Acyl Coenzyme A:1-Acylglycerophosphorylglycerol Acyltransferase from Rat Liver
Rat liver microsomes are capable of catalyzing the acylation of 1-palmitoyl- sn -glycero-3-phosphoryl- rac -glycerol for phosphatidylglycerol formation. The requirements for the reaction appear to be the same as the analogous reaction for lecithin synthesis. In contrast, however, to oleoyl-CoA:1-pal...
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Veröffentlicht in: | The Journal of biological chemistry 1973-04, Vol.248 (8), p.2906-2911 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Rat liver microsomes are capable of catalyzing the acylation of 1-palmitoyl- sn -glycero-3-phosphoryl- rac -glycerol for phosphatidylglycerol formation. The requirements for the reaction appear to be the same as the analogous reaction
for lecithin synthesis. In contrast, however, to oleoyl-CoA:1-palmitoyl- sn -glycero-3-phosphorylcholine acyltransferase, which has a pH optimum of 7.0, oleoyl-CoA:1-palmitoyl- sn -glycero-3-phosphoryl- rac -glycerol acyltransferase functions optimally at pH 9.0. The latter is also distinguishable by being more stable at the alkaline
pH than the former. The data indicate that in addition to positional specificity and acyl group preferability, acyl-CoA:acyl
glycerophospholipid acyltransferases also possess phosphorylalcohol group specificity. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(19)44093-3 |