BRENDA - Enzyme Database

Activation of the chloroplast monogalactosyldiacylglycerol synthase, MGD1, by phosphatidic acid and phosphatidylglycerol

Dubots, E.; Audry, M.; Yamaryo, Y.; Bastien, O.; Ohta, H.; Breton, C.; Marechal, E.; Block, M.A.; J. Biol. Chem. 285, 6003-6011 (2010)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
2.4.1.46
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)
EC Number
Commentary
Organism
2.4.1.46
expression of wild-type and mutant C-terminally His6-tagged MGD1 in Escherichia coli
Arabidopsis thaliana
Engineering
EC Number
Amino acid exchange
Commentary
Organism
2.4.1.46
D150N
the mutant shows enhanced activation by phosphatidylglycerol binding, but unaltered activation by phosphatidic acid compared to the wild-type enzyme
Arabidopsis thaliana
2.4.1.46
P189A
the mutant shows wild-type catalytic capability, but modified phosphatidylglycerol binding capability compared to the wild-type enzyme
Arabidopsis thaliana
2.4.1.46
R260A
the mutant shows enhanced activation by phosphatidylglycerol binding, but unaltered activation by phosphatidic acid compared to the wild-type enzyme
Arabidopsis thaliana
2.4.1.46
W287A
the mutant shows wild-type catalytic capability, but modified phosphatidylglycerol binding capability compared to the wild-type enzyme
Arabidopsis thaliana
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.4.1.46
chloroplast envelope
-
Arabidopsis thaliana
9941
-
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.4.1.46
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
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.4.1.46
Arabidopsis thaliana
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
2.4.1.46
recombinant wild-type and mutant C-terminally His6-tagged MGD1 from Escherichia coli by nickel affinity chromatography and gel filtration
Arabidopsis thaliana
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
2.4.1.46
rosette leaf
-
Arabidopsis thaliana
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.4.1.46
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
704698
Arabidopsis thaliana
?
-
-
-
-
2.4.1.46
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
704698
Arabidopsis thaliana
?
-
-
-
-
Subunits
EC Number
Subunits
Commentary
Organism
2.4.1.46
More
the structure model for an MGD monomer comprises 2 Rossman domains, C- and N-domains
Arabidopsis thaliana
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.4.1.46
7.8
-
assay at
Arabidopsis thaliana
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
2.4.1.46
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) (protein specific)
EC Number
Commentary
Organism
2.4.1.46
expression of wild-type and mutant C-terminally His6-tagged MGD1 in Escherichia coli
Arabidopsis thaliana
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
2.4.1.46
D150N
the mutant shows enhanced activation by phosphatidylglycerol binding, but unaltered activation by phosphatidic acid compared to the wild-type enzyme
Arabidopsis thaliana
2.4.1.46
P189A
the mutant shows wild-type catalytic capability, but modified phosphatidylglycerol binding capability compared to the wild-type enzyme
Arabidopsis thaliana
2.4.1.46
R260A
the mutant shows enhanced activation by phosphatidylglycerol binding, but unaltered activation by phosphatidic acid compared to the wild-type enzyme
Arabidopsis thaliana
2.4.1.46
W287A
the mutant shows wild-type catalytic capability, but modified phosphatidylglycerol binding capability compared to the wild-type enzyme
Arabidopsis thaliana
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.4.1.46
chloroplast envelope
-
Arabidopsis thaliana
9941
-
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2.4.1.46
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
?
-
-
-
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
2.4.1.46
recombinant wild-type and mutant C-terminally His6-tagged MGD1 from Escherichia coli by nickel affinity chromatography and gel filtration
Arabidopsis thaliana
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
2.4.1.46
rosette leaf
-
Arabidopsis thaliana
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.4.1.46
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
704698
Arabidopsis thaliana
?
-
-
-
-
2.4.1.46
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
704698
Arabidopsis thaliana
?
-
-
-
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
2.4.1.46
More
the structure model for an MGD monomer comprises 2 Rossman domains, C- and N-domains
Arabidopsis thaliana
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.4.1.46
7.8
-
assay at
Arabidopsis thaliana
General Information
EC Number
General Information
Commentary
Organism
2.4.1.46
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
General Information (protein specific)
EC Number
General Information
Commentary
Organism
2.4.1.46
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