Open AccessNAD‐dependent glutamate dehydrogenase from Pseudomonas aeruginosa is a membrane‐bound enzyme
Author(s) -
Joannou C.L.,
Brown P.R.
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb05153.x
Subject(s) - nad+ kinase , glutamate dehydrogenase , biochemistry , enzyme , dehydrogenase , intracellular , incubation , chemistry , bacteria , extracellular , lactate dehydrogenase , biology , microbiology and biotechnology , glutamate receptor , receptor , genetics
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.