教師簡介

代表著作

  • Wei, C. L., Yang, Y. B., Liu, W. C., Chen, W. Y., Liaw, S. H.*, and Ysai, Y. C.* Mutational Shuffling of Streptomyces clavuligerus Deacetoxycephalosporin C Synthase to Improve Penicillin G Expansion. In submission.
  • Chen, S. C., Shen, C. Y., Yen, T. M., Yu, H. C., Chang, T. H., Lai, W. L., and Liaw, S. H.* Evolution of vitamin B2 biosynthesis: eubacterial RibG and fungal Rib2 deaminases. Acta Cryst. D In press
  • Huang, Y. L., Chung, T. W., Chen, C. H, Chang, C. M., Liao, C. C., Tsay, Y. G., Shaw, G. C., Liaw, S. H., Sun, C. M., and Lin, C. H.* Qualitative analysis of the fluorophosphonate-based chemical probes using the serine hydrolases from mouse liver and poly-3-hydroxybutyrate depolymerase (PhaZ) from Bacillus thuringiensis Anal. Bioanal. Chem. In press
  • Huang, T. H., Peng, H. J., Su, S. N., and Liaw, S. H.* (2012) Various cross-reactivity of the grass pollen group 4 allergens: crystallographic study of the Bermuda grass isoallergen Cyn d 4. Acta Cryst. D68, 1303-1310
  • Chen, C. S., Chiou, C. T., Chen, G., Chen, S. C., Hu, C. Y., Chi, W. K., Chu, Y. D., Hwang, L. H., Chen, P. J., Liaw, S. H.*, Chen, D. S.*, and Chern, J. W.* (2009) Structure-based discovery of triphenylmethane derivatives as inhibitors of hepatitis C virus helicase. J. Med. Chem. 52, 2716-2723
  • Chen, S. C., Lin, Y. H, Yu, H. C., and Liaw, S. H.* (2009) Complex structure of Bacillus subtilis RibG: the reduction mechanism during riboflavin biosynthesis. J. Biol. Chem. 284, 1725-1731
  • Huang, C. H., Winkler, A., Chen, C. L., Lai, W. L., Tsai, Y. C., Macheroux, P., and Liaw, S. H.* (2008) Functional roles of the 6-S-cysteinyl, 8-N1-histidyl FAD in glucooligosaccharide oxidase from Acremonium strictum. J. Biol. Chem. 283, 30990-30996
  • Chen, S. C., Chang, Y. C, Lin, C. H, Lin, C. H., and Liaw, S. H.* (2006) Crystal structure of Bacillus subtilis RibG: The ring structure of the deaminase-reductase in the riboflavin biosynthesis. J. Biol. Chem. 281, 7605-7613
  • Huang, C. H., Lai, W. L., Lee, M. H., Chen, C. J., Vasella, A., Tsai, Y. C., and Liaw, S. H.* (2005) Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: A novel flavinylation of 6-S-cysteinyl, 8a-N1-histidyl FAD. J. Biol. Chem. 280, 38831-38838.
  • Lai, W. L., Lee, M. H., Liaw, S. H.*, and Tsai, Y. C. (2005) Structural characterization of glucooligosaccharide oxidase from Acremonium strictum. Appl. Environ. Microbiol. 71, 8881-8887.
  • Wei, C. L.,Yang, Y. B., Deng, C. H., Liu, W. C., Hsu, J. S., Lin, Y. C., Liaw, S. H.*, and Tsai, Y. C.* (2005) Directed evolution of Streptomyces clavuligerus deacetoxycephalosporin c synthase for enhancement of penicillin G expansion. Appl. Environ. Microbiol. 71, 8873-8870.
  • Tsai, M. L., Liaw, S. H.*, and Chang, N. C.* (2004) The high-resolution crystal structure of Ym1 suggests a lack of N-acetylglucosamine-binding affinity. J. Struct. Biol. 148, 290-296.
  • Hsu, J. S., Yang, Y. B., Deng, C. H., Wei, C. L., Liaw, S. H.*, and Tsai, Y. C.* (2004) Family shuffling of expandase genes to enhance substrate specificty to penicillin G. Appl. Environ. Microbiol. 70, 6257-6263.
  • Liaw, S. H.*, Chang, Y. J., Lai, C. T., Chang, H. C., and Chang, G. G. (2004) Crystal structure of the Bacillus subtilis guanine deaminase. The first domain-swapped structure in the cytidine deaminase superfamily. J. Biol. Chem. 279, 35479-35485.
  • Lai, W. L., Chou, L. Y., Ting, C. Y., Kirby, R., Tsai, Y. C., Wang, A. H. J., and Liaw, S. H.* (2004) The functional role of the binuclear metal center in D-aminoacylase. One-metal activation and second-metal inhibition. J. Biol. Chem. 279, 13962-13967.
  • Ko, T.P., Lin, J. J., Hu, C. Y., Hsu, Y. H., Wang, A. H. J., and Liaw, S. H.* (2003) Crystal structure of the yeast cytosine deaminase. Insights into the enzyme mechanism and evolution. J. Biol. Chem. 278, 19111-19117.
  • Liaw, S. H., Chen, S. J., Ko, T. P., Hsu, C. S., Chen, C. J., Wang, A. H. J.*, and Tsai, Y. C.* (2003) Crystal Structure of D-aminoacylase from Alcaligenes faecalis DA1. A Novel subset of amidohydrolases and insights into the enzyme mechanism. J. Biol. Chem. 278, 4957-4962.