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Literature summary for 2.4.1.337 extracted from

  • Li, L.; Karlsson, O.P.; Wieslander, A.
    Activating amphiphiles cause a conformational change of the 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii membranes according to proteolytic digestion (1997), J. Biol. Chem., 272, 29602-29606.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
dodecylphosphoglycerol anionic amphiphiles are essential for the restoration of a proper conformation. Amphiphilic environment with a critical fraction of negatively charged headgroups induces a catalytic, active site conformation of the enzyme Acholeplasma laidlawii
dodecylphosphoglycerol can stimulate the MGlcDAG synthase activity efficiently with a concomitant protection toward proteolytic digestion Acholeplasma laidlawii
phosphatidylglycerol anionic amphiphiles are essential for the restoration of a proper conformation. Amphiphilic environment with a critical fraction of negatively charged headgroups induces a catalytic, active site conformation of the enzyme Acholeplasma laidlawii

General Stability

General Stability Organism
total digestion by proteinase K, trypsin or chymotrypsin when no lipid is present, the activity is highly restored in micelles containing 1,2-dioleoyl-phosphatidylglycerol and 1,2-dioleoyl-phosphatidylserine Acholeplasma laidlawii

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Acholeplasma laidlawii 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDPglucose + 1,2-diacylglycerol Acholeplasma laidlawii the enzyme synthesizes the major nonbilayer-prone lipid monoglucosyldiacylglycerol in the membrane, which is important for spontaneous curvature, and is an important site for the lipid surface charge density UDP + 3-D-glucosyl-1,2-diacylglycerol
-
?

Organism

Organism UniProt Comment Textmining
Acholeplasma laidlawii
-
-
-
Acholeplasma laidlawii Q93P60
-
-

Purification (Commentary)

Purification (Comment) Organism
proteolytic resistance shows a good correlation with the enzyme activity in various lipid-CHAPS mixed micelles. Anionic lipids 1,2-dioleoyl-phosphatidylglycerol and 1,2-dioleoyl-posphatidylserine are able to protect the exposed MGlc-DAG synthase from digestion, whereas 1,2-dioleoyl-phosphatidylcholine and diglucosyldiacylglycerol can not. The detergent dodecylphosphoglycerol can also stimulate the MGlcDAG synthase activity efficiently with a concomitant protection toward proteolytic digestion Acholeplasma laidlawii

Renatured (Commentary)

Renatured (Comment) Organism
critical fractions of anionic phospholipids 1,2-dioleoyl-phosphatidylglycerol and 1,2-dioleoyl-posphatidylserine are essential for the restoration of enzyme activity, while the zwitterionic 1,2-dioleoyl-phosphatidylcholine and the uncharged diglucosyldiacylglycerol are not Acholeplasma laidlawii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDPglucose + 1,2-diacylglycerol
-
Acholeplasma laidlawii UDP + 3-D-glucosyl-1,2-diacylglycerol
-
?
UDPglucose + 1,2-diacylglycerol the enzyme synthesizes the major nonbilayer-prone lipid monoglucosyldiacylglycerol in the membrane, which is important for spontaneous curvature, and is an important site for the lipid surface charge density Acholeplasma laidlawii UDP + 3-D-glucosyl-1,2-diacylglycerol
-
?

Synonyms

Synonyms Comment Organism
MGlcDAG synthase
-
Acholeplasma laidlawii

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
28
-
half-life in 1,2-dioleoylphosphatidylglycerol-CHAPS micelles is more than 2 h, half-life is less than 0.5 h in 1,2-dioleoylphosphatidylcholine-CHAPS micelles Acholeplasma laidlawii