Bacterial and mammalian HMG-CoA reductases: related enzymes with distinct architectures.
The committed step in the biosynthesis of isoprenoids is catalyzed by HMG-CoA reductase. Recently determined structures of the distantly related bacterial and mammalian HMG-CoA reductases have revealed two distinct classes of the protein with differently formed active sites and oligomeric states. An appreciation of the remarkable differences in the active site architecture may ultimately lead to the development of novel antibacterial agents.
Istvan
E S
ES
Howard Hughes Medical Institute and Department of Microbiology, Washington University School of Medicine, St Louis, MO 63110, USA. Istvan@borcim.wustl.edu
D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria / Q000201:enzymology / Q000378:metabolism; D001665:Binding Sites; D002384:Catalysis; D020134:Catalytic Domain; D019143:Evolution, Molecular; D006801:Humans; D006903:Hydroxymethylglutaryl CoA Reductases / Q000737:chemistry*; D019161:Hydroxymethylglutaryl-CoA Reductase Inhibitors; D008322:Mammals; D008969:Molecular Sequence Data; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment
D019161:Hydroxymethylglutaryl-CoA Reductase Inhibitors; D006903:Hydroxymethylglutaryl CoA Reductases