Importance of Saccharomyces cerevisiae oxidosqualene-lanosterol cyclase tyrosine 707 residue for chair-boat bicyclic ring formation and deprotonation reactions.
A contact mapping strategy was applied to identify putative amino acid residues that influence the oxidosqualene-lanosterol B-ring cyclization reaction. A bicyclic intermediate with two altered deprotonation products, in conjunction with lanosterol, were isolated from the ERG7(Y707X) mutants, indicating that the Tyr707 residue may play a functional role in stabilizing the chair-boat bicyclic C-8 cation and the lanosteryl C-8/C-9 cation intermediates.
Wu
Tung-Kung
TK
Department of Biological Science and Technology, National Chiao Tung University, 300, Hsin-Chu, Taiwan, Republic of China. tkwmll@mail.nctu.edu.tw
Wang
Tsai-Ting
TT
Chang
Cheng-Hsiang
CH
Liu
Yuan-Ting
YT
Shie
Wen-Shiang
WS
D019086:Bridged Bicyclo Compounds, Heterocyclic / Q000737:chemistry* / Q000378:metabolism*; D003500:Cyclization; D019751:Intramolecular Transferases / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D015394:Molecular Structure; D009154:Mutation / Q000235:genetics; D011522:Protons; D012441:Saccharomyces cerevisiae / Q000737:chemistry* / Q000201:enzymology* / Q000235:genetics; D014443:Tyrosine / Q000235:genetics / Q000378:metabolism
D019086:Bridged Bicyclo Compounds, Heterocyclic; D011522:Protons; D014443:Tyrosine; D019751:Intramolecular Transferases; C021924:lanosterol synthase