5FRD
Name : Structure of a thermophilic esterase
Revelation date : 25-May-2016
Family : 6_AlphaBeta_hydrolase
Gene_locus : arcfu-est2
PDB file : ESTHER: header of PDB entry RCSB: Full entry
Comment
Sayer, C., Finnigan, W., Isupov, M.N., Levisson, M., Kengen, S.W.M., van der Oost, J., Harmer, N., Littlechild, J.A.:
A thermophilic esterase with high activity towards short- to medium-chain
p-nitrophenyl carboxylic esters with optimal activity towards the valerate ester.
The AF-Est2 has good solvent and pH stability and is very thermostable,
showing no loss of activity after incubation for 30min at 80 C.
The structure reveals a bound CoA molecule in the vicinity of the active site
Ligand :
References (1)
| Title : Structural and biochemical characterisation of Archaeoglobus fulgidus esterase reveals a bound CoA molecule in the vicinity of the active site - Sayer_2016_Sci.Rep_6_25542 |
| Author(s) : Sayer C , Finnigan W , Isupov MN , Levisson M , Kengen SW , Van der Oost J , Harmer NJ , Littlechild JA |
| Ref : Sci Rep , 6 :25542 , 2016 |
| Abstract : Sayer_2016_Sci.Rep_6_25542 |
| ESTHER : Sayer_2016_Sci.Rep_6_25542 |
| PubMedSearch : Sayer_2016_Sci.Rep_6_25542 |
| PubMedID: 27160974 |
| Gene_locus related to this paper: arcfu-est2 |
Representative scheme of Prolylcarboxypeptidase structure and an image from PDBsum server
