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Literature summary extracted from

  • Poulsen, K.R.; Snabe, T.; Petersen, E.I.; Fojan, P.; Neves-Petersen, M.T.; Wimmer, R.; Petersen, S.B.
    Quantization of pH: evidence for acidic activity of triglyceride lipases (2005), Biochemistry, 44, 11574-11580.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.3 expression of cutinase in Escherichia coli strain BL21(DE3) periplasmic space Fusarium solani

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Burkholderia cepacia P22088
-
-
3.1.1.3 Fusarium solani
-
-
-
3.1.1.3 Rhizomucor miehei
-
-
-
3.1.1.3 Thermomyces lanuginosus O59952
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.3 recombinant cutinase partially from Escherichia coli strain BL21(DE3) periplasmic space by cation exchange chromatography Fusarium solani

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate activity required deprotonation of the catalytic His residue Rhizomucor miehei
a
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate activity required deprotonation of the catalytic His residue Burkholderia cepacia
a
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate activity required deprotonation of the catalytic His residue Thermomyces lanuginosus
a
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate activity required deprotonation of the catalytic His188 residue, model of electrostatics in the active site, the active site is essentially covered with lipod surface during catalysis Fusarium solani
a

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 3.2
-
 pH 4.0, partially purified recombinant enzyme Fusarium solani
3.1.1.3 12.4
-
 pH 6.0, partially purified recombinant enzyme Fusarium solani

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 triolein + H2O
-
 Fusarium solani diolein + oleate
-
 ?
3.1.1.3 triolein + H2O
-
 Rhizomucor miehei diolein + oleate
-
 ?
3.1.1.3 triolein + H2O
-
 Burkholderia cepacia diolein + oleate
-
 ?
3.1.1.3 triolein + H2O
-
 Thermomyces lanuginosus diolein + oleate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.3 lipase
-
 Fusarium solani
3.1.1.3 lipase
-
 Rhizomucor miehei
3.1.1.3 lipase
-
 Burkholderia cepacia
3.1.1.3 lipase
-
 Thermomyces lanuginosus
3.1.1.3 pisi cutinase
-
 Fusarium solani
3.1.1.3 triglyceride lipase
-
 Fusarium solani
3.1.1.3 triglyceride lipase
-
 Rhizomucor miehei
3.1.1.3 triglyceride lipase
-
 Burkholderia cepacia
3.1.1.3 triglyceride lipase
-
 Thermomyces lanuginosus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.3 25
-
 assay at Fusarium solani

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.3 6
-
 broad optimum, influence of pH on catalytic mechanism, overview Thermomyces lanuginosus
3.1.1.3 8
-
 influence of pH on catalytic mechanism, overview Rhizomucor miehei
3.1.1.3 8
-
 influence of pH on catalytic mechanism, overview Burkholderia cepacia
3.1.1.3 8.5
-
 influence of pH on catalytic mechanism, pH-activity profile, overview Fusarium solani

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.3 4 10.5 pH profile, the enzyme is active under acidic conditions Fusarium solani
3.1.1.3 4 10.5 pH profile, the enzyme is active under acidic conditions and shows 22.4% of maximal activity at pH 4.0 Rhizomucor miehei
3.1.1.3 4 10.5 pH profile, the enzyme is active under acidic conditions and shows 25.3% of maximal activity at pH 4.0 Burkholderia cepacia
3.1.1.3 4 10.5 pH profile, the enzyme is active under acidic conditions and shows 70.6% of maximal activity at pH 4.0 Thermomyces lanuginosus