D-amino acid dehydrogenase (quinone)
| D-amino acid dehydrogenase (quinone) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.4.5.1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
D-amino acid dehydrogenase (quinone) (EC 1.4.5.1, DadA) is an enzyme with systematic name D-amino acid:quinone oxidoreductase (deaminating).[1][2] This enzyme catalyses the following chemical reaction
- D-amino acid + H2O + quinone 2-oxo carboxylate + NH3 + quinol
This enzyme is iron-sulfur flavoprotein.
References
- ↑ Olsiewski, P.J.; Kaczorowski, G.J.; Walsh, C. (1980). "Purification and properties of D-amino acid dehydrogenase, an inducible membrane-bound iron-sulfur flavoenzyme from Escherichia coli B". J. Biol. Chem. 255 (10): 4487–4494. PMID 6102989.
- ↑ Tanigawa, M.; Shinohara, T.; Saito, M.; Nishimura, K.; Hasegawa, Y.; Wakabayashi, S.; Ishizuka, M.; Nagata, Y. (2010). "D: -Amino acid dehydrogenase from Helicobacter pylori NCTC 11637". Amino Acids. 38: 247–255. doi:10.1007/s00726-009-0240-0. PMID 19212808.
External links
- D-amino acid dehydrogenase (quinone) at the US National Library of Medicine Medical Subject Headings (MeSH)
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