and Cellular Biochemistry·J Tang
May 1, 1970·The Journal of Antibiotics·H UmezawaM Hamada
Aug 6, 1998·European Journal of Biochemistry·M Ramalho-SantosC Faro
Jul 6, 2000·Bioscience, Biotechnology, and Biochemistry·H ParkH Kobayashi

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Citations

Sep 26, 2015·Biochimie·Elfriede Dall, Hans Brandstetter
Sep 18, 2008·Phytochemistry·Miguel A Mazorra-Manzano, Rickey Y Yada
May 22, 2004·European Journal of Biochemistry·Isaura Simões, Carlos Faro
Apr 18, 2015·Journal of Plant Physiology·Hsien-Jung ChenYaw-Huei Lin
Aug 20, 2011·The FEBS Journal·Malene JørgensenKaren Gjesing Welinder
Jan 29, 2005·The Journal of Biological Chemistry·Pedro CastanheiraCarlos Faro
Jun 12, 2020·Trends in Plant Science·Lennie K Y CheungRickey Y Yada

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