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Dihydroorotate dehydrogenase - Wikipedia, the free encyclopedia

Dihydroorotate dehydrogenase

From Wikipedia, the free encyclopedia

Dihydroorotate dehydrogenase fom E. coli
Identifiers
Symbol DHO_dh
Pfam PF01180
InterPro IPR001295
PROSITE PDOC00708
SCOP 1dor
OPM family 59
OPM protein 1uum
Available PDB structures:

1f76A:47-336 1uumA:77-377 1uuoA:77-377 1d3gA:77-377 1d3hA:77-377 2b0mA:77-377 1lx3A:49-334 1tv5A:207-550 1ep3A:6-291 1ep2A:6-291 1ep1A:6-291 1h7xA:532-838 1gteA:532-838 1h7wB:532-838 1gthA:532-838 1gt8A:532-838 1jueA:1-293 1jrbA:1-293 1jubA:1-293 1jqxA:1-293 1jrcB:1-293 2dorA:1-293 1nfcA:1-293 1jqvB:1-293 1ovdB:1-293 1dorA:1-293 2b4gD:2-294


Human dihydroorotate dehydrogenase
Identifiers
Symbol DHODH
Entrez 1723
HUGO 2867
OMIM 126064
PDB 1D3G
RefSeq NM_001361
UniProt Q02127
Other data
EC number 1.3.3.1
Locus Chr. 16 q22

Dihydroorotate dehydrogenase (EC 1.3.3.1) is an enzyme that catalyzes the fourth step in the de novo biosynthesis of pyrimidine. It converts dihydroorotate to orotate:

Dihydroorotate dehydrogenase is a ubiquitous FAD flavoprotein. In bacteria (gene pyrD), it is located on the inner side of the cytosolic membrane. In some yeasts, such as in Saccharomyces cerevisiae (gene URA1), it is a cytosolic protein while in other eukaryotes it is found in the mitochondria[1].

Contents

[edit] Human proteins containing this domain

DHODH; DPYD;

[edit] References

  1. ^ Lacroute F, Thomas D, Nagy M (1992). "Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts". Proc. Natl. Acad. Sci. U.S.A. 89 (19): 8966–8970. doi:10.1073/pnas.89.19.8966. PMID 1409592. 

[edit] Further reading

  • [1]. The crystal structure of Lactococcus lactis dihydroorotate dehydrogenase A complexed with the enzyme reaction product throws light on its enzymatic function. Rowland P, Bjornberg O, Nielsen FS, Jensen KF, Larsen S; Protein Sci 1998;7:1269-1279. PubMed

[edit] External links

This article includes text from the public domain Pfam and InterPro IPR001295


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