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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/LEU3_THET8 LEU3_THET8]] Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.[HAMAP-Rule:MF_01033] | [[http://www.uniprot.org/uniprot/LEU3_THET8 LEU3_THET8]] Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.[HAMAP-Rule:MF_01033] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The mutant E270A of Thermus thermophilus 3-isopropylmalate dehydrogenase exhibits largely reduced ( approximately 1%) catalytic activity and negligible activation by K(+) compared to the wild-type enzyme. A 3-4kcal/mol increase in the activation energy of the catalysed reaction upon this mutation could also be predicted by QM/MM calculations. In the X-ray structure of the E270A mutant a water molecule was observed to take the place of K(+). SAXS and FRET experiments revealed the essential role of E270 in stabilisation of the active domain-closed conformation of the enzyme. In addition, E270 seems to position K(+) into close proximity of the nicotinamide ring of NAD(+) and the electron-withdrawing effect of K(+) may help to polarise the aromatic ring in order to aid the hydride-transfer. | ||
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| + | Glutamate 270 plays an essential role in K(+)-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase.,Graczer E, Pallo A, Olah J, Szimler T, Konarev PV, Svergun DI, Merli A, Zavodszky P, Weiss MS, Vas M FEBS Lett. 2015 Jan 16;589(2):240-5. doi: 10.1016/j.febslet.2014.12.005. Epub, 2014 Dec 10. PMID:25497013<ref>PMID:25497013</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:26, 14 January 2015
Structure of the E270A Mutant Isopropylmalate dehydrogenase from Thermus thermophilus in complex with IPM, Mn and NADH
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