Purification and properties of two succinic semialdehyde dehydrogenases from Klebsiella pneumoniae

Biochim Biophys Acta. 1989 Mar 24;990(3):225-31. doi: 10.1016/s0304-4165(89)80038-8.


Two forms of succinic semialdehyde dehydrogenase have been isolated in Klebsiella pneumoniae M5a1. The two enzymes could be separated by filtration on Sephacryl S-300 and their apparent molecular weights were approx. 275,000 and 300,000. The large enzyme is specific for NADP. The smaller enzyme, which is induced by growth on 3-hydroxyphenylacetic acid, 4-hydroxyphenylacetic acid, 3,4-dihydroxyphenylacetic acid and gamma-aminobutyrate, has been purified to 96% homogeneity by affinity chromatography. The NAD-linked succinic semialdehyde dehydrogenase was able to use NADP as cofactor. Its induction is coordinated with 3- and 4-hydroxylase, the enzymes which initiate degradation of 3- and 4-hydroxyphenylacetic acid. The NAD-linked form is also induced by exogenous succinic semialdehyde. The large enzyme is specific for NADP and has been isolated from a defective mutant which lacked the activity of the NAD-linked succinic semialdehyde dehydrogenase. Activity and stability conditions and true K m values for substrates and cosubstrates of the two enzymes were determined. Some aspects of the induction of the NAD-linked enzyme participating in the metabolism of 4-hydroxyphenylacetic and gamma-aminobutyrate were studied.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enzyme Induction
  • Hydroxybutyrate Dehydrogenase / isolation & purification*
  • Hydroxybutyrate Dehydrogenase / metabolism
  • Kinetics
  • Klebsiella pneumoniae / enzymology*
  • NAD
  • NADP


  • NAD
  • NADP
  • Hydroxybutyrate Dehydrogenase
  • 4-hydroxybutyrate dehydrogenase