A novel caffeine dehydrogenase in Pseudomonas sp. strain CBB1 oxidizes caffeine to trimethyluric acid

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 Q0 was the preferred electron acceptor. The enzyme was specific for caffeine and theobromine and showed no activity with xanthine. Copyright © 2008, American Society for Microbiology. All Rights Reserved.