Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Cong, F.; Xing, K.; Gao, R.; Cao, S.; Zhang, G.
    Enhanced activity and enantioselectivity of a hyperthermophilic esterase from archaeon Aeropyrum pernix K1 by acetone treatment (2011), Appl. Biochem. Biotechnol., 165, 795-801.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.1 glycerol some increase for the activity of the wild-type enzyme treated with acetone Aeropyrum pernix

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.1 R11G/L36P/V225A/I551L/A564T in the resolution of 2-octanol acetate, the acetone-treated mutant A has a 9fold enantioselective increase relative to that purified by Ni-chelating column Aeropyrum pernix

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.1 glycerol inhibition of mutant enzyme R11G/L36P/V225A/I551L/A564T no matter that it is or is not treated by acetone Aeropyrum pernix
3.1.1.1 Tween-80 inhibition of wild-type and mutant enzyme R11G/L36P/V225A/I551L/A564T no matter that they are or are not treated by acetone Aeropyrum pernix

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.1 Aeropyrum pernix Q9YBQ2
-
-
3.1.1.1 Aeropyrum pernix DSM 11879 Q9YBQ2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.1 acetone is utilized to purify wild-type and mutant enzymes to improve their activity and enantioselectivity Aeropyrum pernix

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.1 2-octanyl acetate + H2O the mutant enzyme R11G/L36P/V225A/I551L/A564T treated twice with acetone has a 9fold increase for enantioselectivity in resolution of 2-octanyl acetate relative to that purified by Ni-chelating column, but the wild-type enzyme is less sensitive to acetone in terms of enantioselectivity Aeropyrum pernix 2-octanol + acetate
-
 ?
3.1.1.1 2-octanyl acetate + H2O the mutant enzyme R11G/L36P/V225A/I551L/A564T treated twice with acetone has a 9fold increase for enantioselectivity in resolution of 2-octanyl acetate relative to that purified by Ni-chelating column, but the wild-type enzyme is less sensitive to acetone in terms of enantioselectivity Aeropyrum pernix DSM 11879 2-octanol + acetate
-
 ?
3.1.1.1 4-nitrophenyl octanoate + H2O acetone is utilized to purify wild-type and mutant enzymes to improve their activity and enantioselectivity Aeropyrum pernix 4-nitrophenol + octanoate
-
 ?
3.1.1.1 4-nitrophenyl octanoate + H2O acetone is utilized to purify wild-type and mutant enzymes to improve their activity and enantioselectivity Aeropyrum pernix DSM 11879 4-nitrophenol + octanoate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.1 APE1547
-
 Aeropyrum pernix

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.1 98
-
-
 Aeropyrum pernix

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.1 additional information
-
 acetone treatment shifts the optimum pH of wild-type and mutant enzymes Aeropyrum pernix
3.1.1.1 8
-
 assay at Aeropyrum pernix
3.1.1.1 8
-
 wild-type enzyme purified by Ni-chelating column Aeropyrum pernix
3.1.1.1 8.3
-
 mutant enzyme R11G/L36P/V225A/I551L/A564T purified by Ni-chelating column Aeropyrum pernix
3.1.1.1 9
-
 wild-type enzyme purified by acetone treatment, mutant enzyme R11G/L36P/V225A/I551L/A564T purified by acetone treatment Aeropyrum pernix