Literature summary for 2.4.1.337 extracted from

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 (2003), Biochemistry, 42, 9677-9686.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Acholeplasma laidlawii

Localization

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

Organism

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

Purification (Commentary)

Purification (Comment)	Organism
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	Acholeplasma laidlawii

Purification (Comment)

Organism

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

Acholeplasma laidlawii

Reaction

Reaction	Comment	Organism	Reaction ID
UDP-glucose + 1,2-diacyl-sn-glycerol = UDP + 3-D-glucosyl-1,2-diacyl-sn-glycerol	electrostatic association of the enzyme with membrane surface is accompanied by hydrophobic interactions and a conformational change. Binding kinetics fit a two-state model	Acholeplasma laidlawii	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	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	Acholeplasma laidlawii	?	-	?