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Literature summary extracted from

  • Maruyama, T.; Nakajima, M.; Kondo, H.; Kawasaki, K.; Seki, M.; Goto, M.
    Can lipases hydrolyze a peptide bond? (2003), Enzyme Microb. Technol., 32, 655-657.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.3 gene lipA, expression in Bacillus megaterium WH320 Bacillus subtilis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.3 extracellular secretion to the medium, native and recombinant enzyme Bacillus subtilis
-
-

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Alcaligenes ssp.
-
 commercial product
-
3.1.1.3 Bacillus subtilis
-
 gene lipA
-
3.1.1.3 Bacillus subtilis 168 BsL
-
 gene lipA
-
3.1.1.3 Chromobacterium viscosum
-
 commercial product
-
3.1.1.3 Diutina rugosa
-
 type VII, commercial product
-
3.1.1.3 Fusarium solani
-
 cutinase, commercial product, 90% pure enzyme
-
3.1.1.3 Homo sapiens
-
-
-
3.1.1.3 Rhizomucor miehei
-
 commercial product
-
3.1.1.3 Rhizopus arrhizus
-
 commercial product
-
3.1.1.3 Rhizopus japonicus
-
 commercial product
-
3.1.1.3 Sus scrofa
-
 3 commercially available enzymes, PPL
-
3.1.1.3 Thermomyces lanuginosus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.3 partial purification of the commercial product from elastin Sus scrofa
3.1.1.3 recombinant extracellular enzyme, expressed in Bacillus megaterium, from culture supernatant, to more than 90% purity Bacillus subtilis

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate the catalytic triad consists of Ser, His, and Asp residues, as for serine proteases Homo sapiens
a
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate the catalytic triad consists of Ser, His, and Asp residues, as for serine proteases Sus scrofa
a
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate the catalytic triad consists of Ser, His, and Asp residues, as for serine proteases Rhizopus arrhizus
a
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate the catalytic triad consists of Ser, His, and Asp residues, as for serine proteases Diutina rugosa
a
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate the catalytic triad consists of Ser, His, and Asp residues, as for serine proteases Thermomyces lanuginosus
a
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate the catalytic triad consists of Ser, His, and Asp residues, as for serine proteases Rhizopus japonicus
a
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate the catalytic triad consists of Ser, His, and Asp residues, as for serine proteases Chromobacterium viscosum
a
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate the catalytic triad consists of Ser, His, and Asp residues, as for serine proteases Alcaligenes ssp.
a
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate the catalytic triad consists of Ser, His, and Asp residues, as for serine proteases, enzyme contains the alpha-helical lid structure Rhizomucor miehei
a
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate the catalytic triad consists of Ser, His, and Asp residues, as for serine proteases, lipase contains no lid structure Fusarium solani
a
3.1.1.3 triacylglycerol + H2O = diacylglycerol + a carboxylate the catalytic triad consists of Ser, His, and Asp residues, as for serine proteases, the enzyme contains no lid structure Bacillus subtilis
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.3 cartilage elastin, commercial product Sus scrofa
-
3.1.1.3 pancreas
-
 Homo sapiens
-
3.1.1.3 pancreas 2 commercially available enzymes Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 4-nitrophenol butyrate + H2O
-
 Bacillus subtilis 4-nitrophenol + butyrate
-
 ?
3.1.1.3 4-nitrophenol butyrate + H2O
-
 Bacillus subtilis 168 BsL 4-nitrophenol + butyrate
-
 ?
3.1.1.3 additional information enzyme also utilizes water-soluble substrates, enzyme does not possess protease activity and does not hydrolyze peptide bonds, no activity with N-benzoyl-L-tyrosine 4-nitroanilide Fusarium solani ?
-
 ?
3.1.1.3 additional information enzyme does not possess protease activity and does not hydrolyze peptide bonds, no activity with N-benzoyl-L-tyrosine 4-nitroanilide Bacillus subtilis ?
-
 ?
3.1.1.3 additional information enzyme does not possess protease activity and does not hydrolyze peptide bonds, no activity with N-benzoyl-L-tyrosine 4-nitroanilide Homo sapiens ?
-
 ?
3.1.1.3 additional information enzyme does not possess protease activity and does not hydrolyze peptide bonds, no activity with N-benzoyl-L-tyrosine 4-nitroanilide Sus scrofa ?
-
 ?
3.1.1.3 additional information enzyme does not possess protease activity and does not hydrolyze peptide bonds, no activity with N-benzoyl-L-tyrosine 4-nitroanilide Rhizopus arrhizus ?
-
 ?
3.1.1.3 additional information enzyme does not possess protease activity and does not hydrolyze peptide bonds, no activity with N-benzoyl-L-tyrosine 4-nitroanilide Diutina rugosa ?
-
 ?
3.1.1.3 additional information enzyme does not possess protease activity and does not hydrolyze peptide bonds, no activity with N-benzoyl-L-tyrosine 4-nitroanilide Rhizomucor miehei ?
-
 ?
3.1.1.3 additional information enzyme does not possess protease activity and does not hydrolyze peptide bonds, no activity with N-benzoyl-L-tyrosine 4-nitroanilide Thermomyces lanuginosus ?
-
 ?
3.1.1.3 additional information enzyme does not possess protease activity and does not hydrolyze peptide bonds, no activity with N-benzoyl-L-tyrosine 4-nitroanilide Rhizopus japonicus ?
-
 ?
3.1.1.3 additional information enzyme does not possess protease activity and does not hydrolyze peptide bonds, no activity with N-benzoyl-L-tyrosine 4-nitroanilide Chromobacterium viscosum ?
-
 ?
3.1.1.3 additional information enzyme does not possess protease activity and does not hydrolyze peptide bonds, no activity with N-benzoyl-L-tyrosine 4-nitroanilide Alcaligenes ssp. ?
-
 ?
3.1.1.3 additional information enzyme does not possess protease activity and does not hydrolyze peptide bonds, no activity with N-benzoyl-L-tyrosine 4-nitroanilide Bacillus subtilis 168 BsL ?
-
 ?
3.1.1.3 tributyrin + H2O
-
 Bacillus subtilis dibutyrin + butyrate
-
 ?
3.1.1.3 tributyrin + H2O
-
 Homo sapiens dibutyrin + butyrate
-
 ?
3.1.1.3 tributyrin + H2O
-
 Sus scrofa dibutyrin + butyrate
-
 ?
3.1.1.3 tributyrin + H2O
-
 Rhizopus arrhizus dibutyrin + butyrate
-
 ?
3.1.1.3 tributyrin + H2O
-
 Fusarium solani dibutyrin + butyrate
-
 ?
3.1.1.3 tributyrin + H2O
-
 Diutina rugosa dibutyrin + butyrate
-
 ?
3.1.1.3 tributyrin + H2O
-
 Rhizomucor miehei dibutyrin + butyrate
-
 ?
3.1.1.3 tributyrin + H2O
-
 Thermomyces lanuginosus dibutyrin + butyrate
-
 ?
3.1.1.3 tributyrin + H2O
-
 Rhizopus japonicus dibutyrin + butyrate
-
 ?
3.1.1.3 tributyrin + H2O
-
 Chromobacterium viscosum dibutyrin + butyrate
-
 ?
3.1.1.3 tributyrin + H2O
-
 Alcaligenes ssp. dibutyrin + butyrate
-
 ?
3.1.1.3 tributyrin + H2O
-
 Bacillus subtilis 168 BsL dibutyrin + butyrate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.3 cutinase
-
 Fusarium solani
3.1.1.3 lipase
-
 Bacillus subtilis
3.1.1.3 lipase
-
 Homo sapiens
3.1.1.3 lipase
-
 Sus scrofa
3.1.1.3 lipase
-
 Rhizopus arrhizus
3.1.1.3 lipase
-
 Diutina rugosa
3.1.1.3 lipase
-
 Rhizomucor miehei
3.1.1.3 lipase
-
 Thermomyces lanuginosus
3.1.1.3 lipase
-
 Rhizopus japonicus
3.1.1.3 lipase
-
 Chromobacterium viscosum
3.1.1.3 lipase
-
 Alcaligenes ssp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.3 25
-
 assay at Bacillus subtilis
3.1.1.3 25
-
 assay at Homo sapiens
3.1.1.3 25
-
 assay at Sus scrofa
3.1.1.3 25
-
 assay at Rhizopus arrhizus
3.1.1.3 25
-
 assay at Fusarium solani
3.1.1.3 25
-
 assay at Diutina rugosa
3.1.1.3 25
-
 assay at Rhizomucor miehei
3.1.1.3 25
-
 assay at Thermomyces lanuginosus
3.1.1.3 25
-
 assay at Rhizopus japonicus
3.1.1.3 25
-
 assay at Chromobacterium viscosum
3.1.1.3 25
-
 assay at Alcaligenes ssp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.3 7
-
 assay at Bacillus subtilis
3.1.1.3 7
-
 assay at Homo sapiens
3.1.1.3 7
-
 assay at Sus scrofa
3.1.1.3 7
-
 assay at Rhizopus arrhizus
3.1.1.3 7
-
 assay at Fusarium solani
3.1.1.3 7
-
 assay at Diutina rugosa
3.1.1.3 7
-
 assay at Rhizomucor miehei
3.1.1.3 7
-
 assay at Thermomyces lanuginosus
3.1.1.3 7
-
 assay at Rhizopus japonicus
3.1.1.3 7
-
 assay at Chromobacterium viscosum
3.1.1.3 7
-
 assay at Alcaligenes ssp.