2-deoxy-D-gluconate 3-dehydrogenase
2-deoxy-D-gluconate 3-dehydrogenase (EC 1.1.1.125) is an enzyme that catalyzes the chemical reaction
- 2-deoxy-D-gluconate + NAD+ 3-dehydro-2-deoxy-D-gluconate + NADH + H+
| 2-deoxy-D-gluconate 3-dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.1.125 | ||||||||
| CAS number | 37250-54-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Thus, the two substrates of this enzyme are 2-deoxy-D-gluconate and NAD+, whereas its 3 products are 3-dehydro-2-deoxy-D-gluconate, NADH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is 2-deoxy-D-gluconate:NAD+ 3-oxidoreductase. This enzyme is also called 2-deoxygluconate dehydrogenase. This enzyme participates in pentose and glucuronate interconversions.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1X1E.
gollark: This is Haskell. I am assigning to variables.
gollark: Ah.
gollark: Good idea. Maybe somewhere cheaper.
gollark: Have you tried not living there?
gollark: ```haskelldoThing :: Expr -> (M.Map Int IVal, Int)doThing expr = evalState (go expr) 0 where go :: Expr -> State Int (M.Map Int IVal, Int) go (Int x) = do vcount <- update (+1) pure (M.singleton vcount (Lit x), vcount) go (Op o a b) = do (m1, c1) <- go a (m2, c2) <- go b let prev = M.union m1 m2 nxt <- update (+1) pure (M.insert nxt (ROp o c1 c2) prev, nxt)```NONE are safe from my Haskell code.
References
- Eichhorn MM, Cynkin MA (January 1965). "Microbial metabolism of 2-deoxyglucose; 2-deoxyglucose acid dehydrogenase". Biochemistry. 4: 159–65. doi:10.1021/bi00877a024. PMID 14285233.
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