3-isopropylmalate dehydratase, large subunit
Short name | 3-IsopropMal_deHydase_lsu |
Overlapping homologous superfamilies |
Description
References
1.The aconitase family: three structural variations on a common theme. Gruer MJ, Artymiuk PJ, Guest JR. Trends Biochem. Sci. 22, 3-6, (1997). View articlePMID: 9020582
2.Branched-chain amino acid biosynthesis genes in Lactococcus lactis subsp. lactis. Godon JJ, Chopin MC, Ehrlich SD. J. Bacteriol. 174, 6580-9, (1992). View articlePMID: 1400210
3.The organization of the leuC, leuD and leuB genes of the extreme thermophile Thermus thermophilus. Tamakoshi M, Yamagishi A, Oshima T. Gene 222, 125-32, (1998). View articlePMID: 9813279
4.Crystal structure of the Pyrococcus horikoshii isopropylmalate isomerase small subunit provides insight into the dual substrate specificity of the enzyme. Yasutake Y, Yao M, Sakai N, Kirita T, Tanaka I. J. Mol. Biol. 344, 325-33, (2004). View articlePMID: 15522288
5.Kinetics and product analysis of the reaction catalysed by recombinant homoaconitase from Thermus thermophilus. Jia Y, Tomita T, Yamauchi K, Nishiyama M, Palmer DR. Biochem. J. 396, 479-85, (2006). View articlePMID: 16524361
6.Functional specification of Arabidopsis isopropylmalate isomerases in glucosinolate and leucine biosynthesis. He Y, Chen B, Pang Q, Strul JM, Chen S. Plant Cell Physiol. 51, 1480-7, (2010). View articlePMID: 20663849
GO terms
biological process
molecular function
cellular component
- None
Cross References
ENZYME
Genome Properties