دورية أكاديمية
Essential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1.
العنوان: | Essential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1. |
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المؤلفون: | Roche TE; Department of Biochemistry, Kansas State University, Manhattan, Kansas 66506, USA. bchter@ksu.edu, Hiromasa Y, Turkan A, Gong X, Peng T, Yan X, Kasten SA, Bao H, Dong J |
المصدر: | European journal of biochemistry [Eur J Biochem] 2003 Mar; Vol. 270 (6), pp. 1050-6. |
نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Review |
اللغة: | English |
بيانات الدورية: | Publisher: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Country of Publication: England NLM ID: 0107600 Publication Model: Print Cited Medium: Print ISSN: 0014-2956 (Print) Linking ISSN: 00142956 NLM ISO Abbreviation: Eur J Biochem Subsets: MEDLINE |
أسماء مطبوعة: | Publication: -2004: Oxford, UK : Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Original Publication: Berlin, New York, Springer. |
مواضيع طبية MeSH: | Protein Structure, Tertiary*, Isoenzymes/*metabolism , Protein Kinases/*metabolism , Pyruvate Dehydrogenase (Lipoamide)-Phosphatase/*metabolism, Animals ; Calcium/metabolism ; Enzyme Activation ; Isoenzymes/chemistry ; Models, Molecular ; Protein Kinases/chemistry ; Protein Serine-Threonine Kinases ; Protein Subunits ; Pyruvate Dehydrogenase (Lipoamide)-Phosphatase/chemistry ; Pyruvate Dehydrogenase Acetyl-Transferring Kinase |
مستخلص: | Four pyruvate dehydrogenase kinase and two pyruvate dehydrogenase phosphatase isoforms function in adjusting the activation state of the pyruvate dehydrogenase complex (PDC) through determining the fraction of active (nonphosphorylated) pyruvate dehydrogenase component. Necessary adaptations of PDC activity with varying metabolic requirements in different tissues and cell types are met by the selective expression and pronounced variation in the inherent functional properties and effector sensitivities of these regulatory enzymes. This review emphasizes how the foremost changes in the kinase and phosphatase activities issue from the dynamic, effector-modified interactions of these regulatory enzymes with the flexibly held outer domains of the core-forming dihydrolipoyl acetyl transferase component. |
Number of References: | 33 |
معلومات مُعتمدة: | DK 18320 United States DK NIDDK NIH HHS |
المشرفين على المادة: | 0 (Isoenzymes) 0 (Protein Subunits) 0 (Pyruvate Dehydrogenase Acetyl-Transferring Kinase) EC 2.7.- (Protein Kinases) EC 2.7.11.1 (Protein Serine-Threonine Kinases) EC 3.1.3.43 (Pyruvate Dehydrogenase (Lipoamide)-Phosphatase) SY7Q814VUP (Calcium) |
تواريخ الأحداث: | Date Created: 20030313 Date Completed: 20030509 Latest Revision: 20211203 |
رمز التحديث: | 20231215 |
DOI: | 10.1046/j.1432-1033.2003.03468.x |
PMID: | 12631265 |
قاعدة البيانات: | MEDLINE |
تدمد: | 0014-2956 |
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DOI: | 10.1046/j.1432-1033.2003.03468.x |