protein

Recombinant Human D-2-hydroxyglutarate dehydrogenase, mitochondrial

MBS1350347

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human D-2-hydroxyglutarate dehydrogenase, mitochondrial

D-2-hydroxyglutarate dehydrogenase

D-2-hydroxyglutarate dehydrogenase, mitochondrial isoform 2; D-2-hydroxyglutarate dehydrogenase, mitochondrial; D-2-hydroxyglutarate dehydrogenase, mitochondrial; D-2-hydroxyglutarate dehydrogenase

D2HGDH

D2HGDH; D2HGDH; D2HGD; D2HGD

D2HDH_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

14-521

387

LRGAPGAAGSWGRPVGPLARRGCCSAPGTPEVPLTRERY
PVRRLPFSTVSKQDLAAFERIVPGGVVTDPEALQAPNVD
WLRTLRGCSKVLLRPRTSEEVSHILRHCHERNLAVNPQG
GNTGMVGGSVPVFDEIILSTARMNRVLSFHSVSGILVCQ
AGCVLEELSRYVEERDFIMPLDLGAKGSCHIGGNVATNA
GGLRFLRYGSLHGTVLGLEVVLADGTVLDCLTSLRKDNT
GYDLKQLFIGSEGTLGIITTV

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 oxidation of D-2-hydroxyglutarate to alpha-ketoglutarate.

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) Generation and annotation of the DNA sequences of human chromosomes 2 and 4.Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.Nature 434:724-731(2005) Identification of a dehydrogenase acting on D-2-hydroxyglutarate.Achouri Y., Noel G., Vertommen D., Rider M.H., Veiga-Da-Cunha M., van Schaftingen E.Biochem. J. 381:35-42(2004) Mutations in the D-2-hydroxyglutarate dehydrogenase gene cause D-2-hydroxyglutaric aciduria.Struys E.A., Salomons G.S., Achouri Y., van Schaftingen E., Grosso S., Craigen W.J., Verhoeven N.M., Jakobs C.Am. J. Hum. Genet. 76:358-360(2005) Mutations in phenotypically mild D-2-hydroxyglutaric aciduria.Struys E.A., Korman S.H., Salomons G.S., Darmin P.S., Achouri Y., van Schaftingen E., Verhoeven N.M., Jakobs C.Ann. Neurol. 58:626-630(2005) Phenotypic heterogeneity in the presentation of D-2-hydroxyglutaric aciduria in monozygotic twins.Misra V.K., Struys E.A., O'brien W., Salomons G.S., Glover T., Jakobs C., Innis J.W.Mol. Genet. Metab. 86:200-205(2005) D-2-Hydroxyglutaric aciduria in three patients with proven SSADH deficiency genetic coincidence or a related biochemical epiphenomenon?Struys E.A., Verhoeven N.M., Salomons G.S., Berthelot J., Vianay-Saban C., Chabrier S., Thomas J.A., Tsai A.C.-H., Gibson K.M., Jakobs C.Mol. Genet. Metab. 88:53-57(2006)

564730541

NP_001274178.1

NM_001287249.1

Q8N465

70.83kD

Interconversion Of 2-oxoglutarate And 2-hydroxyglutarate Pathway (1270126); Metabolism Pathway (1269956); Pyruvate Metabolism And Citric Acid (TCA) Cycle Pathway (1270122); The Citric Acid (TCA) Cycle And Respiratory Electron Transport Pathway (1270121)

This gene encodes D-2hydroxyglutarate dehydrogenase, a mitochondrial enzyme belonging to the FAD-binding oxidoreductase/transferase type 4 family. This enzyme, which is most active in liver and kidney but also active in heart and brain, converts D-2-hydroxyglutarate to 2-ketoglutarate. Mutations in this gene are present in D-2-hydroxyglutaric aciduria, a rare recessive neurometabolic disorder causing developmental delay, epilepsy, hypotonia, and dysmorphic features. [provided by RefSeq, Jul 2008]

D2HGDH: an oxidoreductase that act on the CH-OH group of donor with other acceptors. Catalyzes the oxidation of D-2-hydroxyglutarate (2HG) to alpha-ketoglutarate. Belongs to the FAD-binding oxidoreductase/transferase type 4 family. 2 human isoforms produced by alternative splicing. Defects in D2HGDH are the cause of D-2-hydroxyglutaric aciduria (D2HGA), a rare recessive neurometabolic disorder causing developmental delay, epilepsy, hypotonia, and dysmorphic features. Both a mild and a severe phenotype exist. The severe phenotype is homogeneous and is characterized by early infantile-onset epileptic encephalopathy and cardiomyopathy. The mild phenotype has a more variable clinical presentation. Diagnosis is based on the presence of an excess of D-2-hydroxyglutaric acid in the urine. Protein type: EC 1.1.99.-; Oxidoreductase; Mitochondrial. Chromosomal Location of Human Ortholog: 2q37.3. Cellular Component: mitochondrial matrix; mitochondrion. Molecular Function: (R)-2-hydroxyglutarate dehydrogenase activity; FAD binding. Biological Process: 2-oxoglutarate metabolic process; cellular metabolic process; cellular protein metabolic process; response to calcium ion; response to cobalt ion; response to magnesium ion; response to manganese ion; response to zinc ion. Disease: D-2-hydroxyglutaric Aciduria 1

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

1 mg (E-Coli)

1180

0.05 mg (Baculovirus)

1295