Purification, cloning, and bacterial expression of retinol dehydratase from Spodoptera frugiperda. Academic Article uri icon

Overview

abstract

  • Anhydroretinol and 14-hydroxy-4,14-retro-retinol, retro-retinoids endogenous to both mammals and insects, act as agonist and antagonist, respectively, in controlling proliferation in lymphoblasts and other retinol-dependent cells. We describe here the identification, purification, cloning, and bacterial expression of the enzyme retinol dehydratase, which converts retinol to anhydroretinol in Spodoptera frugiperda. Retinol dehydratase has nanomolar affinity for its substrate and is, therefore, the first enzyme characterized able to utilize free retinol at physiological intracellular concentrations. The enzyme shows sequence homology to the sulfotransferases and requires 3'-phosphoadenosine 5'-phosphosulfate for activity.

publication date

  • July 5, 1996

Research

keywords

  • Hydro-Lyases
  • Spodoptera

Identity

Scopus Document Identifier

  • 0030037451

Digital Object Identifier (DOI)

  • 10.1074/jbc.271.27.16135

PubMed ID

  • 8663216

Additional Document Info

volume

  • 271

issue

  • 27