Substrate Specificity of Acyl-CoA:Lysophospholipid Acyltransferase (LAT) from Pig Spleen

The present investigation was undertaken to gain insights into the nature of both substrate binding sites of acyl-CoA:lysophospholipid acyltransferase (LAT) which could be potentially useful for the identification and purification of this specific acyltransferase. Therefore, we have investigated the...

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Veröffentlicht in:Archives of biochemistry and biophysics 1998-03, Vol.351 (2), p.220-226
Hauptverfasser: Kerkhoff, Claus, Habben, Kai, Gehring, Lars, Resch, Klaus, Kaever, Volkhard
Format: Artikel
Sprache:eng
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Zusammenfassung:The present investigation was undertaken to gain insights into the nature of both substrate binding sites of acyl-CoA:lysophospholipid acyltransferase (LAT) which could be potentially useful for the identification and purification of this specific acyltransferase. Therefore, we have investigated the specificity of LAT from crude membranes of pig spleen toward various 1-palmitoyl-glycerophospholipids and 1-acyl-glycerophosphocholines (1-acyl-GPC). The enzyme showed the highest specificity toward 1-acyl-GPC and was able to distinguish between the acyl-chain length of the 1-acyl group within the 1-acyl-GPC molecule. We found preferential reactivity in the order C10:0 < C12:0
ISSN:0003-9861
1096-0384
DOI:10.1006/abbi.1997.0560