D-proline dehydrogenase
| D-proline dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.5.99.13 | ||||||||
| 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-proline dehydrogenase (EC 1.5.99.13, D-Pro DH, D-Pro dehydrogenase, dye-linked D-proline dehydrogenase) is an enzyme with systematic name D-proline:acceptor oxidoreductase.[1][2] This enzyme catalyses the following chemical reaction
- D-proline + acceptor 1-pyrroline-2-carboxylate + reduced acceptor
This enzyme is a flavoprotein (FAD).
References
- ↑ Tani, Y.; Tanaka, K.; Yabutani, T.; Mishima, Y.; Sakuraba, H.; Ohshima, T.; Motonaka, J. (2008). "Development of a D-amino acids electrochemical sensor based on immobilization of thermostable D-proline dehydrogenase within agar gel membrane". Anal. Chim. Acta. 619 (2): 215–220. doi:10.1016/j.aca.2008.04.063. PMID 18558115.
- ↑ Satomura, T.; Kawakami, R.; Sakuraba, H.; Ohshima, T. (2002). "Dye-linked D-proline dehydrogenase from hyperthermophilic archaeon Pyrobaculum islandicum is a novel FAD-dependent amino acid dehydrogenase". J. Biol. Chem. 277 (15): 12861–12867. doi:10.1074/jbc.M112272200. PMID 11823469.
External links
- D-proline dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH)
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