2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase
| 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.2.1.10 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase (EC 2.2.1.10, ADH synthase, ADHS, MJ0400 (gene)) is an enzyme with systematic name L-aspartate 4-semialdehyde:1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate methylglyoxaltransferase.[1][2][3] This enzyme catalyses the following chemical 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
The enzyme plays a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate.
References
- ^ White, R.H. (2004). "L-Aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii". Biochemistry. 43 (23): 7618–7627. doi:10.1021/bi0495127. PMID 15182204.
- ^ Samland, A.K.; Wang, M.; Sprenger, G.A. (2008). "MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity". FEMS Microbiol. Lett. 281 (1): 36–41. doi:10.1111/j.1574-6968.2008.01079.x. PMID 18318840.
- ^ Morar, M.; White, R.H.; Ealick, S.E. (2007). "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 (37): 10562–10571. doi:10.1021/bi700934v. PMID 17713928.
External links
- 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)