1.5.5.2	?	x * 40000, recombinant His-tagged enzyme, SDS-PAGE	-, 742641	
1.5.5.2	?	x * 54000, about, sequence calculation	741642	
1.5.5.2	?	x * 55000-57000, SDS-PAGE	742487	
1.5.5.2	dimer	-	-, 743635	
1.5.5.2	dimer	2 * 119000-124000, SDS-PAGE	392560	
1.5.5.2	dimer	2 * 137000, bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase, SDS-PAGE	722591	
1.5.5.2	dimer	2 * 74401, recombinant MBP-tagged enzyme, sequence calculation, 2 * 71899, recombinant enzyme mutant DELTAABC, sequence calculation	-, 743834	
1.5.5.2	dimer	domain-swapped dimer with each subunit comprising three domains: a helical dimerization arm, a 120-residue domain containing a three-helix bundle similar to that in the helix-turn-helix superfamily of DNA-binding proteins and a beta/alpha-barrel PRODH domain with a bound lactate inhibitor	659987	
1.5.5.2	heterooctamer	4 * 55300 + 4 * 42700, calculated from amino acid sequence	739932	
1.5.5.2	homodimer	2 * 37000, SDS-PAGE	724389	
1.5.5.2	additional information	homology-based three-dimensional structural modeling of JcProDH, overview	741642	
1.5.5.2	additional information	Pseudomonas putida enzyme contains 51% alpha-helics, 7% beta-strand, and 41% coils, three-dimensional homology structure modeling, overview	-, 742641	
1.5.5.2	additional information	recombinant wild-type detagged enzyme and recombinant wild-type MBP-tagged enzyme both form oligomers. Peptide mapping	-, 742162	
1.5.5.2	octamer	the enzyme is a alpha4beta4-type ProDH	-, 741732	
1.5.5.2	tetramer	alpha,beta, 2 * 50000 + 2 * 40000, SDS-PAGE	392570	
1.5.5.2	tetramer	alphabetagammadelta, 1 * 54000 + 1 * 43000 + 1 * 19000 + 1 * 8000, the beta-subunit catalyzes the dye-linked L-proline dehydrogenase reaction by itself, the alpha-subunit exhibts dye-linked NADH dehydrogenase activity, SDS-PAGE	658668	
1.5.5.2	tetramer	the enzyme is a alphabetagammadelta-type ProDH	-, 741732