EC 2.2.1.7 - 1-deoxy-D-xylulose-5-phosphate synthase

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IntEnz Enzyme Nomenclature
EC 2.2.1.7

Names

Accepted name:
1-deoxy-D-xylulose-5-phosphate synthase
Other names:
1-deoxy-D-xylulose-5-phosphate pyruvate-lyase (carboxylating)
DXP-synthase
1-deoxyxylulose-5-phosphate synthase
Systematic name:
pyruvate:D-glyceraldehyde-3-phosphate acetaldehydetransferase (decarboxylating)

Reaction

Cofactor

Comments:

Requires thiamine diphosphate. The enzyme forms part of an alternative nonmevalonate pathway for terpenoid biosynthesis.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00635
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008661
UniProtKB/Swiss-Prot: (523) [show] [UniProt]

References

  1. Sprenger, G.A., Schörken, U., Weigert, T., Grolle, S., deGraaf, A.A., Taylor, S.V., Begley,
    Identification of a thiamin-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor to isoprenoids, thiamin, and pyridoxol.
    Proc. Natl. Acad. Sci. USA 94 : 12857-12862 (1997). [PMID: 9371765]
  2. Kuzuyama, T., Takagi, M., Takahashi, S. and Seto, H.
    Cloning and characterization of 1-deoxy-D-xylulose 5-phosphate synthase from Streptomyces sp. strain CL190, which uses both the mevalonate and nonmevalonate pathways for isopentenyl diphosphate biosynthesis.
    J. Bacteriol. 182 : 891-897 (2000). [PMID: 10648511]

[EC 2.2.1.7 created 2001 as EC 4.1.3.37, transferred 2002 to EC 2.2.1.7]