دورية أكاديمية
Analysis of conformationally restricted alpha-ketoglutarate analogues as substrates of dehydrogenases and aminotransferases.
| العنوان: | Analysis of conformationally restricted alpha-ketoglutarate analogues as substrates of dehydrogenases and aminotransferases. |
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| المؤلفون: | Denton TT; Department of Chemistry, University of Montana, Missoula, Montana 59812, USA., Thompson CM, Cooper AJ |
| المصدر: | Analytical biochemistry [Anal Biochem] 2001 Nov 15; Vol. 298 (2), pp. 265-74. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Country of Publication: United States NLM ID: 0370535 Publication Model: Print Cited Medium: Print ISSN: 0003-2697 (Print) Linking ISSN: 00032697 NLM ISO Abbreviation: Anal Biochem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: <2000- > : San Diego, CA : Elsevier Original Publication: Orlando Fl : Academic Press |
| مواضيع طبية MeSH: | Glutamic Acid/*analogs & derivatives , Ketoglutarate Dehydrogenase Complex/*metabolism , Ketoglutaric Acids/*metabolism , Oxidoreductases/*metabolism , Transaminases/*metabolism, Animals ; Cattle ; Chromatography, High Pressure Liquid ; Glutamic Acid/metabolism ; Heart/physiology ; Kinetics ; Liver/enzymology ; Mass Spectrometry ; Mathematics ; Molecular Conformation ; Muscles/enzymology ; Rabbits ; Rats ; Substrate Specificity ; Swine |
| مستخلص: | Five synthetic, conformationally restricted alpha-ketoglutarate analogues were tested as substrates of a variety of dehydrogenases and aminotransferases. The compounds were found not to be detectable substrates of glutamate dehydrogenase, L-leucine dehydrogenase, L-phenylalanine dehydrogenase, lactate dehydrogenase, malate dehydrogenase, glutamine transaminase K, aspartate aminotransferase, alanine aminotransferase, and alpha-ketoglutarate dehydrogenase complex. However, two thermostable aminotransferases were identified that catalyze transamination between several L-amino acids (e.g., phenylalanine, glutamate) and the alpha-ketoglutarate analogues of interest. Transamination between L-glutamate (or L-phenylalanine) and the alpha-ketoglutarate analogues was found to be 0.13 to 1.08 micromol/h/mg at 45 degrees C. The products resulting from transamination between L-phenylalanine and the alpha-ketoglutarate analogues were separated by reverse-phase HPLC, and the newly formed amino acid analogues were analyzed by LC-MS in an ion selective mode. In each case, the ions obtained were consistent with the expected product and a representative example is provided. The possibility existed that although the alpha-ketoglutarate analogues are not substrates of the dehydrogenases and most of the aminotransferases investigated, they might be good inhibitors. Weak inhibition of aminotransferases and glutamate dehydrogenase was found with some of the alpha-ketoglutarate analogues. The newly available thermostable aminotransferases may have general utility in the synthesis of bulky L-amino acids from the corresponding alpha-keto acids. (Copyright 2001 Academic Press.) |
| معلومات مُعتمدة: | NS38248 United States NS NINDS NIH HHS |
| المشرفين على المادة: | 0 (Ketoglutaric Acids) 3KX376GY7L (Glutamic Acid) EC 1.- (Oxidoreductases) EC 1.2.4.2 (Ketoglutarate Dehydrogenase Complex) EC 2.6.1.- (Transaminases) |
| تواريخ الأحداث: | Date Created: 20011110 Date Completed: 20020314 Latest Revision: 20181130 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1006/abio.2001.5366 |
| PMID: | 11700982 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 0003-2697 |
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| DOI: | 10.1006/abio.2001.5366 |