TOWARD A BLUEPRINT FOR β-PRIMEVEROSIDASE FROM TEA LEAVES STRUCTURE/FUNCTION PROPERTIES:HOMOLOGY MODELING STUDY
By means of the Homology modeling and the known structure of cyannogenic 000-glycosidase from white clover (1CBG, EC 3-2.1.21), we construct a 3D model of the β-primeverosidase (EC 3.2.1.149) and search for the binding site of substrate. The 3D model is then refined by using molecular mechanics (optimization and molecular dynamics) simulation. Finally, the refined model is further assessed by Profile-3D and PROCHECK, and the results showed that the final model is reliable. Further more, the docking of the substrates into the active site of the protein indicates that β-primeverosidase is able to hydrolyze β-primeverosides, but not act on 2-phenylethyl β-D-glucopyranoside. These results suggest that β-primeverosidase shows broad sub strate specificity with respect to the disaccharide glycon moiety subsite-2). This is consistent with the experimental observation. Thr271 and Thr415 play important roles in subsite-2 of β-primeverosidase. Our results may be helpful for further experimental investigations.
β-Primeverosidase molecular dynamics docking.
WEI-WEI HAN ZE-SHENG LI QING-CHUAN ZHENG CHIA-CHUNG SUN
Institute of Theoretical Chemistry, State Key Laboratory of Theoretical and Computational Chemistry, Jilin University Changchun 130023, P.R.China
国际会议
杭州
英文
1491-1504
2007-04-01（万方平台首次上网日期，不代表论文的发表时间）