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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.

Forouhar F, Hussain M, Farid R, Benach J, Abashidze M, Edstrom WC, Vorobiev SM, Xiao R, Acton TB, Fu Z, Kim JJ, Miziorko HM, Montelione GT, Hunt JF,
Journal of Biological Chemistry (2006) 281(11):7533-45 PublishedPSI:Phase 2  
Northeast Structural Genomics Consortium

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The enzyme 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) lyase catalyzes the terminal steps in ketone body generation and leucine degradation. ...
chemistry enzymology 
Binding Sites Catalytic Domain Crystallography, X-Ray Humans Protein Structure, Tertiary Amino Acid Sequence Models, Molecular Molecular Sequence Data Protein Binding Protein Structure, Secondary Models, Chemical Oxidative Stress Catalysis Chromatography, Gel Protein Conformation Protein Folding Sequence Homology, Amino Acid Kinetics Lysine Stereoisomerism Aspartic Acid Carbon Bacillus subtilis Point Mutation Light Scattering, Radiation Cations Oxo-Acid-Lyases 2-Isopropylmalate Synthase Brucella melitensis 
16330546  
10.1074/jbc.M507996200  
21 (Last update: 11/17/2018 12:13:53pm)  
1YDN
1YDO  
structure  
multiple pdbids [1ydo,1ydn]