Disease relevance of DHODH

• Dihydroorotate dehydrogenase from Clostridium oroticum was purified to apparent homogeneity and found to be a heterotetramer consisting of two alpha (32 kDa) and two beta (28 kDa) polypeptides [1].

High impact information on DHODH

• This subunit composition, coupled with known cofactor requirements and the ability to transfer electrons from L-dihydroorotate to NAD(+), defines the C. oroticum enzyme as a family 1B dihydroorotate dehydrogenase [1].
• Dihydroorotates deuteriated at both C5 and C6 have been prepared and used to probe the mechanism of the bovine liver mitochondrial dihydroorotate dehydrogenase [2].
• These findings suggest that dihydroorotate dehydrogenase may follow a nonclassical, two-site ping-pong mechanism, typical of an enzyme that contains two non-overlapping and kinetically isolated substrate binding sites [3].
• Dihydroorotate dehydrogenase w3as in the mitochondrial fraction with no evidence for a cytosolic enzyme requiring pyridine nucleotides [4].
• Dihydroorotate dehydrogenase (EC 1.3.3.1) (DHODH) carries out the fourth committed step in the pathway and may also be important for mitochondrial electron transport and oxygen radical metabolism [5].

Associations of DHODH with chemical compounds

• Mammalian respiratory chain inhibitors and ubiquinone analogues caused inhibition of the Babesia dihydroorotate dehydrogenase [6].

References