Structural highlights
Function
[LEU3_THETH] 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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A loop-deleted mutant form of 3-isopropylmalate dehydrogenase from Thermus thermophilus was constructed to investigate the relationship between the flexibility of the structure and the thermostability of the enzyme. The structure of the mutant enzyme was determined by X-ray crystallography and was found to be almost the same as that of the native enzyme with a reduced temperature factor. Although the mutant protein had lost the flexible loop, its function and thermostability had remained unchanged. This phenomenon can be explained by an internal reprieve tolerance mechanism.
Structure of a loop-deleted variant of 3-isopropylmalate dehydrogenase from Thermus thermophilus: an internal reprieve tolerance mechanism.,Sakurai M, Ohzeki M, Miyazaki K, Moriyama H, Sato M, Tanaka N, Oshima T Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):124-8. PMID:15299733[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sakurai M, Ohzeki M, Miyazaki K, Moriyama H, Sato M, Tanaka N, Oshima T. Structure of a loop-deleted variant of 3-isopropylmalate dehydrogenase from Thermus thermophilus: an internal reprieve tolerance mechanism. Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):124-8. PMID:15299733 doi:http://dx.doi.org/10.1107/S0907444995007190
