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Results 1 - 10 of 42 > >>
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2392569 Oxidation of L-thiazolidine-4-carboxylate by L-proline dehydrogenase in Escherichia coli J. Gen. Microbiol. 138 1593-1598 1992 Escherichia coli -
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2392572 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 -
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2392560 Membrane-bound proline dehydrogenase from Escherichia coli. Solubilization, purification, and characterization J. Biol. Chem. 253 5997-6001 1978 Escherichia coli 355248
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2722591 Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli J. Biol. Chem. 267 13086-13092 1992 Escherichia coli 1618807
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2392555 Membrane association of proline dehydrogenase in Escherichia coli is redox dependent Proc. Natl. Acad. Sci. USA 84 373-377 1987 Escherichia coli 3540963
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2392556 Proline dehydrogenase from Escherichia coli K12. Reconstitution of a functional membrane association J. Biol. Chem. 259 2656-2661 1984 Escherichia coli 6321477
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2392571 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
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2392570 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
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2392565 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
Show all pathways known for 1.5.5.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.5.2659987 Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein Nat. Struct. Biol. 10 109-114 2003 Escherichia coli 12514740
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