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Literature summary for 4.1.1.65 extracted from

  • Dowhan, W.; Li, Q.X.
    Phosphatidylserine decarboxylase from Escherichia coli (1992), Methods Enzymol., 209, 348-359.
    View publication on PubMed
Search for more literature for 4.1.1.65

Protein Variants

Protein Variants Comment Organism
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
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

Inhibitors Comment Organism Structure
Hydrazines in presence of an amine Escherichia coli
hydroxylamine in presence of an amine Escherichia coli
NaBH4 in presence of an amine Escherichia coli
NaCNBH3 in presence of an amine Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane associated with cytoplasmic membrane Escherichia coli 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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
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
170000
-
 sucrose density gradient centrifugation in absence of Triton Escherichia coli
200000
-
 gel filtration in presence of Triton X-100 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
55
-
-
 Escherichia coli

Storage Stability

Storage Stability Organism
-80°C to -20°C, stable for several years Escherichia coli
0°C, stable for several months Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Phosphatidyl-L-serine
-
 Escherichia coli Phosphatidylethanolamine + CO2
-
 ?

Subunits

Subunits Comment Organism
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]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
 10 min, 50% loss of activity, membrane-associated enzyme Escherichia coli

pH Stability

pH Stability pH Stability Maximum Comment Organism
6.5 7.5 maximal stability in the range Escherichia coli