Crystallization and preliminary X-ray diffraction analysis of various enzyme–substrate complexes of isopropylmalate dehydrogenase fromThermus thermophilus
| Autor: | Karuppasamy Manikandan, Linda Schuldt, Manfred S. Weiss, Péter Závodszky, Angelo Merli, Rajesh Kumar Singh, Mária Vas, Éva Gráczer |
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| Rok vydání: | 2010 |
| Předmět: |
3-Isopropylmalate Dehydrogenase
Biophysics Dehydrogenase Crystallography X-Ray Biochemistry Cofactor Substrate Specificity Divalent law.invention Structural Biology law Genetics Crystallization chemistry.chemical_classification biology Thermus thermophilus Substrate (chemistry) Condensed Matter Physics biology.organism_classification Crystallography chemistry Crystallization Communications biology.protein NAD+ kinase |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66:738-743 |
| ISSN: | 1744-3091 |
| Popis: | The Thermus thermophilus 3-isopropylmalate dehydrogenase (Tt-IPMDH) enzyme catalyses the penultimate step of the leucine-biosynthesis pathway. It converts (2R,3S)-3-isopropylmalate to (2S)-2-isopropyl-3-oxosuccinate in the presence of divalent Mg(2+) or Mn(2+) and with the help of NAD(+). In order to elucidate the detailed structural and functional mode of the enzymatic reaction, crystals of Tt-IPMDH were grown in the presence of various combinations of substrate and/or cofactors. Here, the crystallization, data collection and preliminary crystallographic analyses of six such complexes are reported. |
| Databáze: | OpenAIRE |
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