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 | ||||||||
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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]
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.
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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