دورية أكاديمية
Roles of lysine 219 and 255 residues in tobacco acetolactate synthase.
| العنوان: | Roles of lysine 219 and 255 residues in tobacco acetolactate synthase. |
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| المؤلفون: | Yoon TY; School of Life Science and Research Institute for Genetic Engineering, Chungbuk National University, Cheongju 361-763, Republic of Korea., Chung SM, Chang SI, Yoon MY, Hahn TR, Choi JD |
| المصدر: | Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2002 Apr 26; Vol. 293 (1), pp. 433-9. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Country of Publication: United States NLM ID: 0372516 Publication Model: Print Cited Medium: Print ISSN: 0006-291X (Print) Linking ISSN: 0006291X NLM ISO Abbreviation: Biochem Biophys Res Commun Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: <2002- >: San Diego, CA : Elsevier Original Publication: New York, Academic Press. |
| مواضيع طبية MeSH: | Lysine*, Acetolactate Synthase/*chemistry , Nicotiana/*enzymology, Acetolactate Synthase/antagonists & inhibitors ; Acetolactate Synthase/genetics ; Acetolactate Synthase/metabolism ; Amino Acid Substitution ; Circular Dichroism ; Enzyme Inhibitors/pharmacology ; Herbicides/pharmacology ; Kinetics ; Mutagenesis, Site-Directed ; Polymerase Chain Reaction ; Protein Conformation ; Recombinant Proteins/antagonists & inhibitors ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Spectrophotometry |
| مستخلص: | Acetolactate synthase (ALS) catalyzes the first common step in the biosynthesis of valine, leucine, and isoleucine. The ALS is the target of several classes of herbicides, including the sulfonylureas, the imidazolinones, and the triazolopyrimidines. The roles of three well-conserved lysine residues (K219, K255, K299) in tobacco ALS were determined using site-directed mutagenesis. The mutation of K219Q inactivated the enzyme and abolished the binding affinity for cofactor FAD. However, the secondary structure of the enzyme was not changed significantly by the mutation. Both mutants, K255F and K255Q, showed strong resistance to three classes of herbicides Londax (a sulfonylurea), Cadre (an imidazolinone), and TP (a triazolopyrimidine). In addition, there was no difference in the secondary structures of wALS and K255F. On the other hand, the mutation of K299Q did not show any significant effect on the kinetic properties or any sensitivity to the herbicides. These results suggest that Lys219 is located at the active site and is likely involved in the binding of FAD, and that Lys255 is located at a binding site common for the three herbicides in tobacco ALS. |
| المشرفين على المادة: | 0 (Enzyme Inhibitors) 0 (Herbicides) 0 (Recombinant Proteins) EC 2.2.1.6 (Acetolactate Synthase) K3Z4F929H6 (Lysine) |
| تواريخ الأحداث: | Date Created: 20020611 Date Completed: 20020705 Latest Revision: 20231213 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1016/S0006-291X(02)00249-8 |
| PMID: | 12054619 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 0006-291X |
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| DOI: | 10.1016/S0006-291X(02)00249-8 |