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Literature summary for 3.1.1.1 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

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

Protein Variants

Protein Variants Comment Organism
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

Inhibitors Comment Organism Structure
glycerol inhibition of mutant enzyme R11G/L36P/V225A/I551L/A564T no matter that it is or is not treated by acetone Aeropyrum pernix
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

Organism UniProt Comment Textmining
Aeropyrum pernix Q9YBQ2
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-
Aeropyrum pernix DSM 11879 Q9YBQ2
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-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
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
-
?
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
-
?
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

Synonyms Comment Organism
APE1547
-
Aeropyrum pernix

Temperature Optimum [°C]

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

pH Optimum

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