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Probing conserved amino acids in phospholipase D (Brassica oleracea var. capitata) for their importance in hydrolysis and transphosphatidylation activity.

Protein engineering, design & selection : PEDS - 1 Oct 2006

Lerchner Alexandra, Mansfeld Johanna, Kuppe Konstantin, Ulbrich-Hofmann Renate

Abstract excerpt

In addition to hydrolysis of glycerophospholipids, phospholipases D (PLDs) catalyze the head group exchange. The molecular basis of this transphosphatidylation potential, which strongly varies for PLDs from different sources, is unknown hitherto. Recently, the genes of two PLD isoenzymes from white cabbage have been sequenced and expressed in Escherchia coli, yielding the basis for mutational studies. In the...

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Identifiers

PMID: 16845127
DOI: 10.1093/protein/gzl028

Genes

PLD2

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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