Archaeoglobus fulgidus thermophilic esterase AF1537
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 which regulates substrate specificity
MLERVFIDVD GVKVSLLKGR ERKVFYIHSS GSDATQWVNQ LTAIGGYAID LPNHGQSDTV EVNSVDEYAY YASESLKKTV GKAVVVGHSL GGAVAQKLYL RNPEICLALV LVGTGARLRV LPEILEGLKK EPEKAVDLML SMAFASKGEE YEKKRREFLD RVDVLHLDLS LCDRFDLLED YRNGKLKIGV PTLVIVGEED KLTPLKYHEF FHKHIPNSEL VVIPGASHMV MLEKHVEFNE ALEKFLKKVG V
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 |