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Literature summary extracted from

  • Kim, H.K.; Choi, H.J.; Kim, M.H.; Sohn, C.B.; Oh, T.K.
    Expression and characterization of Ca2+-independent lipase from Bacillus pumilus B26 (2002), Biochim. Biophys. Acta, 1583, 205-212.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.3 DNA sequence determination and analysis, expression in Escherichia coli XL1-Blue and in Bacillus subtilis DB104 Bacillus pumilus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.3 extracellular secretion to the culture medium Bacillus pumilus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.3 Ca2+ enzyme shows Ca2+-independent thermostability and catalytic activity, enzyme contains no Ca2+-binding motif around the catalytic His156 residue Bacillus pumilus

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Bacillus pumilus
-
 Ca2+-independent lipase
-
3.1.1.3 Bacillus pumilus B26
-
 Ca2+-independent lipase
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.3 recombinant enzyme from Bacillus subtilis culture supernatant, 4.3fold, purification of the wild-type Bacillus pumilus strain is not possible due to the low expression level Bacillus pumilus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.3 138
-
 purified enzyme, substrate is olive oil emulsion Bacillus pumilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 4-nitrophenyl butyrate + H2O the enzyme shows a typical interfacial activation mechanism towards the substrate Bacillus pumilus 4-nitrophenol + butyrate
-
 ?
3.1.1.3 4-nitrophenyl butyrate + H2O the enzyme shows a typical interfacial activation mechanism towards the substrate Bacillus pumilus B26 4-nitrophenol + butyrate
-
 ?
3.1.1.3 additional information an emulsion containing olive oil and gum arabic is used as substrate, enzyme shows a preference for short-chain triacylglycerides Bacillus pumilus ?
-
 ?
3.1.1.3 additional information an emulsion containing olive oil and gum arabic is used as substrate, enzyme shows a preference for short-chain triacylglycerides Bacillus pumilus B26 ?
-
 ?
3.1.1.3 tributyrin + H2O
-
 Bacillus pumilus dibutyrin + butyrate
-
 ?
3.1.1.3 tributyrin + H2O
-
 Bacillus pumilus B26 dibutyrin + butyrate
-
 ?
3.1.1.3 triolein + H2O low activity Bacillus pumilus diolein + oleate
-
 ?
3.1.1.3 triolein + H2O low activity Bacillus pumilus B26 diolein + oleate
-
 ?
3.1.1.3 tripropionin + H2O the enzyme shows a typical interfacial activation mechanism towarsd the substrate Bacillus pumilus dipropionin + propionate
-
 ?
3.1.1.3 tripropionin + H2O the enzyme shows a typical interfacial activation mechanism towarsd the substrate Bacillus pumilus B26 dipropionin + propionate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.3 lipase B26
-
 Bacillus pumilus
3.1.1.3 More the enzyme belongs to the lipase family I.4 Bacillus pumilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.3 35
-
-
 Bacillus pumilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.3 40
-
 stable up to, in presence or absence of 10 mM Ca2+ Bacillus pumilus
3.1.1.3 45
-
 rapid decrease in activity Bacillus pumilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.3 8.5
-
-
 Bacillus pumilus