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

BRENDA support

Literature summary extracted from

  • Lan, D.M.; Yang, N.; Wang, W.K.; Shen, Y.F.; Yang, B.; Wang, Y.H.
    A novel cold-active lipase from Candida albicans: cloning, expression and characterization of the recombinant enzyme (2011), Int. J. Mol. Sci., 12, 3950-3965.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.3 mutant enzymes S154L and S154L/S293L are expressed in Pichia pastoris, no obvious expression is observed from wild type and the S293L mutant enzymes Candida albicans

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.3 S154L the mutation results in loss of enzyme expression Candida albicans
3.1.1.3 S154L/S293L the mutant exhibits a preference for the short- and medium-chain length 4-nitrophenyl (C4 and C8 acyl group) esters rather than the long chain length 4-nitrophenyl esters (C12, C16 and C18 acyl group), the pure Lip5 double mutant is stable at pH 5.0-9.0 and at temperatures ranging from 15-35°C Candida albicans
3.1.1.3 S293L the mutation causes a marked reduction in the lipase activity Candida albicans

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.3 Ba2+ 77.22% residual activity at 5 mM Candida albicans
3.1.1.3 Ca2+ 72.04% residual activity at 5 mM Candida albicans
3.1.1.3 Cu2+ 78.35% residual activity at 5 mM Candida albicans
3.1.1.3 EDTA 65.41% residual activity at 5 mM Candida albicans
3.1.1.3 Fe2+ strong inhibition with residual activity of 20.27% at 5 mM Candida albicans
3.1.1.3 Fe3+ strong inhibition with residual activity of 35.11% at 5 mM Candida albicans
3.1.1.3 Hg2+ strong inhibition with residual activity of 13.19% at 5 mM Candida albicans
3.1.1.3 Li+ 92.24% residual activity at 5 mM Candida albicans
3.1.1.3 Mg2+ 94.49% residual activity at 1 mM Candida albicans
3.1.1.3 Mn2+ 90.66% residual activity at 5 mM Candida albicans
3.1.1.3 Ni2+ 92.24% residual activity at 5 mM Candida albicans
3.1.1.3 phenylmethylsulfonyl fluoride 38.54% residual activity 5 mM Candida albicans
3.1.1.3 SDS SDS sharply decreases the lipase activity by 85% at 0.1% (w/v) Candida albicans
3.1.1.3 Triton X-100 48.55% residual activity at 0.1% (v/v) Candida albicans
3.1.1.3 Tween 20 82.52% residual activity at 0.1% (v/v) Candida albicans
3.1.1.3 Tween 80 57.24% residual activity at 0.1% (v/v) Candida albicans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.3 0.27
-
 4-nitrophenyl caprylate mutant enzyme S154L/S293L, at pH 6.0 and 25°C Candida albicans
3.1.1.3 0.36
-
 4-nitrophenyl palmitate mutant enzyme S154L/S293L, at pH 6.0 and 25°C Candida albicans
3.1.1.3 0.41
-
 4-nitrophenyl butyrate mutant enzyme S154L/S293L, at pH 6.0 and 25°C Candida albicans
3.1.1.3 0.5
-
 4-nitrophenyl laurate mutant enzyme S154L/S293L, at pH 6.0 and 25°C Candida albicans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.3 Zn2+ Zn2+ increases the recombinant lipase activity at 1 mM to 119.22% or at 5 mM to 115.19% Candida albicans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.3 50000
-
 x * 50000, S154L and S154L/S293L mutant enzymes Candida albicans

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
3.1.1.3 Acetone the residual activities of Lip5 double mutant remains at 44.76% after incubation for 1 h in 30% (v/v) acetone Candida albicans
3.1.1.3 Ethanol the residual activities of Lip5 double mutant remains at 24.32% after incubation for 1 h in 30% (v/v) ethanol Candida albicans
3.1.1.3 isopropanol lipase activity is almost lost (4.59% residual activity) in the presence of 30% (v/v) isopropanol Candida albicans
3.1.1.3 Methanol the residual activities of Lip5 double mutant remains at 48.23% after incubation for 1 h in 30% (v/v) methanol Candida albicans

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Candida albicans
-
-
-
3.1.1.3 Candida albicans ATCC 10231
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.3 ammonium sulfate precipitation and Q Sepharose column chromatography Candida albicans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 4-nitrophenyl butyrate + H2O
-
 Candida albicans 4-nitrophenol + butyrate
-
 ?
3.1.1.3 4-nitrophenyl butyrate + H2O
-
 Candida albicans ATCC 10231 4-nitrophenol + butyrate
-
 ?
3.1.1.3 4-nitrophenyl caprylate + H2O highest activity of mutant enzyme S154L/S293L Candida albicans 4-nitrophenol + caprylate
-
 ?
3.1.1.3 4-nitrophenyl caprylate + H2O highest activity of mutant enzyme S154L/S293L Candida albicans ATCC 10231 4-nitrophenol + caprylate
-
 ?
3.1.1.3 4-nitrophenyl laurate + H2O lowest activity of mutant enzyme S154L/S293L Candida albicans 4-nitrophenol + laurate
-
 ?
3.1.1.3 4-nitrophenyl laurate + H2O lowest activity of mutant enzyme S154L/S293L Candida albicans ATCC 10231 4-nitrophenol + laurate
-
 ?
3.1.1.3 4-nitrophenyl palmitate + H2O
-
 Candida albicans 4-nitrophenol + palmitate
-
 ?
3.1.1.3 4-nitrophenyl palmitate + H2O
-
 Candida albicans ATCC 10231 4-nitrophenol + palmitate
-
 ?
3.1.1.3 additional information the enzyme also uses olive oil and safflower oil as substrates Candida albicans ?
-
 ?
3.1.1.3 additional information the enzyme also uses olive oil and safflower oil as substrates Candida albicans ATCC 10231 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.3 ? x * 50000, S154L and S154L/S293L mutant enzymes Candida albicans

Synonyms

EC Number Synonyms Comment Organism
3.1.1.3 Lip5
-
 Candida albicans
3.1.1.3 lipase
-
 Candida albicans

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.3 15 25 the recombinant lipase displays the highest activity at 15 and 25°C Candida albicans

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.3 5 25 the recombinant lipase maintains more than 70% of the maximum activity at 35°C. Even at a lower temperature of 5°C, the recombinant lipase still retains more than 50% of the maximal activity Candida albicans

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.3 15 45 the Lip5 double mutant shows good thermostability over a range of temperature from 15°C to 45°C, with more than 60% of maximal activity retained after 2 h incubation. However, the stability of recombinant lipase decreases at 55°C, with 23.86% residual activity after incubation for 2 h Candida albicans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.1.3 9.41
-
 4-nitrophenyl laurate mutant enzyme S154L/S293L, at pH 6.0 and 25°C Candida albicans
3.1.1.3 31.59
-
 4-nitrophenyl palmitate mutant enzyme S154L/S293L, at pH 6.0 and 25°C Candida albicans
3.1.1.3 54.18
-
 4-nitrophenyl butyrate mutant enzyme S154L/S293L, at pH 6.0 and 25°C Candida albicans
3.1.1.3 55.12
-
 4-nitrophenyl caprylate mutant enzyme S154L/S293L, at pH 6.0 and 25°C Candida albicans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.3 5 6 the recombinant lipase displays the highest activity at pH 5.0 and 6.0 Candida albicans

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.1.3 4 9 the Lip5-double mutant activity exhibits stable within the pH range of 5.0-9.0, and it remains more than 60% of maximal activity. The recombinant lipase sharply loses its activity when incubated at pH 4.0, and only preserves 26% activity after 12 h of incubation Candida albicans

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1.1.3 18.58
-
 4-nitrophenyl laurate mutant enzyme S154L/S293L, at pH 6.0 and 25°C Candida albicans
3.1.1.3 86.86
-
 4-nitrophenyl palmitate mutant enzyme S154L/S293L, at pH 6.0 and 25°C Candida albicans
3.1.1.3 131
-
 4-nitrophenyl butyrate mutant enzyme S154L/S293L, at pH 6.0 and 25°C Candida albicans
3.1.1.3 203.4
-
 4-nitrophenyl caprylate mutant enzyme S154L/S293L, at pH 6.0 and 25°C Candida albicans