Delineation of the Caffeine C-8 Oxidation Pathway in Pseudomonas sp. Strain CBB1 via Characterization of a New Trimethyluric Acid Monooxygenase and Genes Involved in Trimethyluric Acid Metabolism

Journal of Bacteriology
2012.0

Abstract

<jats:title>ABSTRACT</jats:title> <jats:p> The molecular basis of the ability of bacteria to live on caffeine via the C-8 oxidation pathway is unknown. The first step of this pathway, caffeine to trimethyluric acid (TMU), has been attributed to poorly characterized caffeine oxidases and a novel quinone-dependent caffeine dehydrogenase. Here, we report the detailed characterization of the second enzyme, a novel NADH-dependent trimethyluric acid monooxygenase (TmuM), a flavoprotein that catalyzes the conversion of TMU to 1,3,7-trimethyl-5-hydroxyisourate (TM-HIU). This product spontaneously decomposes to racemic 3,6,8-trimethylallantoin (TMA). TmuM prefers trimethyluric acids and, to a lesser extent, dimethyluric acids as substrates, but it exhibits no activity on uric acid. Homology models of TmuM against uric acid oxidase HpxO (which catalyzes uric acid to 5-hydroxyisourate) reveal a much bigger and hydrophobic cavity to accommodate the larger substrates. Genes involved in the caffeine C-8 oxidation pathway are located in a 25.2-kb genomic DNA fragment of CBB1, including <jats:italic>cdhABC</jats:italic> (coding for caffeine dehydrogenase) and <jats:italic>tmuM</jats:italic> (coding for TmuM). Comparison of this gene cluster to the uric acid-metabolizing gene cluster and pathway of <jats:named-content xmlns:xlink="http://www.w3.org/1999/xlink" content-type="genus-species" xlink:type="simple">Klebsiella pneumoniae</jats:named-content> revealed two major open reading frames coding for the conversion of TM-HIU to <jats:italic>S</jats:italic> -(+)-trimethylallantoin [ <jats:italic>S</jats:italic> -(+)-TMA]. The first one, designated <jats:italic>tmuH</jats:italic> , codes for a putative TM-HIU hydrolase, which catalyzes the conversion of TM-HIU to 3,6,8-trimethyl-2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (TM-OHCU). The second one, designated <jats:italic>tmuD</jats:italic> , codes for a putative TM-OHCU decarboxylase which catalyzes the conversion of TM-OHCU to <jats:italic>S</jats:italic> -(+)-TMA. Based on a combination of enzymology and gene-analysis, a new degradative pathway for caffeine has been proposed via TMU, TM-HIU, TM-OHCU to <jats:italic>S</jats:italic> -(+)-TMA.

Knowledge Graph

Similar Paper

Delineation of the Caffeine C-8 Oxidation Pathway in Pseudomonas sp. Strain CBB1 via Characterization of a New Trimethyluric Acid Monooxygenase and Genes Involved in Trimethyluric Acid Metabolism
Journal of Bacteriology 2012.0
Purine metabolism and the biosynthesis of caffeine in maté leaves
Phytochemistry 1993.0
Elucidation of the trigonelline degradation pathway reveals previously undescribed enzymes and metabolites
Proceedings of the National Academy of Sciences 2018.0
Theacrine (1,3,7,9-tetramethyluric acid) synthesis in leaves of a Chinese tea, kucha (Camellia assamica var. kucha)
Phytochemistry 2002.0
Extractionless method for the simultaneous high-performance liquid chromatographic determination of urinary caffeine metabolites for N-acetyltransferase 2, cytochrome P450 1A2 and xanthine oxidase activity assessment
Journal of Chromatography B: Biomedical Sciences and Applications 2001.0
Characterization of <i>TrdL</i> as a 10-Hydroxy Dehydrogenase and Generation of New Analogues from a Tirandamycin Biosynthetic Pathway
Organic Letters 2011.0
Transformation of Isopropylamine to <scp>l</scp> -Alaninol by <i>Pseudomonas</i> sp. Strain KIE171 Involves <i>N</i> -Glutamylated Intermediates
Applied and Environmental Microbiology 2002.0
Molecular Mechanism of Nicotine Degradation by a Newly Isolated Strain, Ochrobactrum sp. Strain SJY1
Applied and Environmental Microbiology 2015.0
Purification and Characterization of a Monooxygenase Involved in the Biosynthetic Pathway of the Antitumor Drug Mithramycin
Journal of Bacteriology 2003.0
Genome Mining of the Biosynthetic Gene Cluster of the Polyene Macrolide Antibiotic Tetramycin and Characterization of a P450 Monooxygenase Involved in the Hydroxylation of the Tetramycin B Polyol Segment
ChemBioChem 2012.0