The enzyme from the bacterium Acholeplasma laidlawii, which lacks a cell wall, produces the major non-bilayer lipid in the organism. The enzyme from the bacterium Agrobacterium tumefaciens acts under phosphate deprivation, generating glycolipids as surrogates for phospholipids. The enzyme belongs to the GT4 family of configuration-retaining glycosyltransferases. Many diacylglycerols with long-chain acyl groups can act as acceptors. cf. EC 2.4.1.336, monoglucosyldiacylglycerol synthase.
electrostatic association of the enzyme with membrane surface is accompanied by hydrophobic interactions and a conformational change. Binding kinetics fit a two-state model
The enzyme from the bacterium Acholeplasma laidlawii, which lacks a cell wall, produces the major non-bilayer lipid in the organism. The enzyme from the bacterium Agrobacterium tumefaciens acts under phosphate deprivation, generating glycolipids as surrogates for phospholipids. The enzyme belongs to the GT4 family of configuration-retaining glycosyltransferases. Many diacylglycerols with long-chain acyl groups can act as acceptors. cf. EC 2.4.1.336, monoglucosyldiacylglycerol synthase.
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
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
enzymic activity depends on the bilayer lipid environment. The activity depends on membrane binding per se but the enzyme must also adopt a certain conformation or orientation, and activity can be substantially modulated by interaction with various charged lipids or soluble molecules
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
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
stimulates the enzyme by an activating, potentially cooperative mechanism. Physiological concentrations of dioleoyl-phosphatidylglycerol influence the turnover number of the enzyme but not the interaction with UDP-glucose
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; can stimulate the MGlcDAG synthase activity efficiently with a concomitant protection toward proteolytic digestion
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
; associated with, in vitro enzyme binds less efficiently to liposomes containing only zwitterionic lipids whereas increasing fractions of anionic phosphatidyglycerol or cardiolipin strongly promote binding
enzyme deletion mutants lacking monoglucosyl diacylglycerol and glucuronosyl diacylglycerol or all glycolipids are not impaired in growth or virulence during infection of tobacco leaf discs
enzyme deletion mutants lacking monoglucosyl diacylglycerol and glucuronosyl diacylglycerol or all glycolipids are not impaired in growth or virulence during infection of tobacco leaf discs
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
Binding of the enzyme to lipid bilayers containing biological fractions of anionic lipids is essentially irreversible under most conditions examined. Binding is strongly influenced by anionic lipids, by nonbilayer-prone molecules and by charged polypeptides. Binding to membranes follows a two-step process. The binding is faster and stronger by electrostatic attraction, but hydrophobic interactions are also involved in enhancing the binding and activation process. Once the enzyme is bound to the membrane, it is practically glued in an irreversible fashion
during purification, the concentration of detergent is just as important as the type of detergent, and a low concentration of n-dodecyl-beta-D-maltoside (about 1 x critical micelle concentration) is the best for keeping the protein stable and homogeneous
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
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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
optimization of protein expression through controlling a few basic expression parameters, including temperature and growth media. The final expression level can be increased by two orders of magnitude, reaching 170 mg of pure protein per litre culture
Activating amphiphiles cause a conformational change of the 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii membranes according to proteolytic digestion
Berg, S.; Edman, M.; Li, L.; Wikstrom, M.; Wieslander, A.
Sequence properties of the 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii membranes: recognition of a large group of lipid glycosyltransferases in eubacteria and archaea
Li, L.; Storm, P.; Karlsson, O.P.; Berg, S.; Wieslander, A.
Irreversible binding and activity control of the 1,2-diacylglycerol 3-glucosyltransferase from Acholeplasma laidlawii at an anionic lipid bilayer surface
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2.4.1.337 1,2-diacylglycerol 3-alpha-glucosyltransferase
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