Quinate dehydrogenase
From Wikipedia, the free encyclopedia
| quinate 5-dehydrogenase | |||||||
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| Identifiers | |||||||
| EC number | 1.1.1.24 | ||||||
| CAS number | 9028-28-8 | ||||||
| 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 / EGO | ||||||
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In enzymology, a quinate dehydrogenase (EC 1.1.1.24) is an enzyme that catalyzes the chemical reaction
- L-quinate + NAD+
3-dehydroquinate + NADH + H+
Thus, the two substrates of this enzyme are L-quinate and NAD+, whereas its 3 products are 3-dehydroquinate, 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 L-quinate:NAD+ 3-oxidoreductase. Other names in common use include quinic dehydrogenase, quinate:NAD oxidoreductase, quinate 5-dehydrogenase, and quinate:NAD+ 5-oxidoreductase. This enzyme participates in phenylalanine, tyrosine and tryptophan biosynthesis.
[edit] References
- Gamborg OL (1966). "Aromatic metabolism in plants. III. Quinate dehydrogenase from mung bean cell suspension cultures". Biochim. Biophys. Acta 128: 483–491.
- MITSUHASHI S, DAVIS BD (1954). "Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase". Biochim. Biophys. Acta. 15 (2): 268–80. doi:10.1016/0006-3002(54)90069-4. PMID 13208693.
| This EC 1.1.1 enzyme-related article is a stub. You can help Wikipedia by expanding it. |
3-dehydroquinate + NADH + H+