Squalene-hopene cyclase: catalytic mechanism and substrate recognition.
Rapid progress on the catalytic mechanism and substrate recognition by squalene-hopene cyclase, which has occurred only in the last several years, is reported. A series of site-directed mutation experiments and some squalene analogues have provided deep insight into the polycyclization mechanism and catalytic sites in conjunction with the information from X-ray crystal data.
Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University, Ikarashi, Niigata 950-2181, Japan. hoshitsu@agr.niigata-u.ac.jp
Tsutomu
T
Hoshino
Tsutomu
T
Sato
D000595:Amino Acid Sequence; D000818:Animals; D002240:Carbohydrate Sequence; D002384:Catalysis; D018360:Crystallography, X-Ray; D003500:Cyclization; D016937:Gram-Positive Endospore-Forming Rods / Q000201:enzymology / Q000235:genetics; D019751:Intramolecular Transferases / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D011487:Protein Conformation; D013379:Substrate Specificity; D013769:Tetrahymena pyriformis / Q000235:genetics
D019751:Intramolecular Transferases; C066630:squalene-hopene cyclase