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Literature summary extracted from

  • An, S.Y.; Kim, S.W.; Choi, Y.L.; Cho, Y.S.; Joo, W.H.; Lee, Y.C.
    Cloning, expression in Escherichia coli, and enzymatic properties of a lipase from Pseudomonas sp. SW-3 (2003), J. Microbiol., 41, 95-101.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.3 cloning of lipase gene lipA and its activator gene lipB, immediately downstream of lipA, DNA and amino acid sequences determination and analysis, overexpression of the insoluble protein in Escherichia coli BL21(DE3) with coexpression of lipB resulting in an active enzyme, enzyme expressed without lipB is not active Pseudomonas sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.3 Co2+ 2 mM, pH 8.0 Pseudomonas sp.
3.1.1.3 Fe2+ 2 mM, pH 8.0 Pseudomonas sp.
3.1.1.3 Hg2+ 2 mM, pH 8.0 Pseudomonas sp.
3.1.1.3 Mg2+ 2 mM, pH 8.0 Pseudomonas sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.3 Ca2+
-
Pseudomonas sp.
3.1.1.3 Na+
-
Pseudomonas sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.3 31000
-
x * 31000, recombinant refolded enzyme, SDS-PAGE Pseudomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Pseudomonas sp. Q9F0L9 lipase LipA or PLS, gene lipA
-
3.1.1.3 Pseudomonas sp. SW-3 Q9F0L9 lipase LipA or PLS, gene lipA
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.3 insoluble overexpressed recombinant enzyme from Escherichia coli, coeexpressed with activator LipB Pseudomonas sp.

Renatured (Commentary)

EC Number Renatured (Comment) Organism
3.1.1.3 insoluble recombinant enzyme is solubilized by 8 M urea, purified and refolded by removing urea in presence of Ca2+ Pseudomonas sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.3 36.3
-
purified recombinant refolded enzyme, substrate 4-nitrophenyl palmitate Pseudomonas sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 4-nitrophenyl caprate + H2O
-
Pseudomonas sp. 4-nitrophenol + caprate
-
?
3.1.1.3 4-nitrophenyl caprate + H2O
-
Pseudomonas sp. SW-3 4-nitrophenol + caprate
-
?
3.1.1.3 4-nitrophenyl laurate + H2O
-
Pseudomonas sp. 4-nitrophenol + laurate
-
?
3.1.1.3 4-nitrophenyl laurate + H2O
-
Pseudomonas sp. SW-3 4-nitrophenol + laurate
-
?
3.1.1.3 4-nitrophenyl myristate + H2O
-
Pseudomonas sp. 4-nitrophenol + myristate
-
?
3.1.1.3 4-nitrophenyl myristate + H2O
-
Pseudomonas sp. SW-3 4-nitrophenol + myristate
-
?
3.1.1.3 4-nitrophenyl palmitate + H2O best substrate Pseudomonas sp. 4-nitrophenol + palmitate
-
?
3.1.1.3 4-nitrophenyl palmitate + H2O best substrate Pseudomonas sp. SW-3 4-nitrophenol + palmitate
-
?
3.1.1.3 4-nitrophenyl stearate + H2O
-
Pseudomonas sp. 4-nitrophenol + stearate
-
?
3.1.1.3 additional information enzyme shows a preference for long-chain fatty acid triacylglyceride substrates Pseudomonas sp. ?
-
?
3.1.1.3 additional information enzyme shows a preference for long-chain fatty acid triacylglyceride substrates Pseudomonas sp. SW-3 ?
-
?

Subunits

EC Number Subunits Comment Organism
3.1.1.3 ? x * 31000, recombinant refolded enzyme, SDS-PAGE Pseudomonas sp.

Synonyms

EC Number Synonyms Comment Organism
3.1.1.3 lipase
-
Pseudomonas sp.
3.1.1.3 More the enzyme belongs to the lipase family I.1 Pseudomonas sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.3 50
-
-
Pseudomonas sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.3 50
-
stable, 90% remaining activity, 30 min Pseudomonas sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.3 8
-
-
Pseudomonas sp.