Deletion of the Gly600 residue of Alicyclobacillus acidocaldarius squalene cyclase alters the substrate specificity into that of the eukaryotic-type cyclase specific to (3S)-2,3-oxidosqualene.
Hoshino
Tsutomu
T
Department of Applied Biological Chemistry, Faculty of Agriculture and Graduate School of Science and Technology, Niigata University, Ikarashi, Niigata 950-2181, Japan. hoshitsu@agr.niigata-u.ac.jp
Shimizu
Kunio
K
Sato
Tsutomu
T
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology* / Q000235:genetics; D001665:Binding Sites; D003500:Cyclization; D019751:Intramolecular Transferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008190:Lyases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D016133:Polymerase Chain Reaction; D013185:Squalene / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity; D014315:Triterpenes / Q000737:chemistry / Q000378:metabolism
C002821:2,3-oxidosqualene; D014315:Triterpenes; D013185:Squalene; D008190:Lyases; C022651:squalene cyclase; D019751:Intramolecular Transferases; C021924:lanosterol synthase