Biosynthesis of castor oil: effect of polyamines on the acylation of lysophosphatidic acid at the sn-2 position with ricinoleic acid.
Polyamines with diamine structures of chain length longer than 3C were essential for the synthesis of phosphatidic acid (PA) from ricinoleoyl-CoA and lysophosphatidic acid (LPA) by the castor LPA acyltransferase reaction, suggesting that polyamines modulate enzyme affinity for the acyl-CoA substrate in vivo.
Tomosugi
Mitsuhiro
M
Department of Biological Chemistry, Faculty of Agriculture, Kyoto Prefectural University, Shimogamo, Kyoto, Japan. a0120712@kpu.ac.jp
Ohshiro
Akane
A
Hara
Shin'ichiro
S
Ichihara
Ken'ichi
K
D000214:Acyl Coenzyme A / Q000378:metabolism; D000215:Acylation / Q000187:drug effects; D002368:Castor Oil / Q000096:biosynthesis*; D008246:Lysophospholipids / Q000378:metabolism*; D010712:Phosphatidic Acids / Q000096:biosynthesis; D011073:Polyamines / Q000494:pharmacology*; D012277:Ricinoleic Acids / Q000378:metabolism
D000214:Acyl Coenzyme A; D008246:Lysophospholipids; D010712:Phosphatidic Acids; D011073:Polyamines; D012277:Ricinoleic Acids; D002368:Castor Oil; C030521:ricinoleic acid; C032881:lysophosphatidic acid