DXP reductoisomerase
1-deoxy-D-xylulose 5-phosphate reductoisomerase | |||||||||
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crystal structure of dxr in complex with the substrate 1-deoxy-d-xylulose-5-phosphate | |||||||||
Identifiers | |||||||||
Symbol | DXP_reductoisom | ||||||||
Pfam | PF02670 | ||||||||
Pfam clan | CL0063 | ||||||||
InterPro | IPR013512 | ||||||||
SCOP | 1onn | ||||||||
SUPERFAMILY | 1onn | ||||||||
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1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal | |||||||||
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crystal structure of dxr in complex with the substrate 1-deoxy-d-xylulose-5-phosphate | |||||||||
Identifiers | |||||||||
Symbol | DXP_redisom_C | ||||||||
Pfam | PF08436 | ||||||||
Pfam clan | CL0063 | ||||||||
InterPro | IPR013644 | ||||||||
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DXP reductoisomerase or (1-deoxy-d-xylulose 5-phosphate reductoisomerase) is an enzyme that intraconverts 1-deoxy-D-xylulose 5-phosphate and 2-C-methyl-D-erythritol 4-phosphate.[1]
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2-C-methylerythritol 4-phosphate
It is classified under EC 1.1.1.267.
It is part of the non-mevalonate pathway, and it is inhibited by fosmidomycin.
It is normally abbreviated DXR, but it is sometimes named IspC.
This enzyme is responsible for terpenoid biosynthesis in some organisms.[1] In Arabidopsis thaliana 1-deoxy-D-xylulose 5-phosphate reductoisomerase is the first committed enzyme of the non-mevalonate pathway for isoprenoid biosynthesis. The enzyme requires Mn2+, Co2+ or Mg2+ for activity, with Mn2+ being most effective.
External links
- DXP reductoisomerase at the US National Library of Medicine Medical Subject Headings (MeSH)
References
- ↑ 1.0 1.1 Takahashi S, Kuzuyama T, Watanabe H, Seto H (August 1998). "A 1-deoxy-D-xylulose 5-phosphate reductoisomerase catalyzing the formation of 2-C-methyl-D-erythritol 4-phosphate in an alternative nonmevalonate pathway for terpenoid biosynthesis". Proc. Natl. Acad. Sci. U.S.A. 95 (17): 9879–84. doi:10.1073/pnas.95.17.9879. PMC 21430. PMID 9707569.
This article incorporates text from the public domain Pfam and InterPro IPR013512
This article incorporates text from the public domain Pfam and InterPro IPR013644
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