Tryptophan 232 within oxidosqualene-lanosterol cyclase from Saccharomyces cerevisiae influences rearrangement and deprotonation but not cyclization reactions.
[reaction: see text] Oxidosqualene-lanosterol cyclases convert oxidosqualene to lanosterol in yeast and mammals. Site-saturated mutants' construction of Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase, at Trp232 exchanges against proteinogenic amino acids, and product profiles are shown. All mutants, except Lys and Arg, produced protosta-12,24-dien-3beta-ol, lanosterol, and parkeol. Overall, Trp232 plays a catalytic role in the influence of rearrangement process and determination of deprotonation position but does not involve intervention in the cyclization steps.
Department of Biological Science and Technology and Department of Applied Chemistry, National Chiao Tung University, 300 Hsin-Chu, Taiwan, Republic of China.
Tung-Kung
TK
Wu
Mei-Ting
MT
Yu
Yuan-Ting
YT
Liu
Cheng-Hsian
CH
Chang
Hsing-Ju
HJ
Wang
Eric Wei-Guang
EW
Diau
D001120:Arginine / Q000737:chemistry / Q000235:genetics; D002384:Catalysis; D003500:Cyclization; D019751:Intramolecular Transferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008239:Lysine / Q000737:chemistry / Q000235:genetics; D010084:Oxidation-Reduction; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics*; D014364:Tryptophan / Q000737:chemistry*
D014364:Tryptophan; D001120:Arginine; D019751:Intramolecular Transferases; C021924:lanosterol synthase; D008239:Lysine