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Article

A plant acyltransferase involved in triacylglycerol biosynthesis complements an Escherichia coli sn-1-acylglycerol-3-phosphate acyltransferase mutant.

European journal of biochemistry - 15 Sept 1995

Hanke C, Wolter F P, Coleman J, Peterek G, Frentzen M

Abstract excerpt

The second acylation reaction in glycerolipid biosynthesis is catalyzed by an sn-1-acylglycerol-3-phosphate acyltransferase. The enzyme of Limnanthes douglasii involved in triacylglycerol synthesis has an unusual specificity for very long chain acyl groups in both of its substrates, namely acyl-CoA and sn-1-acylglycerol-3-phosphate, and causes the enrichment of erucoyl groups in the sn-2 position of the seed oil...

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PMID: 7588719

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A plant acyltransferase involved in triacylglycerol biosynthesis complements an Escherichia coli sn-1-acylglycerol-3-phosphate acyltransferase mutant.PMID 7588719Read ↗

Isolation and characterisation of a maize cDNA that complements a 1-acyl sn-glycerol-3-phosphate acyltransferase mutant of Escherichia coli and encodes a protein which has similarities to other acyltransferases.Semantic proximity Read ↗

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An enzyme regulating triacylglycerol composition is encoded by the ROD1 gene of Arabidopsis.Semantic proximity Read ↗

Acyl editing and headgroup exchange are the major mechanisms that direct polyunsaturated fatty acid flux into triacylglycerols.Semantic proximity Read ↗

Molecular cloning and functional expression of Perilla frutescens 3-ketoacyl-(acyl carrier protein) synthase III.Semantic proximity Read ↗

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