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Bovine brain ketimine reductase.

M Nardini1, G Ricci, L Vesci

  • 1Department of Biochemical Sciences, University of Rome, La Sapienza, Italy.

Biochimica Et Biophysica Acta
|November 23, 1988
PubMed
Summary

Researchers purified a novel bovine brain enzyme that reduces ketimines, compounds derived from sulfur-containing amino acids. This ketimine reductase is found in the cerebellum and cerebral cortices, potentially involved in biosynthesis.

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Enzymology

Background:

  • Ketimines are a newly identified class of cyclic unsaturated compounds.
  • These compounds are formed from the transamination of specific sulfur-containing amino acids.
  • The biological role and metabolic pathways involving ketimines are largely unexplored.

Purpose of the Study:

  • To purify and characterize an enzyme from bovine brain with ketimine reductase activity.
  • To investigate the kinetic and molecular properties of the purified enzyme.
  • To determine the subcellular localization and regional distribution of ketimine reductase activity in the brain.

Main Methods:

  • Purification of NAD(P)H-dependent reductase from bovine brain.
  • Enzyme activity assays using ketimines and related compounds.

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  • Determination of kinetic parameters (Km, Vmax).
  • Subcellular fractionation and Western blotting for localization studies.
  • Analysis of brain tissue homogenates for enzyme distribution.

    • Main Results:

    • A novel NAD(P)H-dependent ketimine reductase was purified from bovine brain.
    • The enzyme actively reduces ketimines derived from L-cystathionine, S-aminoethyl-L-cysteine, and L-lanthionine.
    • It also reduces delta 1-piperidine 2-carboxylate, a carbon analog of aminoethylcysteine ketimine.
    • Ketimine reductase activity is primarily found in the soluble fraction, concentrated in the cerebellum and cerebral cortices.
    • Enzymatic reduction products, cyclothionine and 1,4-thiomorpholine-3,5-dicarboxylic acid, were detected in bovine brain.

    Conclusions:

    • The purified enzyme plays a significant role in the reduction of ketimines in the brain.
    • The enzyme's localization suggests specific functions within the cerebellum and cerebral cortices.
    • The detection of reduction products supports the enzyme's involvement in the biosynthesis of cyclothionine and 1,4-thiomorpholine-3,5-dicarboxylic acid.