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New insights into substrate folding preference of plant OSCs

Science Bulletin 2016年第18期61卷 1407-1412页

作者： Yongshuo Ma Yuan Zhou Sergey Ovchinnikov Per Jr.Greisen Sanwen Huang Yi Shang Institute of Vegetables and Flowers Chinese Academy of Agricultural Sciences Key Laboratory of Biology and Genetic Improvement of Horticultural Crops of the Ministry of Agriculture Sino-Dutch Joint Laboratory of Horticultural Genomics Department of Biochemistry University of Washington Department of Modelling Novo Nordisk A/S 2760 Ml?vDenmark Agricultural Genomic Institute at Shenzhen Chinese Academy of Agricultural Sciences

Sterols and triterpenes are structurally diverse bioactive molecules generated through cyclization of linear 2,3-oxidosqualene. Based on carbocationic intermediates generated during initial substrate preorganization step, oxidosqualene cyclases （OSCs） are roughly segregated into protosteryl cation group that mainly catalyzes tetracyclic products and dammarenyl cation group which mostly generates pentacyclic products. However, in contrast to well-studied cascade of ring-forming reactions, little is known about the mechanism underlying the initial sub- strate folding process. Previously, we have identified a cucurbitadienol synthase （Bi） and its null allele bi （C393Y） from cucumber. By integration of homology modeling, residue coevolution and site-directed mutagenesis, we discover that four covarying amino acids including C393 constitute a dynamic domain that may be involved in substrate folding process for Bi. We also reveal a group of co-conserved residues that closely associated with the segregation of plant OSCs. These residues may act col- laboratively in choice of specific substrate folding inter- mediate for OSCs. Thus, engineer plant OSCs from into five-ringed producer. our findings open a door to four-ringed skeleton catalysts

关键词： Oxidosqualene cyclase Homologymodeling Residue coevolution substrate folding

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