Enzymes involved in 3,5-diaminohexanoate degradation by Brevibacterium sp

J Bacteriol. 1980 Sep;143(3):1165-70. doi: 10.1128/jb.143.3.1165-1170.1980.


Cell-free extracts of Brevibacterium sp. L5 grown on DL-erythro-3,5-diaminohexanoate were found to contain a 3-keto-5-aminohexanoate cleavage enzyme that converts 3-keto-5-aminohexanoate and acetyl-coenzyme A (CokA) to 3-aminobutyryl-CoA and acetoacetate and a deaminase that coverts L-3-aminobutyryl-CoA to crotonyl-CoA. The cleavage enzyme has been purified extensively, and some of its properties have been determined for comparison with the 3-keto-6-acetamido-hexanoate cleavage enzyme of Pseudomonas sp. B4. The deaminase has been partially purified and characterized. Both the cleavage enzyme and the deaminase are induced by growth on 3,5-diaminohexanoate. The presence of these and other accessory enzymes in Brevibacterium sp. extracts accounts for the results of earlier tracer experiments which showed that C-1 and C-2 of 3-keto-5-aminohexanoate are converted mainly to acetoacetate and acetate, whereas C-3 to C-6 are converted mainly to 3-hydroxybutyrate or its coenzyme A thiolester. The enzymes observed in extracts of Brevibacterium sp. can account for the conversion of 3,5-diaminohexanoate to acetyl-CoA.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acids, Diamino / metabolism*
  • Aminocaproates / isolation & purification
  • Aminocaproates / metabolism
  • Ammonia-Lyases / isolation & purification
  • Ammonia-Lyases / metabolism*
  • Brevibacterium / enzymology*
  • Caproates / metabolism*
  • Kinetics
  • Oxo-Acid-Lyases / isolation & purification
  • Oxo-Acid-Lyases / metabolism*
  • Substrate Specificity


  • Amino Acids, Diamino
  • Aminocaproates
  • Caproates
  • 3,5-diaminohexanoate
  • 3-keto-5-aminohexanoate cleavage enzyme
  • Oxo-Acid-Lyases
  • 3-aminobutyryl-CoA deaminase
  • Ammonia-Lyases