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Pseudomonas aeruginosa transhydrogenase

Hydride Transfer in NAD+- and NADP -Dependent Enzymes. The transfer of the hydride ion in redox reaction of NAD+- and NADP+-dependent enzymes can occur either to the re- or the xi-face of the pyridine ring of the coenzyme . Such stereochemistry is crucial in the characterization of these enzymes. The same enzymes from different sources can express different stereospecificities. For example, E. coli NAD(P)+ transhydrogenase expressed one form of stereospecificity whereas the Pseudomonas aeruginosa enzyme catalyzes the identical reaction with the other NAD form . [Pg.145]

Nicotinamide nucleotide transhydrogenase was originally discovered in Pseudomonas fluorescens. Part of the work done with these bacteria by Kaplan and co-workers (see 7) appeared later to have involved Pseudomonas aeruginosa. There is little doubt, however, that these two strains contain transhydrogenases that are closely related. Kaplan and co-workers (5) also demonstrated the presence of transhydrogenase in... [Pg.53]

Pseudomonas aeruginosa nitrite reductase of, 274, 275 transhydrogenase of, 53 molecular properties, 57 purification, 54, 56... [Pg.453]

Adenosine 5 -phosphate J nucleotide transhydrogenase from Pseudomonas aeruginosa ... [Pg.452]

Louie, D. D., and N. Kaplan Stereospecifity of Hydrogen Transfer Reaction of Pseudomonas aeruginosa Pyridine Nucleotide Transhydrogenase. J. Biol. Chem. 245, 5691 (1970). [Pg.522]


See other pages where Pseudomonas aeruginosa transhydrogenase is mentioned: [Pg.55]    [Pg.57]    [Pg.54]    [Pg.55]    [Pg.57]    [Pg.62]    [Pg.190]   
See also in sourсe #XX -- [ Pg.53 ]




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