Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Alquati, C.; De Gioia, L.; Santarossa, G.; Alberghina, L.; Fantucci, P.; Lotti, M.
    The cold-active lipase of Pseudomonas fragi (2002), Eur. J. Biochem., 269, 3321-3328.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.3 DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli at 27°C Pseudomonas fragi

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.3 Ca2+ binding involves residues D217 and D262 Pseudomonas fragi

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Pseudomonas fragi Q9EV86 gene lips
-
3.1.1.3 Pseudomonas fragi IFO 3458 Q9EV86 gene lips
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.3 recombinant His-tagged enzyme from Escherichia coli by metal-chelating affinity chromatography, the His-tag is cleaved off by Tev protease Pseudomonas fragi

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 additional information substrate specificity, the enzyme prefers triacylglycerides with short fatty acid chains Pseudomonas fragi ?
-
 ?
3.1.1.3 additional information substrate specificity, the enzyme prefers triacylglycerides with short fatty acid chains Pseudomonas fragi IFO 3458 ?
-
 ?
3.1.1.3 tributyrin + H2O preferred substrate Pseudomonas fragi dibutyrin + butyrate
-
 ?
3.1.1.3 tributyrin + H2O preferred substrate Pseudomonas fragi IFO 3458 dibutyrin + butyrate
-
 ?
3.1.1.3 tricaprylin + H2O
-
 Pseudomonas fragi dicaprylin + caprylate
-
 ?
3.1.1.3 trilaurin + H2O
-
 Pseudomonas fragi dilaurin + laurate
-
 ?
3.1.1.3 trilaurin + H2O
-
 Pseudomonas fragi IFO 3458 dilaurin + laurate
-
 ?
3.1.1.3 trimyristin + H2O
-
 Pseudomonas fragi dimyristin + myristate
-
 ?
3.1.1.3 triolein + H2O low activity Pseudomonas fragi diolein + oleate
-
 ?
3.1.1.3 triolein + H2O low activity Pseudomonas fragi IFO 3458 diolein + oleate
-
 ?
3.1.1.3 tripalmitin + H2O
-
 Pseudomonas fragi dipalmitin + palmitate
-
 ?
3.1.1.3 tripalmitin + H2O
-
 Pseudomonas fragi IFO 3458 dipalmitin + palmitate
-
 ?
3.1.1.3 tristearin + H2O low activity Pseudomonas fragi distearin + stearate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.3 More three-dimensional structure modelling and analysis, overview Pseudomonas fragi

Synonyms

EC Number Synonyms Comment Organism
3.1.1.3 lipase
-
 Pseudomonas fragi
3.1.1.3 PFL
-
 Pseudomonas fragi

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.3 29
-
-
 Pseudomonas fragi

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.3 10 50 59% of maximal activity at 10°C, 15% at 50°C Pseudomonas fragi

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.3 10
-
 60% remaining activity of the purified recombinant enzyme Pseudomonas fragi
3.1.1.3 27
-
 half-life of the purified recombinant enzyme is about 5 h Pseudomonas fragi
3.1.1.3 50
-
 nearly complete loss of activity within a few min of the purified recombinant enzyme Pseudomonas fragi

pH Optimum

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