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