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.
Wu
Tung-Kung
TK
Department of Biological Science and Technology and Department of Applied Chemistry, National Chiao Tung University, 300 Hsin-Chu, Taiwan, Republic of China.
Yu
Mei-Ting
MT
Liu
Yuan-Ting
YT
Chang
Cheng-Hsian
CH
Wang
Hsing-Ju
HJ
Diau
Eric Wei-Guang
EW
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