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Literature summary extracted from

  • Ruiz, C.; Blanco, A.; Pastor, F.I.; Diaz, P.
    Analysis of Bacillus megaterium lipolytic system and cloning of LipA, a novel subfamily I.4 bacterial lipase (2002), FEMS Microbiol. Lett., 217, 263-267.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.3 SDS 8fold activation at 0.05%, no activation at 0.4% Priestia megaterium

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.3 gene lipA, DNA and amino acid sequence determination and analysis, expression in Escherichia coli 5K, sequence comparisons Priestia megaterium

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.3 Ag+ 48% inhibition at 1 mM Priestia megaterium
3.1.1.3 EDTA 60% inhibition at 20 mM, poor inhibition at 1 mM Priestia megaterium
3.1.1.3 Hg2+ complete inhibition at 1 mM Priestia megaterium
3.1.1.3 phytic acid strong inhibition Priestia megaterium
3.1.1.3 PMSF strong inhibition Priestia megaterium
3.1.1.3 Triton X-100 inhibition at concentrations above 1% Priestia megaterium
3.1.1.3 Urea strong inhibition Priestia megaterium

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.3 extracellular the enzyme is secreted Priestia megaterium
-
-

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Priestia megaterium Q8RJP5 precursor; precursor strain 370, gene lipA
-
3.1.1.3 Priestia megaterium ATCC 9885 Q8RJP5 precursor; precursor strain 370, gene lipA
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.1.3 proteolytic modification the enzyme is expressed as precursor protein Priestia megaterium

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.3 culture condition:rhodamine B-grown cell
-
 Priestia megaterium
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 4-methylumbelliferyl butyrate + H2O
-
 Priestia megaterium 4-methylumbelliferol + butyrate
-
 ?
3.1.1.3 4-methylumbelliferyl butyrate + H2O
-
 Priestia megaterium ATCC 9885 4-methylumbelliferol + butyrate
-
 ?
3.1.1.3 4-nitrophenyl butyrate + H2O high activity Priestia megaterium 4-nitrophenol + butyrate
-
 ?
3.1.1.3 4-nitrophenyl butyrate + H2O high activity Priestia megaterium ATCC 9885 4-nitrophenol + butyrate
-
 ?
3.1.1.3 4-nitrophenyl caprate + H2O
-
 Priestia megaterium 4-nitrophenol + caprate
-
 ?
3.1.1.3 4-nitrophenyl caproate + H2O
-
 Priestia megaterium 4-nitrophenol + caproate
-
 ?
3.1.1.3 4-nitrophenyl caproate + H2O
-
 Priestia megaterium ATCC 9885 4-nitrophenol + caproate
-
 ?
3.1.1.3 4-nitrophenyl caprylate + H2O
-
 Priestia megaterium 4-nitrophenol + caprylate
-
 ?
3.1.1.3 4-nitrophenyl laurate + H2O
-
 Priestia megaterium 4-nitrophenol + laurate
-
 ?
3.1.1.3 4-nitrophenyl valerate + H2O
-
 Priestia megaterium 4-nitrophenol + valerate
-
 ?
3.1.1.3 4-nitrophenyl valerate + H2O
-
 Priestia megaterium ATCC 9885 4-nitrophenol + valerate
-
 ?
3.1.1.3 additional information the recombinant enzyme displays high activity on short to medium chain length substrates, and poor activity on C18 substrates, overview, poor activity with 4-nitrophenyl palmitate, 4-nitrophenyl stearate, and 4-methylumbelliferyl oleate Priestia megaterium ?
-
 ?
3.1.1.3 additional information the recombinant enzyme displays high activity on short to medium chain length substrates, and poor activity on C18 substrates, overview, poor activity with 4-nitrophenyl palmitate, 4-nitrophenyl stearate, and 4-methylumbelliferyl oleate Priestia megaterium ATCC 9885 ?
-
 ?
3.1.1.3 olive oil + H2O
-
 Priestia megaterium ?
-
 ?
3.1.1.3 tributyrin + H2O
-
 Priestia megaterium dibutyrin + butyrate
-
 ?
3.1.1.3 triolein + H2O
-
 Priestia megaterium diolein + oleate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.3 ? x * 22000-22379, precursor protein, SDS-PAGE and sequence calculation, x * 19000-19542, mature protein, SDS-PAGE and sequence calculation Priestia megaterium

Synonyms

EC Number Synonyms Comment Organism
3.1.1.3 LipA
-
 Priestia megaterium
3.1.1.3 More the cloned lipase is a member of a reduced cluster of bacterial serine-esterases grouped in subfamily I.4 of bacterial lipases, exclusive from the mesophilic or moderately thermophilic members of the genus Bacillus Priestia megaterium

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.3 45
-
 recombinant enzyme Priestia megaterium

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.3 4 30 pH 7.0, recombinant enzyme, 40 days, stable Priestia megaterium
3.1.1.3 50
-
 1 h, recombinant enzyme, 9.1% remaining activity Priestia megaterium

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.3 7
-
 recombinant enzyme Priestia megaterium

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.3 6 9 the recombinant enzyme exhibits 87% of maximal activity at pH 6.0 and 66% at pH 9.0 Priestia megaterium

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.1.3 4 12 1 h, room temperature, recombinant enzyme, stable Priestia megaterium

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.1.1.3 Priestia megaterium recombinant mature protein, isoelectric focusing
-
 9.4
3.1.1.3 Priestia megaterium mature protein, sequence calculation
-
 9.42
3.1.1.3 Priestia megaterium precursor protein, sequence calculation
-
 9.56