A common structure of substrate shared by lignostilbenedioxygenase isozymes from Sphingomonas paucimobilis TMY1009

Biosci Biotechnol Biochem. 2003 Jun;67(6):1394-6. doi: 10.1271/bbb.67.1394.

Abstract

A common structure of substrates of lignostilbenedioxygenases was investigated using synthesized stilbenes. Cell-free extracts of Sphingomonas paucimobilis TMY1009 degraded only trans-4-hydroxystilbene and trans-4-hydroxy-3-methoxystilbene. Other stilbenes that had no 4-hydroxyl group and had a cis structure were not substrates for lignostilbenedioxygenases. These results indicate that a 4-hydroxyl group and trans-structure is necessary for the common structure for substrates of lignostilbenedioxygenases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Extracts
  • Chromatography, High Pressure Liquid
  • Dioxygenases*
  • Isoenzymes / chemistry*
  • Isoenzymes / metabolism
  • Ligands
  • Oxygenases / chemistry*
  • Oxygenases / metabolism
  • Sphingomonas / enzymology*
  • Stereoisomerism
  • Stilbenes / chemistry
  • Stilbenes / metabolism
  • Structure-Activity Relationship
  • Substrate Specificity

Substances

  • Cell Extracts
  • Isoenzymes
  • Ligands
  • Stilbenes
  • 4-hydroxystilbene
  • Oxygenases
  • Dioxygenases
  • lignostilbene-alpha,beta-dioxygenase