Esterase (gene EstSL3) from Alkalibacterium sp. SL3

Enzyme Description

Extremophile
Yes "halophilic", "alkalophilic" organism,"cold-adapted" enzyme
EC Number

Sequence

Length: 211 amino acids
MKINKNDTLLFIGDSITDVGRDRMDGEDLGKGFPLMVASHLQSRYPAKRLTVLNRGIGGDSLKDLKRRWEDDCLITNPDIVTLLIGVNDTWRNQNDGVELTDEELDEFESDYRFLLKSLHQRTDARVILMESFVLPYPKRRVGWRNDLDKRIQIVRKMARDYQTELIPLDGLLNAAGIRDGFSYYTGDDGVHPTVAGHGLIANSWLKAVDE
Guozeng Wang et al. (2016) β€” A novel cold-adapted and highly salt-tolerant esterase from Alkalibacterium sp. SL3 from the sediment of a soda lake
Scientific Reports  Β· doi:10.1038/srep19494 β†—  Β· Activity - Classical
22 measurements
Database ID
Sequence Annotation
Explicit - Provided
Protein Source
Recombinant, host bacterium Escherichia coli BL21 (DE3)

Experimental Data (22 measurements)

22 measurements β€” page 2 of 2
Property Assay Solvent Solvent Volume Aqueous Reference Measured Value Units Solution pH Temperature Substrate(s) Product(s) Cofactor(s) Shaking Comments
Activity - Classical Activity measured by absorbance spectrophotometry (p-nitrophenol absorbance measurement, 405 nm) in the presence of organic solvent Ethanol 10% 100.0 93.9 % 50 mM Tris–HCl buffer, 10% acetonitrile 9 30Β°C 1 mM p-Nitrophenol acetate Acetic Acid , p-Nitrophenol β€” β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (p-nitrophenol absorbance measurement, 405 nm) in the presence of organic solvent Methanol 20% 100.0 72.7 % 50 mM Tris–HCl buffer, 10% acetonitrile 9 30Β°C 1 mM p-Nitrophenol acetate Acetic Acid , p-Nitrophenol β€” β€” Classical aqueous control (in %)
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Visualization : Activity β€” Classical

One bar per measurement. Colour = solvent, shade = solvent volume.

Structure

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