Literature summary for 2.3.2.3 extracted from

Lennarz, W.J.; Bonsen, P.P.M.; Van Deenen, L.L.M.
Substrate specificity of O-L-lysylphosphatidylglycerol synthetase. Enzymatic studies on the structure of O-L-lysylphosphatidylglycerol (1967), Biochemistry, 6, 2307-2312.

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Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	anionic surfactant, e.g. sodium-salt of a fatty acid, and high ionic strength lead to activation	Staphylococcus aureus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	-	Staphylococcus aureus	16020	-

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
partial	Staphylococcus aureus

Storage Stability

Storage Stability	Organism
-20°C, membrane-bound enzyme extracted with organic solvents, t1/2: 3-5 days	Staphylococcus aureus
-20°C, native membrane-bound enzyme, several weeks	Staphylococcus aureus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-lysyl-tRNALys + phosphatidylglycerol	2'- (not 3'-) deoxy-analogue of phosphatidylglycerol can also act as L-lysyl-acceptor	Staphylococcus aureus	tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol	-	?

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Release 2023.1 (January 2023)