NAD-dependent glutamate dehydrogenase from Pseudomonas aeruginosa is a membrane-bound enzyme.
Measurements of the deaminating activity of NAD-dependent glutamate dehydrogenase (NAD-GDH) in Pseudomonas aeruginosa strain 8602 (PAC 1) showed an initially constant rate that gave way to a 3.5-fold increased rate on prolonged incubation. Only the faster rate was observed when assay mixtures were preflushed with nitrogen or were treated with the detergent Triton X-100. Comparison of the intracellular distribution of NAD-GDH with marker enzymes showed it to be associated with the cytoplasmic membrane. The results suggest that NAD-GDH may be linked to oxygen through an electron-transport system.
Joannou
C L
CL
Division of Biomolecular Sciences, King's College London, U.K.
Brown
P R
PR
D001426:Bacterial Proteins / Q000032:analysis* / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology / Q000378:metabolism / Q000382:microbiology; D003641:Deamination; D005969:Glutamate Dehydrogenase / Q000032:analysis* / Q000378:metabolism; D018086:Glutamate Dehydrogenase (NADP+); D008565:Membrane Proteins / Q000032:analysis* / Q000378:metabolism; D011550:Pseudomonas aeruginosa / Q000201:enzymology* / Q000378:metabolism
D001426:Bacterial Proteins; D008565:Membrane Proteins; D005969:Glutamate Dehydrogenase; D018086:Glutamate Dehydrogenase (NADP+)