| EC |
1.4.5.1 |
| Accepted name: |
D-amino acid dehydrogenase (quinone) |
| Reaction: |
a D-amino acid + H2O + a quinone = a 2-oxo carboxylate + NH3 + a quinol |
| Other name(s): |
DadA |
| Systematic name: |
D-amino acid:quinone oxidoreductase (deaminating) |
| Comments: |
An iron-sulfur flavoprotein (FAD). The enzyme from the bacterium Helicobacter pylori is highly specific for D-proline, while the enzyme from the bacterium Escherichia coli B is most active with D-alanine, D-phenylalanine and D-methionine. This enzyme may be the same as EC 1.4.99.6. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc |
| References: |
| 1. |
Olsiewski, P.J., Kaczorowski, G.J. and Walsh, C. Purification and properties of D-amino acid dehydrogenase, an inducible membrane-bound iron-sulfur flavoenzyme from Escherichia coli B. J. Biol. Chem. 255 (1980) 4487–4494. [PMID: 6102989] |
| 2. |
Tanigawa, M., Shinohara, T., Saito, M., Nishimura, K., Hasegawa, Y., Wakabayashi, S., Ishizuka, M. and Nagata, Y. D-Amino acid dehydrogenase from Helicobacter pylori NCTC 11637. Amino Acids 38 (2010) 247–255. [DOI] [PMID: 19212808] |
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| [EC 1.4.5.1 created 2010] |
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