| D-amino acid dehydrogenase (quinone) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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.
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AP Biology Lab 2: Enzyme Catalysis
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Electron transport chain
Transcription
References
- ^ Olsiewski PJ, Kaczorowski GJ, Walsh C (May 1980). "Purification and properties of D-amino acid dehydrogenase, an inducible membrane-bound iron-sulfur flavoenzyme from Escherichia coli B". The Journal of Biological Chemistry. 255 (10): 4487–94. doi:10.1016/S0021-9258(19)85517-5. PMID 6102989.
- ^ Tanigawa M, Shinohara T, Saito M, Nishimura K, Hasegawa Y, Wakabayashi S, Ishizuka M, Nagata Y (January 2010). "D-Amino acid dehydrogenase from Helicobacter pylori NCTC 11637". Amino Acids. 38 (1): 247–55. doi:10.1007/s00726-009-0240-0. PMID 19212808. S2CID 29038373.
External links
- D-amino+acid+dehydrogenase+(quinone) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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This page was last edited on 26 August 2023, at 13:41