| Title : Residue Val237 is critical for the enantioselectivity of Penicillium expansum lipase - Tang_2014_Biotechnol.Lett_36_633 |
| Author(s) : Tang L , Su M , Chi L , Zhang J , Zhang H , Zhu L |
| Ref : Biotechnol Lett , 36 :633 , 2014 |
| Abstract : The shape of the hydrophobic tunnel leading to the active site of Penicillium expansum lipase (PEL) was redesigned by single-point mutations, in order to better understand enzyme enantioselectivity towards naproxen. A variant with a valine-to-glycine substitution at residue 237 exhibited almost no enantioselectivity (E = 1.1) compared with that (E = 104) of wild-type PEL. The function of the residue, Val237, in the hydrophobic tunnel was further analyzed by site-directed mutagenesis. For each of these variants a significant decrease of enantioselectivity (E < 7) was observed compared with that of wild-type enzyme. Further docking result showed that Val237 plays the most important role in stabilizing the correct orientation of (R)-naproxen. Overall, these results indicate that the residue Val237 is the key amino acid residue maintaining the enantioselectivity of the lipase. |
| ESTHER : Tang_2014_Biotechnol.Lett_36_633 |
| PubMedSearch : Tang_2014_Biotechnol.Lett_36_633 |
| PubMedID: 24338160 |
| Gene_locus related to this paper: penex-Q9HFW6 |
| Gene_locus related to this paper: penex-Q9HFW6 |
Tang L, Su M, Chi L, Zhang J, Zhang H, Zhu L (2014)
Residue Val237 is critical for the enantioselectivity of Penicillium expansum lipase
Biotechnol Lett
36 :633
Tang L, Su M, Chi L, Zhang J, Zhang H, Zhu L (2014)
Biotechnol Lett
36 :633