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The dihydroorotate dehydrogenases: Past and present
Archives of Biochemistry and Biophysics, 2017The flavoenzyme dihydroorotate dehydrogenase catalyzes the stereoselective oxidation of (S)-dihydroorotate to orotate in the fourth of the six conserved enzymatic reactions involved in the de novo pyrimidine biosynthetic pathway. Inhibition of pyrimidine metabolism by selectively targeting DHODHs has been exploited in the development of new therapies ...
Renata A.G. Reis +4 more
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Hydrogen Bonding Pathways in Human Dihydroorotate Dehydrogenase
The Journal of Physical Chemistry B, 2006Dihydroorotate dehydrogenase (DHOD) catalyzes the only redox reaction in the pathway for pyrimidine biosynthesis. In this reaction, a proton is transferred from a carbon atom of the substrate to a serine residue, and a hydride is transferred from another carbon atom of the substrate to a cofactor.
Yolanda A, Small +3 more
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INTERACTION OF DIHYDROOROTATE DEHYDROGENASE WITH LIGHT*
Photochemistry and Photobiology, 1967Abstract— Several flavoproteins are known to undergo photoactivated reduction by EDTA. However, the effects of visible light on the non‐heme iron containing flavoproteins have not been characterized previously. Dihydroorotate dehydrogenase was studied as an example of this class of enzymes.
Richard W. Miller, Carolyn T. Kerr
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Selective inhibition of bacterial dihydroorotate dehydrogenases by thiadiazolidinediones
Biochemical Pharmacology, 2000Dihydroorotate dehydrogenase is a critical enzyme of de novo pyrimidine biosynthesis in prokaryotic and eukaryotic cells. Differences in the primary structure of the enzymes from Gram-positive and -negative bacteria and from mammals indicate significant structural divergence among these enzymes.
J, Marcinkeviciene +14 more
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On Dihydroorotate Dehydrogenases and Their Inhibitors and Uses
Journal of Medicinal Chemistry, 2013Proper nucleosides availability is crucial for the proliferation of living entities (eukaryotic cells, parasites, bacteria, and virus). Accordingly, the uses of inhibitors of the de novo nucleosides biosynthetic pathways have been investigated in the past.
Munier-Lehmann, Hélène +3 more
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[9] Dihydroorotate dehydrogenase (Neurospora)
1978Publisher Summary This chapter discusses the purification procedure of the enzyme dihydroorotate dehydrogenase from Neurospora . The enzyme is a lipoprotein that contains solvent-extractable (25°C) fatty acids, phospholipids, and Triton X-100 even after extensive purification. Dihydroorotate dehydrogenase may be obtained in a form that migrates as a
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Human spleen dihydroorotate dehydrogenase: Properties and partial purification
Biochemical Medicine, 1985Human spleen dihydroorotate dehydrogenase is associated with the mitochondrial membrane and is linked to the respiratory chain via ubiquinone. The enzyme activity was unaffected by pyridine nucleotides. The product of the reaction, orotate, was a potent inhibitor.
A M, Gero, W J, O'Sullivan
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Targeting vulnerability in tumor therapy: Dihydroorotate dehydrogenase
Life SciencesDihydroorotate dehydrogenase (DHODH) is a key enzyme in the de novo pyrimidine biosynthetic pathway and a recognized therapeutic target in various diseases. In oncology research, DHODH has gained increasing importance and become a hot target for various tumor therapy studies.
Fu, Lin +5 more
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