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 p...

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Bibliographic Details
Published in:FEMS microbiology letters 1992-01, Vol.90 (2), p.205-210
Main Authors: Joannou, C.L., Brown, P.R.
Format: Article
Language:English
Subjects:
Bacterial Proteins - analysis
Bacterial Proteins - metabolism
Bacteriology
Biological and medical sciences
Cell Membrane - enzymology
Cell Membrane - metabolism
Cell Membrane - microbiology
cytoplasmic membranes
Deamination
Fundamental and applied biological sciences. Psychology
glutamate dehydrogenase (NAD(P) super(+))
Glutamate Dehydrogenase (NADP+)
Glutamate Dehydrogenase - analysis
Glutamate Dehydrogenase - metabolism
Glutamate dehydrogenase, NAD‐dependent
Membrane Proteins - analysis
Membrane Proteins - metabolism
Membrane‐bound NAD‐GDH
Metabolism. Enzymes
Microbiology
Pseudomonas aeruginosa
Pseudomonas aeruginosa - enzymology
Pseudomonas aeruginosa - metabolism
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Summary: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.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1992.tb05153.x