Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Aktas, M.; Koester, S.; Kizilirmak, S.; Casanova, J.C.; Betz, H.; Fritz, C.; Moser, R.; Yildiz, O.e.; Narberhaus, F.
    Enzymatic properties and substrate specificity of a bacterial phosphatidylcholine synthase (2014), FEBS J., 281, 3523-3541.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.8.24 recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli, recombinant expression of His6-tagged enzyme mutants in Escherichia coli strain C41 (DE3) Agrobacterium tumefaciens

Protein Variants

EC Number Protein Variants Comment Organism
2.7.8.24 D100A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Agrobacterium tumefaciens
2.7.8.24 D104A site-directed mutagenesis, inactive mutant Agrobacterium tumefaciens
2.7.8.24 D78A site-directed mutagenesis, almost inactive mutant Agrobacterium tumefaciens
2.7.8.24 G79A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Agrobacterium tumefaciens
2.7.8.24 G96A site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Agrobacterium tumefaciens
2.7.8.24 R83A site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Agrobacterium tumefaciens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.8.24 carnitine inhibits the enzyme's activity in vitro Agrobacterium tumefaciens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.8.24 additional information
-
 additional information choline-binding by the enzyme is cooperative Agrobacterium tumefaciens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.8.24 membrane the enzyme is an integral membrane protein, that consists of eight transmembrane segments with its N- and C-termini located in the cytoplasm, membrane topology of the enzyme, reaction mechanism, overview Agrobacterium tumefaciens 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.8.24 Mn2+ required for activity Agrobacterium tumefaciens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.8.24 400000
-
 His6-tagged recombinant enzyme, gel filtration Agrobacterium tumefaciens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.8.24 CDP-diacylglycerol + choline Agrobacterium tumefaciens
-
 CMP + phosphatidylcholine
-
 r
2.7.8.24 CDP-diacylglycerol + choline Agrobacterium tumefaciens C58 / ATCC 33970
-
 CMP + phosphatidylcholine
-
 r
2.7.8.24 additional information Agrobacterium tumefaciens no activity with gamma-butyrobetaine, betaine, and carnitine instead of choline ?
-
 ?
2.7.8.24 additional information Agrobacterium tumefaciens C58 / ATCC 33970 no activity with gamma-butyrobetaine, betaine, and carnitine instead of choline ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.8.24 Agrobacterium tumefaciens A9CIM3
-
-
2.7.8.24 Agrobacterium tumefaciens C58 / ATCC 33970 A9CIM3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.8.24 recombinant C-terminally His6-tagged enzyme from Escherichia coli by nickel affinity chromatography, recombinant His6-tagged enzyme mutants from Escherichia coli strain C41 (DE3) Agrobacterium tumefaciens

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.8.24 CDP-diacylglycerol + choline = CMP + phosphatidylcholine the enzyme reaction follows a reversible two-step reaction: in a first choline- and manganese-independent reaction, CDP-diacylglycerol is hydrolyzed releasing a CMP molecule. The resulting phosphatidyl intermediate reacts with choline in a second manganese-dependent step to form phosphatidylcholine Agrobacterium tumefaciens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.8.24 CDP-diacylglycerol + choline
-
 Agrobacterium tumefaciens CMP + phosphatidylcholine
-
 r
2.7.8.24 CDP-diacylglycerol + choline phosphatidylcholine formation by enzyme Pcs is reversible and proceeds via two successive reactions Agrobacterium tumefaciens CMP + phosphatidylcholine
-
 r
2.7.8.24 CDP-diacylglycerol + choline
-
 Agrobacterium tumefaciens C58 / ATCC 33970 CMP + phosphatidylcholine
-
 r
2.7.8.24 CDP-diacylglycerol + choline phosphatidylcholine formation by enzyme Pcs is reversible and proceeds via two successive reactions Agrobacterium tumefaciens C58 / ATCC 33970 CMP + phosphatidylcholine
-
 r
2.7.8.24 additional information no activity with gamma-butyrobetaine, betaine, and carnitine instead of choline Agrobacterium tumefaciens ?
-
 ?
2.7.8.24 additional information the enzyme exhibits broad substrate specificity towards choline derivatives. The presence of CDP-diacylglycerol and manganese is a prerequisite for cooperative binding of choline. No activity with gamma-butyrobetaine, betaine, and carnitine instead of choline Agrobacterium tumefaciens ?
-
 ?
2.7.8.24 additional information no activity with gamma-butyrobetaine, betaine, and carnitine instead of choline Agrobacterium tumefaciens C58 / ATCC 33970 ?
-
 ?
2.7.8.24 additional information the enzyme exhibits broad substrate specificity towards choline derivatives. The presence of CDP-diacylglycerol and manganese is a prerequisite for cooperative binding of choline. No activity with gamma-butyrobetaine, betaine, and carnitine instead of choline Agrobacterium tumefaciens C58 / ATCC 33970 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.8.24 oligomer x * 23000-30000, SDS-PAGE and sequence calculation, the enzyme forms stable oligomers Agrobacterium tumefaciens

Synonyms

EC Number Synonyms Comment Organism
2.7.8.24 PC synthase
-
 Agrobacterium tumefaciens
2.7.8.24 PCS
-
 Agrobacterium tumefaciens

General Information

EC Number General Information Comment Organism
2.7.8.24 additional information cytoplasmic loop between the second and third membrane helix contains the majority of the conserved amino acids of a CDP-alcohol phosphotransferase motif (DGX2ARX12GX3DX3D), crucial role of this motif in choline binding and enzyme activity Agrobacterium tumefaciens
2.7.8.24 physiological function phosphatidylcholine, produced by the enzyme, is essential for the expression of virulence-related genes that is controlled by the two-component system VirA/G Agrobacterium tumefaciens