The Enzyme Database

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EC 2.2.1.10     
Accepted name: 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase
Reaction: L-aspartate 4-semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + 2,3-dioxopropyl phosphate
For diagram of 3-dehydroquinate biosynthesis in archaea, click here
Glossary: 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 6-deoxy-5-ketofructose 1-phosphate
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate = 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate
Other name(s): ADH synthase; ADHS; MJ0400 (gene name)
Systematic name: L-aspartate 4-semialdehyde:1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate methylglyoxaltransferase
Comments: 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 reaction of EC 4.1.2.13, fructose-bisphosphate aldolase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
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 (2004) 7618–7627. [PMID: 15182204]
2.  Samland, A.K., Wang, M. and Sprenger, G.A. MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity. FEMS Microbiol. Lett. 281 (2008) 36–41. [PMID: 18318840]
3.  Morar, M., White, R.H. and 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 (2007) 10562–10571. [PMID: 17713928]
[EC 2.2.1.10 created 2012]
 
 


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