Abstract
Abstract Hydroxyproline-induced α-ketoglutaric semialdehyde dehydrogenase has been purified from a pseudomonas strain and characterized with respect to substrate specificity and other properties. After a variety of growth conditions, pseudomonas extracts also contain a constitutive dehydrogenase, which differs from the induced enzyme in sedimentation and electrophoretic behavior. Although the constitutive enzyme resembles the induced form in many kinetic respects, it is relatively more active with glutaric semialdehyde as a substrate and is tentatively assigned a role in lysine metabolism. Growth on d-glucarate induces a dehydrogenase which, in all kinetic and physical respects examined, appears identical with that induced by growth on hydroxyproline.
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