Receptor

Enzyme

Dehydrogenase

Bacteria

Biology

Molecular biology

Incubation

Chemistry

Glutamate dehydrogenase

Lactate dehydrogenase

Extracellular

NAD+ kinase

Genetics

Biochemistry

Glutamate receptor

Intracellular

FEMS Microbiology Letters

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.

NAD-dependent glutamate dehydrogenase from<i>Pseudomonas aeruginosa</i>is a membrane-bound enzyme

NAD-dependent glutamate dehydrogenase fromPseudomonas aeruginosais a membrane-bound enzyme