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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Sellner, J. M. Frisch, D. A. Shaver, J. M. Gengenbach, B. G. Bittel, D. C. Somers, D. A. |
| Description | Author Affiliation: Shaver JM ( Department of Agronomy and Plant Genetics, University of Minnesota, St. Paul 55108, USA.); |
| Abstract | Dihydrodipicolinate synthase (DHPS; EC 4.2.1.52) catalyzes the first step in biosynthesis of lysine in plants and bacteria. DHPS in plants is highly sensitive to end-product inhibition by lysine and, therefore, has an important role in regulating metabolite flux into lysine. To better understand the feedback inhibition properties of the plant enzyme, we transformed a maize cDNA for lysine-sensitive DHPS into an Escherichia coli strain lacking DHPS activity. Cells were mutagenized with ethylmethanesulfonate, and potential DHPS mutants were selected by growth on minimal medium containing the inhibitory lysine analogue S-2-aminoethyl-L-cysteine. DHPS assays identified surviving colonies expressing lysine-insensitive DHPS activity. Ten single-base-pair mutations were identified in the maize DHPS cDNA sequence; these mutations were specific to one of three amino acid residues (amino acids 157, 162, and 166) localized within a short region of the polypeptide. No other mutations were present in the remaining DHPS cDNA sequence, indicating that altering only one of the three residues suffices to eliminate lysine inhibition of maize DHPS. Identification of these specific mutations that change the highly sensitive maize DHPS to a lysine-insensitive isoform will help resolve the lysine-binding mechanism and the resultant conformational changes involved in inhibition of DHPS activity. The plant-derived mutant DHPS genes may also be used to improve nutritional quality of maize or other cereal grains that have inadequate lysine content when fed to animals such as poultry, swine, or humans. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 5 |
| Volume Number | 93 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1996-09-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Hydro-Lyases Chemistry Zea Mays Enzymology Amino Acid Sequence Bacterial Proteins DNA, Complementary Genetics Enzyme Inhibitors Pharmacology Antagonists & Inhibitors Kinetics Lysine Molecular Sequence Data Plant Proteins Point Mutation Sequence Alignment Structure-Activity Relationship Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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