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
Search PMC articles PubMed articles NCBI proteins

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 ${\displaystyle \rightleftharpoons }$ 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

1. White RH (June 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): 7618–27. doi:10.1021/bi0495127. PMID 15182204.
2. Samland AK, Wang M, Sprenger GA (April 2008). "MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity". FEMS Microbiology Letters. 281 (1): 36–41. doi:10.1111/j.1574-6968.2008.01079.x. PMID 18318840.
3. Morar M, White RH, Ealick SE (September 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): 10562–71. 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)