protein

Recombinant Human Dihydroorotate dehydrogenase (quinone), mitochondrial

MBS953466

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Dihydroorotate dehydrogenase (quinone), mitochondrial

Dihydroorotate dehydrogenase

Dihydroorotate oxidase

dihydroorotate dehydrogenase (quinone), mitochondrial; Dihydroorotate dehydrogenase (quinone), mitochondrial; dihydroorotate dehydrogenase (quinone), mitochondrial; dihydroorotate dehydrogenase (quinone); Dihydroorotate oxidase

DHODH

DHODH; DHODH; URA1; POADS; DHOdehase; DHOdehase

PYRD_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

31-395; Mitochondrial intermembrane domain

395

TGDERFYAEHLMPTLQGLLDPESAHRLAVRFTSLGLLPR
ARFQDSDMLEVRVLGHKFRNPVGIAAGFDKHGEAVDGLY
KMGFGFVEIGSVTPKPQEGNPRPRVFRLPEDQAVINRYG
FNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVNLGKNKT
SVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQG
KAELRRLLTKVLQERDGLRRVHRPAVLVKIAPDLTSQDK
EDIASVVKELGIDGLIVTNTTVSRPAGLQGALRSETGGL
SGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDAL
EKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQG
FGGVTDAIGADHRR

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Metabolism

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.

Cloning and sequencing of a human cDNA coding for dihydroorotate dehydrogenase by complementation of the corresponding yeast mutant.Minet M., Dufour M.E., Lacroute F.Gene 121:393-396(1992) Recombinant human dihydroorotate dehydrogenase expression, purification, and characterization of a catalytically functional truncated enzyme.Copeland R.A., Davis J.P., Dowling R.L., Lombardo D., Murphy K.B., Patterson T.A.Arch. Biochem. Biophys. 323:79-86(1995) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) Functional expression of a fragment of human dihydroorotate dehydrogenase by means of the baculovirus expression vector system, and kinetic investigation of the purified recombinant enzyme.Knecht W., Bergjohann U., Gonski S., Kirschbaum B., Loeffler M.Eur. J. Biochem. 240:292-301(1996) Requirements for the mitochondrial import and localization of dihydroorotate dehydrogenase.Rawls J., Knecht W., Diekert K., Lill R., Loeffler M.Eur. J. Biochem. 267:2079-2087(2000) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Structures of human dihydroorotate dehydrogenase in complex with antiproliferative agents.Liu S., Neidhardt E.A., Grossman T.H., Ocain T., Clardy J.Structure 8:25-33(2000) Dual binding mode of a novel series of DHODH inhibitors.Baumgartner R., Walloschek M., Kralik M., Gotschlich A., Tasler S., Mies J., Leban J.J. Med. Chem. 49:1239-1247(2006) Exome sequencing identifies the cause of a Mendelian disorder.Ng S.B., Buckingham K.J., Lee C., Bigham A.W., Tabor H.K., Dent K.M., Huff C.D., Shannon P.T., Jabs E.W., Nickerson D.A., Shendure J., Bamshad M.J.Nat. Genet. 42:30-35(2010)

45006951

NP_001352.2

NM_001361.4

Q02127

42.4kD

Metabolic Pathways (132956); Metabolism Pathway (1269956); Metabolism Of Nucleotides Pathway (1270133); Pyrimidine Biosynthesis Pathway (1270139); Pyrimidine Metabolism Pathway (1270138); Pyrimidine Metabolism Pathway (82946); Pyrimidine Metabolism Pathway (309); Uridine Monophosphate Biosynthesis, Glutamine (+ PRPP) = UMP Pathway (524498); Uridine Monophosphate Biosynthesis, Glutamine (+ PRPP) = UMP Pathway (468244)

The protein encoded by this gene catalyzes the fourth enzymatic step, the ubiquinone-mediated oxidation of dihydroorotate to orotate, in de novo pyrimidine biosynthesis. This protein is a mitochondrial protein located on the outer surface of the inner mitochondrial membrane. [provided by RefSeq, Jul 2008]

DHODH: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. Defects in DHODH are the cause of postaxial acrofacial dysostosis (POADS); also known as Miller syndrome. POADS is characterized by severe micrognathia, cleft lip and/or palate, hypoplasia or aplasia of the posterior elements of the limbs, coloboma of the eyelids and supernumerary nipples. POADS is a very rare disorder: only 2 multiplex families, each consisting of 2 affected siblings born to unaffected, nonconsanguineous parents, have been described among a total of around 30 reported cases. Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily. Protein type: Nucleotide Metabolism - pyrimidine; Mitochondrial; EC 1.3.5.2; Membrane protein, integral; Oxidoreductase. Chromosomal Location of Human Ortholog: 16q22. Cellular Component: cell soma; integral to membrane; mitochondrial inner membrane; mitochondrion; nucleoplasm. Molecular Function: dihydroorotate dehydrogenase activity; drug binding; FMN binding; ubiquinone binding. Biological Process: 'de novo' pyrimidine base biosynthetic process; female pregnancy; lactation; nucleobase, nucleoside and nucleotide metabolic process; positive regulation of apoptosis; pyrimidine base metabolic process; pyrimidine nucleoside biosynthetic process; response to caffeine; response to drug; response to starvation. Disease: Postaxial Acrofacial Dysostosis

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

0.05 mg (Baculovirus)

950

0.05 mg (Mammalian-Cell)

1170