A Novel Caffeine Dehydrogenase in Pseudomonas Sp. Strain CBB1 Oxidizes Caffeine to Trimethyluric Acid

J Bacteriol. 2008 Jan;190(2):772-6. doi: 10.1128/JB.01390-07. Epub 2007 Nov 2.

Abstract

A unique heterotrimeric caffeine dehydrogenase was purified from Pseudomonas sp. strain CBB1. This enzyme oxidized caffeine to trimethyluric acid stoichiometrically and hydrolytically, without producing hydrogen peroxide. The enzyme was not NAD(P)(+) dependent; coenzyme Q(0) was the preferred electron acceptor. The enzyme was specific for caffeine and theobromine and showed no activity with xanthine.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism*
  • Caffeine / metabolism*
  • Oxidoreductases / chemistry
  • Oxidoreductases / isolation & purification
  • Oxidoreductases / metabolism*
  • Pseudomonas / enzymology*
  • Substrate Specificity
  • Theobromine / metabolism
  • Ubiquinone / metabolism
  • Uric Acid / analogs & derivatives*
  • Uric Acid / metabolism
  • Xanthine / metabolism

Substances

  • Bacterial Proteins
  • Ubiquinone
  • Xanthine
  • Uric Acid
  • Caffeine
  • 1,3,7-trimethyluric acid
  • Oxidoreductases
  • Theobromine