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Literature summary for 2.4.1.46 extracted from

  • Dubots, E.; Audry, M.; Yamaryo, Y.; Bastien, O.; Ohta, H.; Breton, C.; Marechal, E.; Block, M.A.
    Activation of the chloroplast monogalactosyldiacylglycerol synthase, MGD1, by phosphatidic acid and phosphatidylglycerol (2010), J. Biol. Chem., 285, 6003-6011.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
phosphatidic acid allosterically activates MGD1, half-maximal activation at about 0.2 mol%. With 0.15 mol% of phosphatidic acid, the enzyme velocity versus substrate curve is sigmoid, whereas with 1.5 mol% of phosphatidic acid, the curve is hyperbolic. MGDG synthase activity of leaf homogenates is dependent on the constant presence of phosphatidic acid, decrease of phosphatidic acid production leads to a decrease of the MGDG synthase activity. Molecular discrimination of phosphatidic acid and phosphatidylglycerol binding sites, overview Arabidopsis thaliana

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant C-terminally His6-tagged MGD1 in Escherichia coli Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
D150N the mutant shows enhanced activation by phosphatidylglycerol binding, but unaltered activation by phosphatidic acid compared to the wild-type enzyme Arabidopsis thaliana
P189A the mutant shows wild-type catalytic capability, but modified phosphatidylglycerol binding capability compared to the wild-type enzyme Arabidopsis thaliana
R260A the mutant shows enhanced activation by phosphatidylglycerol binding, but unaltered activation by phosphatidic acid compared to the wild-type enzyme Arabidopsis thaliana
W287A the mutant shows wild-type catalytic capability, but modified phosphatidylglycerol binding capability compared to the wild-type enzyme Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast envelope
-
Arabidopsis thaliana 9941
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Arabidopsis thaliana regulation of MGDGsynthesis by phosphatidic acid, which is a general precursor in the synthesis of all glycerolipids and is also a signaling molecule in plants ?
-
?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant C-terminally His6-tagged MGD1 from Escherichia coli by nickel affinity chromatography and gel filtration Arabidopsis thaliana

Source Tissue

Source Tissue Comment Organism Textmining
rosette leaf
-
Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information regulation of MGDGsynthesis by phosphatidic acid, which is a general precursor in the synthesis of all glycerolipids and is also a signaling molecule in plants Arabidopsis thaliana ?
-
?
additional information binding site for UDP-Gal lays in the cleft separating the two Rossmann folds involving residues of a conserved UDP-sugar binding pocket in the C-domain Arabidopsis thaliana ?
-
?

Subunits

Subunits Comment Organism
More the structure model for an MGD monomer comprises 2 Rossman domains, C- and N-domains Arabidopsis thaliana

Synonyms

Synonyms Comment Organism
MGD1
-
Arabidopsis thaliana
MGDG synthase
-
Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Arabidopsis thaliana

General Information

General Information Comment Organism
physiological function MGD1 is the main MGDG synthase expressed in leaves and is essential for chloroplast development, and enrichment of chloroplast membranes with monogalactosyldiacylglycerols Arabidopsis thaliana