| EC |
1.4.1.24 |
| Accepted name: |
3-dehydroquinate synthase II |
| Reaction: |
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + H2O + NAD+ = 3-dehydroquinate + NH3 + NADH + H+ |
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For diagram of 3-dehydroquinate biosynthesis in archaea, click here |
| Glossary: |
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate = 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate |
| Other name(s): |
DHQ synthase II; MJ1249 (gene name); aroB′ (gene name) |
| Systematic name: |
2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate:NAD+ oxidoreductase (deaminating) |
| Comments: |
The enzyme, which was isolated from the archaeon Methanocaldococcus jannaschii, plays a key role in an alternative pathway for the biosynthesis of 3-dehydroquinate (DHQ), an intermediate of the canonical pathway for the biosynthesis of aromatic amino acids. The enzyme catalyses a two-step reaction - an oxidative deamination, followed by cyclization. |
| 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. [DOI] [PMID: 15182204] |
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| [EC 1.4.1.24 created 2012] |
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