title: Isoprenyl diphosphate synthases.
abstract: Isoprenyl diphosphate synthases catalyze consecutive condensations of isopentenyl diphosphates with allylic primer substrates to form linear backbones for all isoprenoid compounds including cholesterol. These synthases are classified according to the final chain length of their end products and the stereochemistry of the newly formed double bonds. Mutagenesis and X-ray crystallography data have uncovered the basic catalytic and chain length determination mechanisms of E-isoprenyl diphosphate synthases and shed light on their possible evolutionary course. Although much less is known about the Z-isoprenyl diphosphate synthase family, successful cloning and subsequent crystallizations in the near future will no doubt bring more insight as researchers begin to unravel the essential components and precise reaction mechanisms of this cellular machinery.
authors: University of California, San Francisco, School of Medicine, San Francisco, CA 94143, USA.
authors: K C
authors: KC
authors: Wang
authors: S
authors: S
authors: Ohnuma
mesh_terms: D019883:Alkyl and Aryl Transferases / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria; D001426:Bacterial Proteins; D002384:Catalysis; D002784:Cholesterol / Q000096:biosynthesis*; D019143:Evolution, Molecular; D006801:Humans; D007700:Kinetics; D008956:Models, Chemical; D015394:Molecular Structure; D010802:Phylogeny; D010944:Plants; D013237:Stereoisomerism
chemical_list: D001426:Bacterial Proteins; D002784:Cholesterol; D019883:Alkyl and Aryl Transferases; C412569:Rv1086 protein, Mycobacterium tuberculosis; C499606:Rv2361c protein, Mycobacterium tuberculosis