Head group specificity of phospholipase D isoenzymes from poppy seedlings (Papaver somniferum L.)

Biotechnol Lett. 2005 Feb;27(3):181-5. doi: 10.1007/s10529-004-7853-x.

Abstract

The biocatalytical potential of two new phospholipase D (PLD) isoenzymes from poppy seedlings (Papaver somniferum L.), PLD-A and PLD-B, was examined by comparing their activities in phospholipid transformation. Both enzymes showed the same ratio in rates of hydrolysis [phosphatidylcholine (PC):phosphatidylglycerol (PG):phosphatidylserine:phosphatidylinositol = 1:0.5:0.3:0.1] and were inactive towards phosphatidylethanolamine (PE). PLD-A did not catalyze head group exchange whereas PLD-B showed a high transphosphatidylation potential in the conversion of PC into PG and PE. This enzyme also catalyzed the transesterification of octadecylphosphocholine into octadecylphosphoglycerol or octadecylphosphoethanolamine.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Hydrogen-Ion Concentration
  • Hydrolysis
  • Isoenzymes / chemistry
  • Isoenzymes / metabolism
  • Molecular Structure
  • Papaver / enzymology*
  • Phosphatidylcholines / metabolism
  • Phosphatidylglycerols / metabolism
  • Phosphatidylinositols / metabolism
  • Phosphatidylserines / metabolism
  • Phospholipase D / chemistry
  • Phospholipase D / metabolism*
  • Phospholipids / metabolism
  • Seedlings / enzymology
  • Substrate Specificity

Substances

  • Isoenzymes
  • Phosphatidylcholines
  • Phosphatidylglycerols
  • Phosphatidylinositols
  • Phosphatidylserines
  • Phospholipids
  • Phospholipase D