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Literature summary extracted from

  • Dowhan, W.; Li, Q.X.
    Phosphatidylserine decarboxylase from Escherichia coli (1992), Methods Enzymol., 209, 348-359.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment 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 Comment 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 Comment 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] Comment 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 UniProt Comment Textmining
4.1.1.65 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) 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] Comment 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.65 Phosphatidyl-L-serine
-
Escherichia coli Phosphatidylethanolamine + CO2
-
?

Subunits

EC Number Subunits Comment 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] Comment 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 Comment Organism
4.1.1.65 6.5 7.5 maximal stability in the range Escherichia coli