Tetraacyldisaccharide 4'-kinase is an enzyme that phosphorylates the 4'-position of a tetraacyldisaccharide 1-phosphate precursor (DS-1-P) of lipopolysaccharide lipid A. This lipid forms outer membranes of Gram-negative bacteria.[1] This enzyme catalyzes the chemical reaction
- ATP + [2-N,3-O-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl]-(1->6)-[2- N,3-O-bis(3-hydroxytetradecanoyl)-beta-D-glucosaminyl phosphate] ADP + [2-N,3-O-bis(3-hydroxytetradecanoyl)-4-O-phosphono-beta-D- glucosaminyl]-(1->6)-[2-N,3-O-bis(3-hydroxytetradecanoyl)-beta-D- glucosaminyl phosphate]
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor.
References
- ^ Garrett TA, Que NL, Raetz CR (May 1998). "Accumulation of a lipid A precursor lacking the 4'-phosphate following inactivation of the Escherichia coli lpxK gene". J. Biol. Chem. 273 (20): 12457–65. doi:10.1074/jbc.273.20.12457. PMID 9575203.
- Ray BL, Raetz CR (1987). "The biosynthesis of gram-negative endotoxin. A novel kinase in Escherichia coli membranes that incorporates the 4'-phosphate of lipid A". J. Biol. Chem. 262 (3): 1122–8. doi:10.1016/S0021-9258(19)75759-7. PMID 3027079.
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