Dihydroorotate Dehydrogenase Protein, Human (His)

Dihydroorotate dehydrogenase is a key enzyme that utilizes quinones as electron acceptors to catalyze the key conversion of dihydroorotate to orotic acid. This enzyme activity is essential for the de novo biosynthesis of UMP (uridine monophosphate), an essential component of nucleotide metabolism. Dihydroorotate Dehydrogenase Protein, Human (His) is the recombinant human-derived Dihydroorotate Dehydrogenase protein, expressed by E. coli , with N-His labeled tag. The total length of Dihydroorotate Dehydrogenase Protein, Human (His) is 365 a.a., with molecular weight of ~41 kDa.

Dihydroorotate dehydrogenase (DHODH) is a pivotal enzyme that plays a crucial role in the de novo biosynthesis of UMP (uridine monophosphate). Its catalytic function involves the conversion of dihydroorotate to orotate, utilizing a quinone as an electron acceptor. This enzymatic activity is essential for the biosynthesis of UMP, a key component of RNA and DNA. As a critical player in pyrimidine biosynthesis, DHODH contributes to the generation of nucleotides required for cellular processes such as DNA replication and RNA synthesis. The involvement of DHODH in the de novo pathway underscores its significance in maintaining the cellular pool of pyrimidine nucleotides, making it an essential enzyme for various biological processes (adapted from the provided passage).

Human

E. coli

N-His

Q02127 (T31-R395)

1723  [NCBI]

45.1kDa

Greater than 90% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.