Lipase from Rhizopus Oryzae KU45

Enzyme Description

Species
Rhizopus Oryzae KU45 β†—
Extremophile
No
EC Number
3.1.1.3 β†—

Sequence

Length: 269 amino acids
SDGGKVVAATTAQIQEFTKYAGIAATAYCRSVVPGNKWDCVQCQKWVPDGKIITTFTSLLSDTNGYVLRSDKQKTIYLVFRGTNSFRSAITDIVFNFSDYKPVKGAKVHAGFLSSYEQVVNDYFPVIQEQLTANPTYKVIVTGHSLGGAQALLAGMDLYQREPRLSPKNLSIFTVGGPRVGNPTFAYYVESTGIPFQRTVHKRDIVPHVPPQSFGFLHPGVESWIKSGTSNVQICTSEIETKDCSNSIVPFTSLLDHLSYFDINEGSCL
Alper Arslanoğlu et al. (2020) β€” Gene Cloning, Heterologous Expression and Biochemical Characterization of A Novel Extracellular Lipase from Rhizopus Oryzae KU45
Iran Journal of Biotechnology  Β· doi:10.30498/IJB.2020.141895.2343 β†—  Β· Activity - Classical
7 measurements ▼
Database ID
β€”
Sequence Annotation
Explicit - Provided
Protein Source
Recombinant, host bacterium Escherichia coli BL21 (DE3)

Experimental Data (7 measurements)

7 measurements
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, 400 nm) in the presence of organic solvent Ethanol 30% 100.0 80.33 % 100 mM Tris–HCl buffer, 150 mM NaCl, 0.5% Triton X-100, 1% acetonitrile 8 45Β°C 0.5 mM p-Nitrophenyl laurate Lauric Acid , p-Nitrophenol β€” β€” Classical aqueous control (in %) | Close UniProt sequence : D0EHQ8 (123 first residues from UniProt sequence removed from mature protein, 1 mutation A7V from mature sequence)
Activity - Classical Activity measured by absorbance spectrophotometry (p-nitrophenol absorbance measurement, 400 nm) in the presence of organic solvent Methanol 30% 100.0 117.66 % 100 mM Tris–HCl buffer, 150 mM NaCl, 0.5% Triton X-100, 1% acetonitrile 8 45Β°C 0.5 mM p-Nitrophenyl laurate Lauric Acid , p-Nitrophenol β€” β€” Classical aqueous control (in %) | Close UniProt sequence : D0EHQ8 (123 first residues from UniProt sequence removed from mature protein, 1 mutation A7V from mature sequence)
Activity - Classical Activity measured by absorbance spectrophotometry (p-nitrophenol absorbance measurement, 400 nm) in the presence of organic solvent Acetone 30% 100.0 30.33 % 100 mM Tris–HCl buffer, 150 mM NaCl, 0.5% Triton X-100, 1% acetonitrile 8 45Β°C 0.5 mM p-Nitrophenyl laurate Lauric Acid , p-Nitrophenol β€” β€” Classical aqueous control (in %) | Close UniProt sequence : D0EHQ8 (123 first residues from UniProt sequence removed from mature protein, 1 mutation A7V from mature sequence)
Activity - Classical Activity measured by absorbance spectrophotometry (p-nitrophenol absorbance measurement, 400 nm) in the presence of organic solvent 1-Propanol 30% 100.0 37.0 % 100 mM Tris–HCl buffer, 150 mM NaCl, 0.5% Triton X-100, 1% acetonitrile 8 45Β°C 0.5 mM p-Nitrophenyl laurate Lauric Acid , p-Nitrophenol β€” β€” Classical aqueous control (in %) | Close UniProt sequence : D0EHQ8 (123 first residues from UniProt sequence removed from mature protein, 1 mutation A7V from mature sequence)
Activity - Classical Activity measured by absorbance spectrophotometry (p-nitrophenol absorbance measurement, 400 nm) in the presence of organic solvent n-Hexane 30% 100.0 0.0 % 100 mM Tris–HCl buffer, 150 mM NaCl, 0.5% Triton X-100, 1% acetonitrile 8 45Β°C 0.5 mM p-Nitrophenyl laurate Lauric Acid , p-Nitrophenol β€” β€” Classical aqueous control (in %) | Close UniProt sequence : D0EHQ8 (123 first residues from UniProt sequence removed from mature protein, 1 mutation A7V from mature sequence)
Activity - Classical Activity measured by absorbance spectrophotometry (p-nitrophenol absorbance measurement, 400 nm) in the presence of organic solvent Dimethylformamide (DMF) 30% 100.0 39.0 % 100 mM Tris–HCl buffer, 150 mM NaCl, 0.5% Triton X-100, 1% acetonitrile 8 45Β°C 0.5 mM p-Nitrophenyl laurate Lauric Acid , p-Nitrophenol β€” β€” Classical aqueous control (in %) | Close UniProt sequence : D0EHQ8 (123 first residues from UniProt sequence removed from mature protein, 1 mutation A7V from mature sequence)
Activity - Classical Activity measured by absorbance spectrophotometry (p-nitrophenol absorbance measurement, 400 nm) in the presence of organic solvent Dimethyl Sulfoxide (DMSO) 30% 100.0 123.33 % 100 mM Tris–HCl buffer, 150 mM NaCl, 0.5% Triton X-100, 1% acetonitrile 8 45Β°C 0.5 mM p-Nitrophenyl laurate Lauric Acid , p-Nitrophenol β€” β€” Classical aqueous control (in %) | Close UniProt sequence : D0EHQ8 (123 first residues from UniProt sequence removed from mature protein, 1 mutation A7V from mature sequence)

Visualization : Activity β€” Classical

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

Structure

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