Superoxide dismutase in Drosophila melanogaster. Mutation site difference between two electromorphs

FEBS Lett. 1985 Jan 1;179(1):115-9. doi: 10.1016/0014-5793(85)80203-9.

Abstract

Two electrophoretically distinguishable variants of superoxide dismutase (SOD) are common in natural populations of Drosophila melanogaster. We have earlier comparatively characterized these two electromorphs, SODF and SODS. By peptide mapping in high-performance liquid chromatography (HPLC), we now show that the difference between the two electromorphs is due to the replacement of Asn-96 (SODF) by Lys-96 (SODS). It is far from clear how this replacement causes the biochemical differences (in thermostability, specific activity, and others) observed between these two forms of the enzyme.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acids / analysis
  • Animals
  • Drosophila melanogaster / enzymology
  • Drosophila melanogaster / genetics*
  • Genetic Variation*
  • Isoenzymes / genetics
  • Mutation*
  • Peptide Fragments / analysis
  • Superoxide Dismutase / genetics*

Substances

  • Amino Acids
  • Isoenzymes
  • Peptide Fragments
  • Superoxide Dismutase