Affiliation:
1. Department of Microbiology, University of Oklahoma School of Medicine, Oklahoma City, Oklahoma 73104
Abstract
A particulate
d
-amino acid dehydrogenase has been partially purified from cell free extracts of
Pseudomonas aeruginosa
grown on
dl
-valine as the source of carbon and energy. A standard assay was developed which utilized 2,6-dichlorophenol-indophenol as the electron acceptor. The
p
H optimum for enzyme activity ranged from 6.0 to 8.0, depending on the amino acid assayed. The enzyme was most active with monoamino-monocarboxylic amino acids and histidine. The Michaelis constant for
d
-phenylalanine was found to be 1.3 × 10
-3
m d
-phenylalanine. Constants could not be calculated for the other amino acids oxidized because anomalous plots of
V
as a function of
V/S
were obtained. Spectra of enzyme preparations reduced with
d
-valine or sodium hydrosulfite exhibited adsorption bands typical of the α, β, and γ bands of cytochromes as well as bleaching in the flavin region of the spectrum. When
dl
-valine was added to a medium with glycerol as the energy source,
d
-amino acid dehydrogenase was detected after the addition of valine and was produced at a rate directly proportional to the synthesis of total protein. The enzyme was formed when
d
-valine,
l
-valine, or
dl
-alanine was the source of carbon and energy, but not when glucose, glycerol, or succinate was the energy source.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
43 articles.
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