Two different enzymes are primarily responsible for retinoic acid synthesis in rabbit liver cytosol

Biochem Biophys Res Commun. 1994 Dec 15;205(2):1278-83. doi: 10.1006/bbrc.1994.2803.


Retinoic acid biosynthesis in rabbit liver was catalyzed by cytosolic NAD(+)-dependent dehydrogenase and oxygen-dependent oxidase, with an activity ratio of 59% and 41% in the presence of 2 mM dithiothreitol under aerobic conditions. The two enzymes could be well separated by fractionation involving ammonium sulfate precipitation. Purification of the enzymes indicated that the oxygen-dependent enzyme was a flavoenzyme, retinal oxidase (EC, composed of two 135 kDa subunits; and the NAD(+)-dependent enzyme was a basic pI retinal dehydrogenase composed of four 55-kDa subunits. A high concentration (1-2 mM) of DTT was required to stabilize the activity of retinal dehydrogenase during the purification procedures and storage, but inhibited the activity of retinal oxidase by 13-38%. The physiological roles of the two retinoic acid synthases in liver cytosol were discussed.

Publication types

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

MeSH terms

  • Aerobiosis
  • Aldehyde Oxidoreductases / chemistry
  • Aldehyde Oxidoreductases / isolation & purification
  • Aldehyde Oxidoreductases / metabolism*
  • Anaerobiosis
  • Animals
  • Chromatography, High Pressure Liquid
  • Cytochrome P-450 Enzyme System / isolation & purification
  • Cytochrome P-450 Enzyme System / metabolism*
  • Cytosol / enzymology
  • Kinetics
  • Liver / enzymology*
  • Macromolecular Substances
  • Molecular Weight
  • Oxygenases / isolation & purification
  • Oxygenases / metabolism*
  • Rabbits
  • Retinal Dehydrogenase
  • Retinaldehyde / metabolism
  • Spectrophotometry
  • Tretinoin / metabolism*


  • Macromolecular Substances
  • Tretinoin
  • Cytochrome P-450 Enzyme System
  • Oxygenases
  • Aldehyde Oxidoreductases
  • Retinal Dehydrogenase
  • Retinaldehyde