Characterization of fatty acid elongase enzymes from germinating pea seeds

Phytochemistry. 1998 Aug;48(8):1295-304. doi: 10.1016/s0031-9422(97)00669-9.

Abstract

In vitro biosynthesis of radioactive arachidate and behenate was observed when microsomal fractions of germinating pea seeds were incubated with exogenous stearoyl-CoA (18:0-CoA) or arachidoyl-CA (20:0-CoA) in the presence of NADPH, [2-14C]malonyl-CoA and ATP. Characterization of parameters required for optimal stearoyl- and arachidoyl-CoA elongation revealed that, at least, two chain-length-specific elongases are necessary for very-long-chain fatty acid synthesis. Both enzymes were found to be sensitive to the group-selective reagents, p-CMB, NEM, iodoacetate, arsenite and phenylglyoxal. Subcellular fractionation studies indicated that both of these elongases were localized mainly in the endoplasmic reticulum.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyl Coenzyme A / metabolism
  • Acyl-Carrier Protein S-Malonyltransferase
  • Acyltransferases / metabolism*
  • Carbon Radioisotopes
  • Kinetics
  • Pisum sativum / enzymology*
  • Substrate Specificity
  • Sulfhydryl Reagents / pharmacology

Substances

  • Acyl Coenzyme A
  • Carbon Radioisotopes
  • Sulfhydryl Reagents
  • Acyltransferases
  • Acyl-Carrier Protein S-Malonyltransferase