BRENDA - Enzyme Database

Phosphatidylserine decarboxylase from Escherichia coli

Dowhan, W.; Li, Q.X.; Methods Enzymol. 209, 348-359 (1992)

Data extracted from this reference:

Engineering
EC Number
Amino acid exchange
Commentary
Organism
4.1.1.65
S254C
S254C and S254T are posttranslationally processed and active enzyme is made in vivo although in significantly reduced amounts. From the S254A mutant only the proenzyme form is made, which has no enzymatic activity. In the case of the S254C and S254T mutant proteins about 10-20% of the proenzyme is processed to the alpha and beta subunits, resulting in 15% and 2%, respectively of the level of activity of the wild-type enzyme
Escherichia coli
4.1.1.65
S254T
S254C and S254T are posttranslationally processed and active enzyme is made in vivo although in significantly reduced amounts. From the S254A mutant only the proenzyme form is made, which has no enzymatic activity. In the case of the S254C and S254T mutant proteins about 10-20% of the proenzyme is processed to the alpha and beta subunits, resulting in 15% and 2%, respectively of the level of activity of the wild-type enzyme
Escherichia coli
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
4.1.1.65
Hydrazines
in presence of an amine
Escherichia coli
4.1.1.65
hydroxylamine
in presence of an amine
Escherichia coli
4.1.1.65
NaBH4
in presence of an amine
Escherichia coli
4.1.1.65
NaCNBH3
in presence of an amine
Escherichia coli
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
4.1.1.65
membrane
associated with cytoplasmic membrane
Escherichia coli
16020
-
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
4.1.1.65
7332
-
x * 7332, alpha, + x * 28579, beta, the heterodimeric enzyme appears to form a defined multimeric structure in the absence of detergent and associate with detergent micelles to form a large detergent micelle-protein complex which is still made up of some multiple of the heterodimer
Escherichia coli
4.1.1.65
28579
-
x * 7332, alpha, + x * 28579, beta, the heterodimeric enzyme appears to form a defined multimeric structure in the absence of detergent and associate with detergent micelles to form a large detergent micelle-protein complex which is still made up of some multiple of the heterodimer
Escherichia coli
4.1.1.65
170000
-
sucrose density gradient centrifugation in absence of Triton
Escherichia coli
4.1.1.65
200000
-
gel filtration in presence of Triton X-100
Escherichia coli
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.1.1.65
Escherichia coli
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
4.1.1.65
-
Escherichia coli
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.1.1.65
55
-
-
Escherichia coli
Storage Stability
EC Number
Storage Stability
Organism
4.1.1.65
-80°C to -20°C, stable for several years
Escherichia coli
4.1.1.65
0°C, stable for several months
Escherichia coli
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.1.1.65
Phosphatidyl-L-serine
-
4786
Escherichia coli
Phosphatidylethanolamine + CO2
-
4786
Escherichia coli
-
Subunits
EC Number
Subunits
Commentary
Organism
4.1.1.65
dimer
x * 7332, alpha, + x * 28579, beta, the heterodimeric enzyme appears to form a defined multimeric structure in the absence of detergent and associate with detergent micelles to form a large detergent micelle-protein complex which is still made up of some multiple of the heterodimer
Escherichia coli
Temperature Stability [°C]
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
4.1.1.65
65
-
10 min, 50% loss of activity, membrane-associated enzyme
Escherichia coli
pH Stability
EC Number
pH Stability
pH Stability Maximum
Commentary
Organism
4.1.1.65
6.5
7.5
maximal stability in the range
Escherichia coli
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
4.1.1.65
S254C
S254C and S254T are posttranslationally processed and active enzyme is made in vivo although in significantly reduced amounts. From the S254A mutant only the proenzyme form is made, which has no enzymatic activity. In the case of the S254C and S254T mutant proteins about 10-20% of the proenzyme is processed to the alpha and beta subunits, resulting in 15% and 2%, respectively of the level of activity of the wild-type enzyme
Escherichia coli
4.1.1.65
S254T
S254C and S254T are posttranslationally processed and active enzyme is made in vivo although in significantly reduced amounts. From the S254A mutant only the proenzyme form is made, which has no enzymatic activity. In the case of the S254C and S254T mutant proteins about 10-20% of the proenzyme is processed to the alpha and beta subunits, resulting in 15% and 2%, respectively of the level of activity of the wild-type enzyme
Escherichia coli
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
4.1.1.65
Hydrazines
in presence of an amine
Escherichia coli
4.1.1.65
hydroxylamine
in presence of an amine
Escherichia coli
4.1.1.65
NaBH4
in presence of an amine
Escherichia coli
4.1.1.65
NaCNBH3
in presence of an amine
Escherichia coli
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
4.1.1.65
membrane
associated with cytoplasmic membrane
Escherichia coli
16020
-
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
4.1.1.65
7332
-
x * 7332, alpha, + x * 28579, beta, the heterodimeric enzyme appears to form a defined multimeric structure in the absence of detergent and associate with detergent micelles to form a large detergent micelle-protein complex which is still made up of some multiple of the heterodimer
Escherichia coli
4.1.1.65
28579
-
x * 7332, alpha, + x * 28579, beta, the heterodimeric enzyme appears to form a defined multimeric structure in the absence of detergent and associate with detergent micelles to form a large detergent micelle-protein complex which is still made up of some multiple of the heterodimer
Escherichia coli
4.1.1.65
170000
-
sucrose density gradient centrifugation in absence of Triton
Escherichia coli
4.1.1.65
200000
-
gel filtration in presence of Triton X-100
Escherichia coli
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
4.1.1.65
-
Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.1.1.65
55
-
-
Escherichia coli
Storage Stability (protein specific)
EC Number
Storage Stability
Organism
4.1.1.65
-80°C to -20°C, stable for several years
Escherichia coli
4.1.1.65
0°C, stable for several months
Escherichia coli
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.1.1.65
Phosphatidyl-L-serine
-
4786
Escherichia coli
Phosphatidylethanolamine + CO2
-
4786
Escherichia coli
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
4.1.1.65
dimer
x * 7332, alpha, + x * 28579, beta, the heterodimeric enzyme appears to form a defined multimeric structure in the absence of detergent and associate with detergent micelles to form a large detergent micelle-protein complex which is still made up of some multiple of the heterodimer
Escherichia coli
Temperature Stability [°C] (protein specific)
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
4.1.1.65
65
-
10 min, 50% loss of activity, membrane-associated enzyme
Escherichia coli
pH Stability (protein specific)
EC Number
pH Stability
pH Stability Maximum
Commentary
Organism
4.1.1.65
6.5
7.5
maximal stability in the range
Escherichia coli