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[Research advances on the metabolic pathways and functions mediated by plant xanthine dehydrogenase].
Sheng Wu Gong Cheng Xue Bao
October 2024
College of Life Sciences, Zhejiang Normal University, Jinhua 321004, Zhejiang, China.
The xanthine dehydrogenase (XDH), a molybdenum-containing oxidoreductase belonging to the molybdenum hydroxylase flavoprotein family, has been identified in a variety of eukaryotes, bacteria, and archaea. XDH catalyzes the conversion of xanthine and hypoxanthine to uric acid, which then undergoes further reactions to form allantoin and allantoic acid. Studies have shown that XDH plays a role in various metabolic processes, including purine metabolism, nitrogen metabolism, hormone metabolism, reactive oxygen species metabolism, and responses to biotic and abiotic stresses.
View Article and Find Full Text PDFThe Drug-Drug Interaction between Erlotinib and OSI-930 Is Mediated through Aldehyde Oxidase Inhibition.
Drug Metab Dispos
August 2024
Pharmacokinetics, Dynamics, and Metabolism, Pfizer Inc., Groton, Connecticut.
The propensity for aldehyde oxidase (AO) substrates to be implicated in drug-drug interactions (DDIs) is not well understood due to the dearth of potent inhibitors that elicit in vivo inhibition of AO. Although there is only one reported instance of DDI that has been ascribed to the inhibition of AO to date, the supporting evidence for this clinical interaction is rather tenuous, and its veracity has been called into question. Our group recently reported that the epidermal growth factor receptor inhibitor erlotinib engendered potent time-dependent inhibition of AO with inactivation kinetic constants in the same order of magnitude as its free circulating plasma concentrations.
View Article and Find Full Text PDFResorcinol Hydroxylase of Azoarcus anaerobius: Molybdenum Dependence, Activity, and Heterologous Expression.
Curr Microbiol
November 2020
University of Konstanz, Fachbereich Biologie, 78457, Constance, Germany.
The obligately anaerobic, denitrifying bacterium Azoarcus anaerobius strain LuFRes1 grows with resorcinol (1,3-dihydroxybenzene) as sole carbon and energy source. Resorcinol is oxidized to hydroxyhydroquinone (1,2,4-trihydroxybenzene) by resorcinol hydroxylase (RH), an inducible membrane-bound enzyme. Sequence comparison places resorcinol hydroxylase into the group of anaerobic molybdopterin oxidoreductases and dimethyl sulfoxide reductase-like enzymes.
View Article and Find Full Text PDFBacterial steroid hydroxylases: enzyme classes, their functions and comparison of their catalytic mechanisms.
Appl Microbiol Biotechnol
October 2018
G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Oblast, 142290, Russia.
The steroid superfamily includes a wide range of compounds that are essential for living organisms of the animal and plant kingdoms. Structural modifications of steroids highly affect their biological activity. In this review, we focus on hydroxylation of steroids by bacterial hydroxylases, which take part in steroid catabolic pathways and play an important role in steroid degradation.
View Article and Find Full Text PDFA Novel Degradation Mechanism for Pyridine Derivatives in Alcaligenes faecalis JQ135.
Appl Environ Microbiol
August 2018
Key Laboratory of Agricultural Environmental Microbiology, Ministry of Agriculture, College of Life Sciences, Nanjing Agricultural University, Nanjing, China
5-Hydroxypicolinic acid (5HPA), a natural pyridine derivative, is microbially degraded in the environment. However, the physiological, biochemical, and genetic foundations of 5HPA metabolism remain unknown. In this study, an operon (), responsible for 5HPA degradation, was cloned from JQ135.
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