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Paper Details

Crystal structures of two bacterial 3-hydroxy-3-methylglutaryl-CoA lyases suggest a common catalytic mechanism among a family of TIM barrel metalloenzymes cleaving carbon-carbon bonds.
J Biol Chem
26
2006
2-isopropylmalate, 2-isopropylmalate synthase, 3-hydroxy-3-methylglutaryl-CoA, 3-hydroxy-3-methylglutaryl-coenzyme A, 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) lyase, 4-hydroxy-2-ketovalerate, 4-hydroxy-2-ketovalerate aldolase, Arg, Asp, Asp-Arg, Bacillus subtilis, Brucella melitensis, DRE, DRE-TIM metallolyases, Glu, HMG-CoA, HMG-CoA lyase, HMG-CoA lyases from Bacillus subtilis, TIM, TIM barrel enzymes, TIM barrel metalloenzymes, TIM metallolyases, autosomal recessive disorder, bacterial 3-hydroxy-3-methylglutaryl-CoA lyases, carbon, carbon-carbon, enolate, human, human HMG-CoA lyase, human orthologue, hypoglycemia, leucine, primary metabolic aciduria, transcarboxylase 5S, triose-phosphate, triose-phosphate isomerase

Datasets

Release 1.2