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show all sequences of 3.1.1.3

Molecular cloning and functional expression of esf gene encoding enantioselective lipase from Serratia marcescens ES-2 for kinetic resolution of optically active (S)-flurbiprofen

Lee, K.W.; Bae, H.A.; Lee, Y.H.; J. Microbiol. Biotechnol. 17, 74-80 (2007)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
additional information
Triton X-207 induces and enhances enzyme secretion from the overexpressing Serratia marcescens strain best at 3.0%, effect of surfactants on secretion of enantioselective Esf lipase in transformant strain BESF overexpressing the esf gene
Serratia marcescens
Cloned(Commentary)
Commentary
Organism
gene esf, construction and screening of a genetic library, DNA and amino acid sequence determination and analysis, reintroduction, overexpression in, and secretion from the transformed parent strain ES-2, i.e. strain BESF, expression as His-tagged enzyme in Escherichia coli
Serratia marcescens
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
extracellular
enzyme secretion, the Esf lipase does not possess an N-terminal signal sequence commonly required for the secretion of lipase, but it contains an extreme C-terminal motif consisting of a hydrophobic five-residue sequence that can be recognized by an ABC-transporter system correlated to a signal peptide-independent mechanism for the secretion of protein in Gram-negative bacteria
Serratia marcescens
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates 4.6fold at 10 mM, the Esf lipase contains a nine-residue GGXGXDXXX sequence motif in the upstream region of the C-terminal motif, known to form a parallel beta-roll structure binding Ca2+ ions
Serratia marcescens
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
64978
-
x * 64978, sequence calculation, x * 65000, wild-type enzyme, SDS-PAGE, x * 69000, recombinant His-tagged enzyme
Serratia marcescens
65000
-
x * 64978, sequence calculation, x * 65000, wild-type enzyme, SDS-PAGE, x * 69000, recombinant His-tagged enzyme
Serratia marcescens
69000
-
x * 64978, sequence calculation, x * 65000, wild-type enzyme, SDS-PAGE, x * 69000, recombinant His-tagged enzyme
Serratia marcescens
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Serratia marcescens
Q0MVP2
gene esf
-
Serratia marcescens ES-2
Q0MVP2
gene esf
-
Purification (Commentary)
Commentary
Organism
native secreted enantioselective lipase 12.1fold from culture supernatant by ultrafiltration, hydrophobic interaction and anion exchange chromatography
Serratia marcescens
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Serratia marcescens
58.4
-
purified Esf lipase
Serratia marcescens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R,S)-flurbiprofen ethyl ester + H2O
high enantiomeric excess and conversion yield of 98% and 48%, respectively
681358
Serratia marcescens
(S)-flurbiprofen + ethanol
-
-
-
?
4-nitrophenyl butyrate + H2O
-
681358
Serratia marcescens
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
-
681358
Serratia marcescens ES-2
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl caprate + H2O
high activity
681358
Serratia marcescens
4-nitrophenol + caprate
-
-
-
?
4-nitrophenyl caproate + H2O
high activity
681358
Serratia marcescens
4-nitrophenol + caproate
-
-
-
?
4-nitrophenyl caproate + H2O
high activity
681358
Serratia marcescens ES-2
4-nitrophenol + caproate
-
-
-
?
4-nitrophenyl caprylate + H2O
best 4-nitrophenyl ester substrate
681358
Serratia marcescens
4-nitrophenol + caprylate
-
-
-
?
4-nitrophenyl caprylate + H2O
best 4-nitrophenyl ester substrate
681358
Serratia marcescens ES-2
4-nitrophenol + caprylate
-
-
-
?
4-nitrophenyl laurate + H2O
-
681358
Serratia marcescens
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl myristate + H2O
-
681358
Serratia marcescens
4-nitrophenol + myristate
-
-
-
?
4-nitrophenyl palmitate + H2O
low activity
681358
Serratia marcescens
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl propionate + H2O
low activity
681358
Serratia marcescens
4-nitrophenol + propionate
-
-
-
?
4-nitrophenyl propionate + H2O
low activity
681358
Serratia marcescens ES-2
4-nitrophenol + propionate
-
-
-
?
additional information
substrate specificity, no or poor activity with tributyrin, triacetin, tripropionin, tristearin, 4-nitrophenyl stearate, and 4-nitrophenyl acetate, the lipase shows preferential substrate specificity toward the medium-chain-length fatty acids, overview
681358
Serratia marcescens
?
-
-
-
-
additional information
substrate specificity, no or poor activity with tributyrin, triacetin, tripropionin, tristearin, 4-nitrophenyl stearate, and 4-nitrophenyl acetate, the lipase shows preferential substrate specificity toward the medium-chain-length fatty acids, overview
681358
Serratia marcescens ES-2
?
-
-
-
-
tricaprin + H2O
best triacylglyceride substrate
681358
Serratia marcescens
dicaprin + caprate
-
-
-
?
tricaproin + H2O
-
681358
Serratia marcescens
dicaproin + caproate
-
-
-
?
tricaprylin + H2O
-
681358
Serratia marcescens
dicaprylin + caprylate
-
-
-
?
trilaurin + H2O
high activity
681358
Serratia marcescens
dilaurin + laurate
-
-
-
?
trimyristin + H2O
-
681358
Serratia marcescens
dimyristin + myristate
-
-
-
?
tripalmitin + H2O
low activity
681358
Serratia marcescens
dipalmitin + palmitate
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 64978, sequence calculation, x * 65000, wild-type enzyme, SDS-PAGE, x * 69000, recombinant His-tagged enzyme
Serratia marcescens
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
-
Serratia marcescens
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
20
80
-
Serratia marcescens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Serratia marcescens
pH Range
pH Minimum
pH Maximum
Commentary
Organism
4
11
-
Serratia marcescens
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
additional information
Triton X-207 induces and enhances enzyme secretion from the overexpressing Serratia marcescens strain best at 3.0%, effect of surfactants on secretion of enantioselective Esf lipase in transformant strain BESF overexpressing the esf gene
Serratia marcescens
Cloned(Commentary) (protein specific)
Commentary
Organism
gene esf, construction and screening of a genetic library, DNA and amino acid sequence determination and analysis, reintroduction, overexpression in, and secretion from the transformed parent strain ES-2, i.e. strain BESF, expression as His-tagged enzyme in Escherichia coli
Serratia marcescens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
extracellular
enzyme secretion, the Esf lipase does not possess an N-terminal signal sequence commonly required for the secretion of lipase, but it contains an extreme C-terminal motif consisting of a hydrophobic five-residue sequence that can be recognized by an ABC-transporter system correlated to a signal peptide-independent mechanism for the secretion of protein in Gram-negative bacteria
Serratia marcescens
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Ca2+
activates 4.6fold at 10 mM, the Esf lipase contains a nine-residue GGXGXDXXX sequence motif in the upstream region of the C-terminal motif, known to form a parallel beta-roll structure binding Ca2+ ions
Serratia marcescens
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
64978
-
x * 64978, sequence calculation, x * 65000, wild-type enzyme, SDS-PAGE, x * 69000, recombinant His-tagged enzyme
Serratia marcescens
65000
-
x * 64978, sequence calculation, x * 65000, wild-type enzyme, SDS-PAGE, x * 69000, recombinant His-tagged enzyme
Serratia marcescens
69000
-
x * 64978, sequence calculation, x * 65000, wild-type enzyme, SDS-PAGE, x * 69000, recombinant His-tagged enzyme
Serratia marcescens
Purification (Commentary) (protein specific)
Commentary
Organism
native secreted enantioselective lipase 12.1fold from culture supernatant by ultrafiltration, hydrophobic interaction and anion exchange chromatography
Serratia marcescens
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Serratia marcescens
58.4
-
purified Esf lipase
Serratia marcescens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R,S)-flurbiprofen ethyl ester + H2O
high enantiomeric excess and conversion yield of 98% and 48%, respectively
681358
Serratia marcescens
(S)-flurbiprofen + ethanol
-
-
-
?
4-nitrophenyl butyrate + H2O
-
681358
Serratia marcescens
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
-
681358
Serratia marcescens ES-2
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl caprate + H2O
high activity
681358
Serratia marcescens
4-nitrophenol + caprate
-
-
-
?
4-nitrophenyl caproate + H2O
high activity
681358
Serratia marcescens
4-nitrophenol + caproate
-
-
-
?
4-nitrophenyl caproate + H2O
high activity
681358
Serratia marcescens ES-2
4-nitrophenol + caproate
-
-
-
?
4-nitrophenyl caprylate + H2O
best 4-nitrophenyl ester substrate
681358
Serratia marcescens
4-nitrophenol + caprylate
-
-
-
?
4-nitrophenyl caprylate + H2O
best 4-nitrophenyl ester substrate
681358
Serratia marcescens ES-2
4-nitrophenol + caprylate
-
-
-
?
4-nitrophenyl laurate + H2O
-
681358
Serratia marcescens
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl myristate + H2O
-
681358
Serratia marcescens
4-nitrophenol + myristate
-
-
-
?
4-nitrophenyl palmitate + H2O
low activity
681358
Serratia marcescens
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl propionate + H2O
low activity
681358
Serratia marcescens
4-nitrophenol + propionate
-
-
-
?
4-nitrophenyl propionate + H2O
low activity
681358
Serratia marcescens ES-2
4-nitrophenol + propionate
-
-
-
?
additional information
substrate specificity, no or poor activity with tributyrin, triacetin, tripropionin, tristearin, 4-nitrophenyl stearate, and 4-nitrophenyl acetate, the lipase shows preferential substrate specificity toward the medium-chain-length fatty acids, overview
681358
Serratia marcescens
?
-
-
-
-
additional information
substrate specificity, no or poor activity with tributyrin, triacetin, tripropionin, tristearin, 4-nitrophenyl stearate, and 4-nitrophenyl acetate, the lipase shows preferential substrate specificity toward the medium-chain-length fatty acids, overview
681358
Serratia marcescens ES-2
?
-
-
-
-
tricaprin + H2O
best triacylglyceride substrate
681358
Serratia marcescens
dicaprin + caprate
-
-
-
?
tricaproin + H2O
-
681358
Serratia marcescens
dicaproin + caproate
-
-
-
?
tricaprylin + H2O
-
681358
Serratia marcescens
dicaprylin + caprylate
-
-
-
?
trilaurin + H2O
high activity
681358
Serratia marcescens
dilaurin + laurate
-
-
-
?
trimyristin + H2O
-
681358
Serratia marcescens
dimyristin + myristate
-
-
-
?
tripalmitin + H2O
low activity
681358
Serratia marcescens
dipalmitin + palmitate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 64978, sequence calculation, x * 65000, wild-type enzyme, SDS-PAGE, x * 69000, recombinant His-tagged enzyme
Serratia marcescens
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
-
Serratia marcescens
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
20
80
-
Serratia marcescens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
-
Serratia marcescens
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
4
11
-
Serratia marcescens
Other publictions for EC 3.1.1.3
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)