Department of Biochemistry

Leading the way in Biomedical Sciences

Assistant Professor YEW Wen Shan

BSC (NUS), MS, PhD (UIUC)

Yew Wen Shan

  • Assistant Professor
  • 8 Medical Drive, MD4A, #01-02, Singapore, 117597
  • (65) 6516 8624
  • bchyws@nus.edu.sg










RESEARCH INTERESTS

* Rational design and directed evolution of enzymatic activities.
* Drug design and therapeutics against infectious diseases.
* Synthetic Enzymology for biomedical and bioremediation applications.
* Deciphering enzyme specificity.
* Mechanistic enzymology of enzymes of pharmaceutical importance.
* Discovery of new enzymatic functions.

SELECTED PUBLICATIONS

1. Chow JY, Xue B, Lee KH, Tung A., Wu L, Robinson, RC, and Yew WS. (2010) Directed evolution of a thermostable quorum-quenching lactonase from the amidohydrolase superfamily. J Biol Chem. 285, 40911-40920.

2. Chow JY, Wu L, and Yew WS. (2009) Directed Evolution of a Quorum-Quenching Lactonase from Mycobacterium avium subsp. paratuberculosis K-10 in the Amidohydrolase Superfamily. Biochemistry. 48: 4344-4353.

3. Yew WS, Fedorov AA, Fedorov EV, Almo SC, and Gerlt JA. (2007) Evolution of enzymatic activities in the enolase superfamily: L-talarate/galactarate dehydratase from Salmonella typhimurium LT2. Biochemistry. 46: 9564-9577.

4. Yew WS, Fedorov AA, Fedorov EV, Rakus JF, Pierce RW, Almo SC, and Gerlt JA. (2006) Evolution of enzymatic activities in the enolase superfamily: L-fuconate dehydratase from Xanthomonas campestris. Biochemistry. 45: 14582-14597.

5. Yew WS, Akana J, Wise EL, Rayment I, and Gerlt JA. (2005) Evolution of enzymatic activities in the orotidine 5'-monophosphate decarboxylase suprafamily: enhancing the promiscuous D-arabino-hex-3-ulose 6-phosphate synthase reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry. 44: 1807-1815.

6. Yew WS, Wise EL, Rayment I, and Gerlt JA. (2004) Evolution of enzymatic activities in the orotidine 5’-monophosphate decarboxylase suprafamily: mechanistic evidence for a proton relay system in the active site of 3-keto-L-gulonate 6-phosphate decarboxylase. Biochemistry. 43: 6427-6437.

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