| Title : Promiscuous esterase activities of the C-C hydrolases from Dyella ginsengisoli - Zhou_2012_Biotechnol.Lett_34_1107 |
| Author(s) : Zhou H , Qu Y , Kong C , Wu Y , Zhu K , Yang J , Zhou J |
| Ref : Biotechnol Lett , 34 :1107 , 2012 |
|
Abstract :
A C-C hydrolase gene (bphD(LA-4)) from strain Dyella ginsengisoli LA-4 was cloned and expressed in Escherichia coli BL21 (DE3). BphD(LA-4) together with another hydrolase MfphA(LA-4), which derived from the same strain, possessed esterase activities. p-Nitrophenyl butyrate was the best substrate for both enzymes. BphD(LA-4) had high catalytic efficiency to p-nitrophenyl benzoate, whereas MfphA(LA-4) had no activity. Homology modeling and docking studies demonstrated that the proper hydrogen bond interaction was important for the reactivity of specific substrate. |
| PubMedSearch : Zhou_2012_Biotechnol.Lett_34_1107 |
| PubMedID: 22361962 |
| Substrate | Paranitrophenyl-benzoate |
Zhou H, Qu Y, Kong C, Wu Y, Zhu K, Yang J, Zhou J (2012)
Promiscuous esterase activities of the C-C hydrolases from Dyella ginsengisoli
Biotechnol Lett
34 :1107
Zhou H, Qu Y, Kong C, Wu Y, Zhu K, Yang J, Zhou J (2012)
Biotechnol Lett
34 :1107