EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
1.5.5.2 | 392555 |
Membrane association of proline dehydrogenase in Escherichia coli is redox dependent |
Proc. Natl. Acad. Sci. USA |
84 |
373-377 |
1987 |
Escherichia coli |
3540963 |
1.5.5.2 | 392556 |
Proline dehydrogenase from Escherichia coli K12. Reconstitution of a functional membrane association |
J. Biol. Chem. |
259 |
2656-2661 |
1984 |
Escherichia coli |
6321477 |
1.5.5.2 | 392560 |
Membrane-bound proline dehydrogenase from Escherichia coli. Solubilization, purification, and characterization |
J. Biol. Chem. |
253 |
5997-6001 |
1978 |
Escherichia coli |
355248 |
1.5.5.2 | 392565 |
Crystallization and preliminary crystallographic analysis of the proline dehydrogenase domain of the multifunctional PutA flavoprotein from Escherichia coli |
Acta Crystallogr. Sect. D |
57 |
1925-1927 |
2001 |
Escherichia coli |
11717519 |
1.5.5.2 | 392569 |
Oxidation of L-thiazolidine-4-carboxylate by L-proline dehydrogenase in Escherichia coli |
J. Gen. Microbiol. |
138 |
1593-1598 |
1992 |
Escherichia coli |
- |
1.5.5.2 | 392570 |
Purification, characterization, and application of a novel dye-linked L-proline dehydrogenase from a hyperthermophilic archaeon, Thermococcus profundus |
Appl. Environ. Microbiol. |
67 |
1470-1475 |
2001 |
Thermococcus profundus |
11282592 |
1.5.5.2 | 392571 |
Conformational change and membrane association of the PutA protein are coincident with reduction of its FAD cofactor by proline |
J. Biol. Chem. |
268 |
8972-8979 |
1993 |
Escherichia coli |
8473341 |
1.5.5.2 | 392572 |
Proline dehydrogenase activity of mungbean rhizobia and their proline prototrophs in relation to their efficacy in symbiotic association |
Indian J. Exp. Biol. |
37 |
1234-1240 |
1999 |
Vigna radiata |
- |
1.5.5.2 | 658033 |
Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors |
Biochemistry |
43 |
12539-12548 |
2004 |
Escherichia coli |
15449943 |
1.5.5.2 | 658211 |
Probing a hydrogen bond pair and the FAD redox properties in the proline dehydrogenase domain of Escherichia coli PutA |
Biochim. Biophys. Acta |
1701 |
49-59 |
2004 |
Escherichia coli |
15450175 |