1-O-Hexadecyl-sn-glycero-3-phosphocholine

Lyso-PAF C-16 can be formed by either the action of PAF-AH on PAF C-16, or by the action of a CoA-independent transacylase on 1-O-hexadecyl-2-acyl-glycerophosphocholine. Lyso-PAF C-16 is a substrate for either PAF C-16 formation by the remodeling pathway or selective acylation with arachidonic acid by a CoA-independent transacylase.

white solid

Lyso-PAF C-16 is an inactive platelet activating factor (PAF).

Lyso-PAF C-16 can be formed by either the action of PAF-AH on PAF C-16, or by the action of a CoA-independent transacylase on 1-O-hexadecyl-2-acyl-glycerophosphocholine. Lyso-PAF C-16 is a substrate for either PAF C-16 formation by the remodeling pathway or selective acylation with arachidonic acid by a CoA-independent transacylase.

ChEBI: Lysophosphatidylcholine O-16:0/0:0 is a lysophosphatidylcholine O-16:0e in which the hexadecyl group at C-1 contains 16 carbons of which none are unsaturated. It has a role as a metabolite. It is a lysophosphatidylcholine O-16:0 and a 1-alkyl-sn-glycero-3-phosphocholine.

[1] D M STAFFORINI  L W T. Human plasma platelet-activating factor acetylhydrolase.[J]. Methods in molecular biology, 1999, 109: 49-58. DOI: 10.1385/1-59259-581-2:49
[2] Y. UEMURA F S T Lee. A coenzyme A-independent transacylase is linked to the formation of platelet-activating factor (PAF) by generating the lyso-PAF intermediate in the remodeling pathway.[J]. The Journal of Biological Chemistry, 1991, 50 1: 8268-8272. DOI: 10.1016/s0021-9258(18)92972-8
[3] M E VENABLE. Conversion of 1-O-[3H]alkyl-2-arachidonoyl-sn-glycero-3-phosphorylcholine to lyso platelet-activating factor by the CoA-independent transacylase in membrane fractions of human neutrophils.[J]. The Journal of Biological Chemistry, 1991, 266 28: 18691-18698.
[4] K DEGUCHI  A D  S Murashima. [Platelet activating factor].[J]. Nihon rinsho. Japanese journal of clinical medicine, 1987, 45 5: 1115-1126.
[5] M. VENABLE. Enzymatic studies of lyso platelet-activating factor acylation in human neutrophils and changes upon stimulation.[J]. The Journal of Biological Chemistry, 1993, 49 1: 7965-7975. DOI: 10.1016/s0021-9258(18)53052-0