A novel caffeine dehydrogenase in Pseudomonas sp. strain CBB1 oxidizes caffeine to trimethyluric acid.
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.
Yu
Chi Li
CL
Center for Biocatalysis & Bioprocessing, The University of Iowa, Oakdale Research Park, 2501 Crosspark Road, Suite C100, Coralville, IA 52241, USA.
Kale
Yogesh
Y
Gopishetty
Sridhar
S
Louie
Tai Man
TM
Subramanian
Mani
M
D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D002110:Caffeine / Q000378:metabolism*; D010088:Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity; D013805:Theobromine / Q000378:metabolism; D014451:Ubiquinone / Q000378:metabolism; D014527:Uric Acid / Q000031:analogs & derivatives* / Q000378:metabolism; D019820:Xanthine / Q000378:metabolism
D001426:Bacterial Proteins; D014451:Ubiquinone; D019820:Xanthine; D014527:Uric Acid; D002110:Caffeine; C039222:1,3,7-trimethyluric acid; D010088:Oxidoreductases; D013805:Theobromine