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

BRENDA support

Literature summary extracted from

  • Wang, Y.; Zhao, J.; Xu, J.H.; Fan, L.Q.; Li, S.X.; Zhao, L.L.; Mao, X.B.
    Significantly improved expression and biochemical properties of recombinant Serratia marcescens lipase as robust biocatalyst for kinetic resolution of chiral ester (2010), Appl. Biochem. Biotechnol., 162, 2387-2399.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.3 additional information the enzyme is not influenced by PEG1500 and PEG20000 Serratia marcescens
3.1.1.3 PEG4000 116% activity at 0.1% (w/v) Serratia marcescens

Application

EC Number Application Comment Organism
3.1.1.3 synthesis the highly enantioselective lipase from Serratia marcescens ECU1010 is a robust biocatalyst for practical use in large-scale production of diltiazem intermediate Serratia marcescens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.3 expressed as an N-terminus His-tag fusion protein in Escherichia coli BL21(DE3) cells Serratia marcescens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.3 EDTA 25.3% residual activity at 2 mM Serratia marcescens
3.1.1.3 SDS 20.1% residual activity at 0.1% (w/v) Serratia marcescens
3.1.1.3 Triton X-100 2.3% residual activity at 0.1% (w/v) Serratia marcescens
3.1.1.3 Tween 20 80.1% residual activity at 0.1% (w/v) Serratia marcescens
3.1.1.3 Zn2+ 80% residual activity at 2 mM Serratia marcescens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.3 222
-
 (+/-)-trans-3-(4'-methoxy-phenyl)-glycidyl methyl ester at pH 7.5 and 30°C Serratia marcescens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.3 Ba2+ 130% activity at 2 mM Serratia marcescens
3.1.1.3 Ca2+ adding Ca2+ to a final concentration of 5 mM increases the activity of lipase by nearly 5fold with respect to the control Serratia marcescens
3.1.1.3 Cu2+ 172.5% activity at 2 mM Serratia marcescens
3.1.1.3 Li+ 140% activity at 2 mM Serratia marcescens
3.1.1.3 additional information the enzyme is not influenced by Fe2+, Mn2+, and Mg2+ Serratia marcescens
3.1.1.3 Ni2+ 172.5% activity at 2 mM Serratia marcescens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.3 65000
-
 x * 65000, SDS-PAGE Serratia marcescens

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Serratia marcescens
-
-
-
3.1.1.3 Serratia marcescens ECU1010
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.3 Ni-NTA agarose column chromatography Serratia marcescens

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 2.4
-
 enzyme from supernatant of cell lysate, using 4-nitrophenyl acetate as substrate, at pH 7.5 and 30°C Serratia marcescens
3.1.1.3 5.7
-
 enzyme after 2.4fold purification, using 4-nitrophenyl acetate as substrate, at pH 7.5 and 30°C Serratia marcescens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 (+/-)-trans-3-(4'-methoxy-phenyl)-glycidyl methyl ester + H2O 50% conversion yield after 4 h in 100 mM potassium phosphate buffer, pH 7.5, at 30 °C Serratia marcescens (2R,3S)-3-(4-hydroxyphenyl)oxirane-2-carboxylic acid + methyl (2S,3R)-3-(4-hydroxyphenyl)oxirane-2-carboxylate + methanol
-
 ?
3.1.1.3 4-nitrophenyl acetate + H2O worst substrate, less than 5% activity compared to 4-nitrophenyl laurate Serratia marcescens 4-nitrophenol + acetate
-
 ?
3.1.1.3 4-nitrophenyl acetate + H2O worst substrate, less than 5% activity compared to 4-nitrophenyl laurate Serratia marcescens ECU1010 4-nitrophenol + acetate
-
 ?
3.1.1.3 4-nitrophenyl butyrate + H2O about 10% activity compared to 4-nitrophenyl laurate Serratia marcescens 4-nitrophenol + butyrate
-
 ?
3.1.1.3 4-nitrophenyl butyrate + H2O about 10% activity compared to 4-nitrophenyl laurate Serratia marcescens ECU1010 4-nitrophenol + butyrate
-
 ?
3.1.1.3 4-nitrophenyl decanoate + H2O about 30% activity compared to 4-nitrophenyl laurate Serratia marcescens 4-nitrophenol + decanoate
-
 ?
3.1.1.3 4-nitrophenyl decanoate + H2O about 30% activity compared to 4-nitrophenyl laurate Serratia marcescens ECU1010 4-nitrophenol + decanoate
-
 ?
3.1.1.3 4-nitrophenyl laurate + H2O maximum activity on 4-nitrophenyl laurate Serratia marcescens 4-nitrophenol + laurate
-
 ?
3.1.1.3 4-nitrophenyl myristate + H2O about 90% activity compared to 4-nitrophenyl laurate Serratia marcescens 4-nitrophenol + myristate
-
 ?
3.1.1.3 4-nitrophenyl palmitate + H2O about 30% activity compared to 4-nitrophenyl laurate Serratia marcescens 4-nitrophenol + palmitate
-
 ?
3.1.1.3 4-nitrophenyl palmitate + H2O about 30% activity compared to 4-nitrophenyl laurate Serratia marcescens ECU1010 4-nitrophenol + palmitate
-
 ?
3.1.1.3 4-nitrophenyl propionate + H2O about 5% activity compared to 4-nitrophenyl laurate Serratia marcescens 4-nitrophenol + propionate
-
 ?
3.1.1.3 4-nitrophenyl propionate + H2O about 5% activity compared to 4-nitrophenyl laurate Serratia marcescens ECU1010 4-nitrophenol + propionate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.3 ? x * 65000, SDS-PAGE Serratia marcescens

Synonyms

EC Number Synonyms Comment Organism
3.1.1.3 lipase
-
 Serratia marcescens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.3 40
-
-
 Serratia marcescens

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.3 25 45 the purified lipase keeps not less than 80% of the maximum activity at 40°C in a temperature range of 25-45°C Serratia marcescens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.3 30 50 the recombinant lipase displays excellent stability below 30°C. After being incubated at temperatures of 30, 40, and 50°Cfor 0.5-2 h, the enzyme has a remaining residual activity of over 90% at 30°C compared with the initial activity before incubation. However, 0.5 h later, the residual activity decreases sharply when the temperature is above 50°C Serratia marcescens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.3 9
-
-
 Serratia marcescens

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.1.3 5 6.8 the recombinant lipase displays excellent stability at pH 5.0-6.8 and is stable over a pH range of 5.0-6.8 with more than 80% residual activity after being incubated at 4°C for 20 h Serratia marcescens