BRENDA - Enzyme Database

Identification, purification, and characterization of a thermally stable lipase from rice bran. A new member of the (phospho) lipase family

Bhardwaj, K.; Raju, A.; Rajasekharan, R.; Plant Physiol. 127, 1728-1738 (2001)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
3.1.1.3
potassium acetate
20-200 mM, 4-5fold increase in activity
Oryza sativa
3.1.1.3
Sodium acetate
20 mM, 2fold increase in activity, no effect at higher concentration at pH 7.5
Oryza sativa
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
3.1.1.3
Cd2+
about 70% inhibition at 2 mM
Oryza sativa
3.1.1.3
CHAPS
inhibitory at 0.5 mM
Oryza sativa
3.1.1.3
Cu2+
about 70% inhibition at 2 mM
Oryza sativa
3.1.1.3
Digitonin
inhibitory at 0.5 mM
Oryza sativa
3.1.1.3
diisopropyl fluorophosphate
inhibits both lipase and phospholipase activities of the enzyme
Oryza sativa
3.1.1.3
Mg2+
about 70% inhibition at 2 mM
Oryza sativa
3.1.1.3
additional information
no inhibition by Ca2+, Triton X-100 and NP-40 decreased the activity marginally at lower concentrations and then restorde the activity at 4 mM
Oryza sativa
3.1.1.3
SDS
50% inhibition at 2mM
Oryza sativa
3.1.1.3
Zn2+
about 70% inhibition at 2 mM
Oryza sativa
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.1.1.3
1.02
-
phosphocholine
pH 7.5, 37°C
Oryza sativa
3.1.1.3
6.71
-
triolein
pH 7.5, 37°C
Oryza sativa
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
3.1.1.3
9400
-
gel filtration and MALDI
Oryza sativa
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.1.1.3
Oryza sativa
-
-
-
Posttranslational Modification
EC Number
Posttranslational Modification
Commentary
Organism
3.1.1.3
glycoprotein
-
Oryza sativa
Purification (Commentary)
EC Number
Commentary
Organism
3.1.1.3
7.6fold to homogeneity
Oryza sativa
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
3.1.1.3
seed coat
-
Oryza sativa
-
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
3.1.1.3
0.00012
-
purified enzyme, phospholipase activity
Oryza sativa
3.1.1.3
0.38
-
purified enzyme, lipase activity
Oryza sativa
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.1.3
diacylglycerol + H2O
-
653521
Oryza sativa
fatty acid + acylglycerol
-
653521
Oryza sativa
?
3.1.1.3
additional information
enzyme also provides phospholipase A2 activity, it preferentially hydrolyzes the sn-2-position of the substrate
653521
Oryza sativa
?
-
653521
Oryza sativa
?
3.1.1.3
phosphatidylethanolamine + H2O
-
653521
Oryza sativa
?
-
653521
Oryza sativa
?
3.1.1.3
triolein + H2O
enzyme shows no positional specificity towards the triacylglycerol
653521
Oryza sativa
diolein + oleate
-
653521
Oryza sativa
?
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
3.1.1.3
80
-
-
Oryza sativa
Temperature Stability [°C]
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
3.1.1.3
20
90
completely stable up to 40°C, 65% remaining activity at 60°C after 1 h, 76°C is the transition temperature, the enzyme is still active and retains most of its secondary structure at 90°C, 34% remaining activity at 90°C after 15 min pretreatment at 90°C, 16% remaining activity at 37°C after 15 min pretreatment at 90°C
Oryza sativa
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.1.1.3
11
-
-
Oryza sativa
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
3.1.1.3
potassium acetate
20-200 mM, 4-5fold increase in activity
Oryza sativa
3.1.1.3
Sodium acetate
20 mM, 2fold increase in activity, no effect at higher concentration at pH 7.5
Oryza sativa
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
3.1.1.3
Cd2+
about 70% inhibition at 2 mM
Oryza sativa
3.1.1.3
CHAPS
inhibitory at 0.5 mM
Oryza sativa
3.1.1.3
Cu2+
about 70% inhibition at 2 mM
Oryza sativa
3.1.1.3
Digitonin
inhibitory at 0.5 mM
Oryza sativa
3.1.1.3
diisopropyl fluorophosphate
inhibits both lipase and phospholipase activities of the enzyme
Oryza sativa
3.1.1.3
Mg2+
about 70% inhibition at 2 mM
Oryza sativa
3.1.1.3
additional information
no inhibition by Ca2+, Triton X-100 and NP-40 decreased the activity marginally at lower concentrations and then restorde the activity at 4 mM
Oryza sativa
3.1.1.3
SDS
50% inhibition at 2mM
Oryza sativa
3.1.1.3
Zn2+
about 70% inhibition at 2 mM
Oryza sativa
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.1.1.3
1.02
-
phosphocholine
pH 7.5, 37°C
Oryza sativa
3.1.1.3
6.71
-
triolein
pH 7.5, 37°C
Oryza sativa
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
3.1.1.3
9400
-
gel filtration and MALDI
Oryza sativa
Posttranslational Modification (protein specific)
EC Number
Posttranslational Modification
Commentary
Organism
3.1.1.3
glycoprotein
-
Oryza sativa
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
3.1.1.3
7.6fold to homogeneity
Oryza sativa
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
3.1.1.3
seed coat
-
Oryza sativa
-
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
3.1.1.3
0.00012
-
purified enzyme, phospholipase activity
Oryza sativa
3.1.1.3
0.38
-
purified enzyme, lipase activity
Oryza sativa
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.1.3
diacylglycerol + H2O
-
653521
Oryza sativa
fatty acid + acylglycerol
-
653521
Oryza sativa
?
3.1.1.3
additional information
enzyme also provides phospholipase A2 activity, it preferentially hydrolyzes the sn-2-position of the substrate
653521
Oryza sativa
?
-
653521
Oryza sativa
?
3.1.1.3
phosphatidylethanolamine + H2O
-
653521
Oryza sativa
?
-
653521
Oryza sativa
?
3.1.1.3
triolein + H2O
enzyme shows no positional specificity towards the triacylglycerol
653521
Oryza sativa
diolein + oleate
-
653521
Oryza sativa
?
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
3.1.1.3
80
-
-
Oryza sativa
Temperature Stability [°C] (protein specific)
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
3.1.1.3
20
90
completely stable up to 40°C, 65% remaining activity at 60°C after 1 h, 76°C is the transition temperature, the enzyme is still active and retains most of its secondary structure at 90°C, 34% remaining activity at 90°C after 15 min pretreatment at 90°C, 16% remaining activity at 37°C after 15 min pretreatment at 90°C
Oryza sativa
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.1.1.3
11
-
-
Oryza sativa