EC - 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase

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IntEnz Enzyme Nomenclature


Accepted name:
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase
Other names:
ADH synthase
Systematic name:
L-aspartate 4-semialdehyde:1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate methylglyoxaltransferase



The enzyme plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. The enzyme can also catalyse the cleavage of fructose-1,6-bisphosphate to glyceraldehyde-3-phosphate and dihydroxyacetone phosphate. Formerly EC 4.1.2.n5.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (12) [show] [UniProt]


  1. White, R. H.
    L-Aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii.
    Biochemistry 43 : 7618-7627 (2004). [PMID: 15182204]
  2. Samland, A. K., Wang, M., Sprenger, G. A.
    MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity.
    FEMS Microbiol. Lett. 281 : 36-41 (2008). [PMID: 18318840]
  3. Morar, M., White, R. H., Ealick, S. E.
    Structure of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, a catalyst in the archaeal pathway for the biosynthesis of aromatic amino acids.
    Biochemistry 46 : 10562-10571 (2007). [PMID: 17713928]

[EC created 2012]