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Crystal structure of human 3-hydroxy-3-methylglutaryl-CoA Lyase: insights into catalysis and the molecular basis for hydroxymethylglutaric aciduria.

Fu Z, Runquist JA, Forouhar F, Hussain M, Hunt JF, Miziorko HM, Kim JJ,
Journal of Biological Chemistry (2006) 281(11):7526-32 PublishedPSI:Phase 2  
Northeast Structural Genomics Consortium

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3-Hydroxy-3-methylglutaryl-CoA (HMG-CoA) lyase is a key enzyme in the ketogenic pathway that supplies metabolic fuel to extrahepatic tissues. ...
metabolism pharmacology chemistry urine 
Crystallography, X-Ray X-Ray Diffraction Glutarates Dimerization Hydrolysis Magnesium Models, Chemical Ligands Ions Protein Folding Substrate Specificity Binding Sites Electrophoresis, Polyacrylamide Gel Amino Acid Sequence Sequence Homology, Amino Acid Cations Serine Models, Molecular Recombinant Proteins Bacillus subtilis Mutation Humans Molecular Sequence Data Enzyme Inhibitors Bacillus Animals Kinetics Mutagenesis Oxo-Acid-Lyases Rats Protein Binding Catalysis 
21 (Last update: 07/22/2017 11:25:23am)  
J Biol Chem. 2006 Mar 17;281(11):7526-32. Epub 2005 Dec 5.