NDLI: A protease responsible for post-translational cleavage of a conserved Asn-Gly linkage in glycinin, the major seed storage protein of soybean.

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A protease responsible for post-translational cleavage of a conserved Asn-Gly linkage in glycinin, the major seed storage protein of soybean.

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A protease responsible for post-translational cleavage of a conserved Asn-Gly linkage in glycinin, the major seed storage protein of soybean.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Jung, R. Muntz, K. Nielsen, N. C. Scott, M. P.
Description	Author Affiliation: Scott MP ( U.S. Department of Agriculture Agricultural Research Service, Department of Agronomy, Purdue University, West Lafayette, IN 47907.);
Abstract	The assembly of 11S globulin seed storage proteins in plants is regulated in part by the activity of a protease that cleaves between asparagine and glycine residues. Post-translational cleavage of subunit precursors into acidic and basic polypeptides is associated with the ability of subunits in trimers to aggregate into hexamers in vitro. An activity is present in extracts from immature soybean seeds that specifically cleaves immature 11S seed storage proteins of soybean and Vicia faba into the polypeptides of the mature proteins. Sequence microanalysis has been used to demonstrate that proglycinin and prolegumin are cut at the legitimate site when proteins synthesized in vitro are used as substrates. A single amino acid change in the cleavage site renders the substrate uncleavable. The protease responsible for this activity also hydrolyzes a synthetic octapeptide whose sequence reproduces four amino acids on either side of the glycinin subunit G4 cleavage site. This assay permitted the purification and characterization of the protease. It is a glycosylated enzyme with an acidic pH optimum and a molecular mass of about 45 kDa in solution.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	2
Volume Number	89
Language	English
Publisher	National Academy of Sciences
Publisher Date	1992-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Endopeptidases Isolation & Purification Globulins Metabolism Plant Proteins Soybeans Enzymology Vegetable Proteins Amino Acid Sequence Chemistry Molecular Sequence Data Molecular Weight Peptides Protein Processing, Post-Translational Soybean Proteins Structure-Activity Relationship Substrate Specificity Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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