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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 chemistry pharmacology urine 
Binding Sites Crystallography, X-Ray Humans Amino Acid Sequence Animals Models, Molecular Molecular Sequence Data Protein Binding Models, Chemical Catalysis Protein Folding Sequence Homology, Amino Acid Recombinant Proteins Mutation Kinetics Dimerization Substrate Specificity Hydrolysis Magnesium Ligands Rats Bacillus subtilis Enzyme Inhibitors Ions Serine Mutagenesis Bacillus Cations Electrophoresis, Polyacrylamide Gel Glutarates Oxo-Acid-Lyases X-Ray Diffraction 
23 (Last update: 03/16/2019 4:33:53pm)  
J Biol Chem. 2006 Mar 17;281(11):7526-32. Epub 2005 Dec 5.