Lysine biosynthesis in Rhodotorula glutinis: properties of pipecolic acid oxidase

J Bacteriol. 1982 Sep;151(3):1073-7. doi: 10.1128/JB.151.3.1073-1077.1982.


Pipecolic acid oxidase from Rhodotorula glutinis, which converts pipecolic acid to alpha-aminoadipic-delta-semialdehyde, an intermediate of the biosynthetic pathway of lysine, was purified 290-fold. The enzyme from the crude extract and purified preparation exhibited a molecular weight of approximately 43,000 and was composed of a single subunit. The purified enzyme was heat labile and exhibited a pH optimum of 8.5 and an apparent Km for L-pipecolic acid of 1.67 X 10(-3) M. L-Proline acted as a competitive inhibitor for the enzyme. The enzyme was inhibited by the sulfhydryl agents p-chloromercuribenzoate and mercuric chloride. The in vitro enzyme activity required oxygen and upon oxidation of pipecolic acid, oxygen was reduced to hydrogen peroxide.

Publication types

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

MeSH terms

  • Hot Temperature
  • Hydrogen Peroxide / metabolism
  • Hydrogen-Ion Concentration
  • Kinetics
  • Lysine / biosynthesis*
  • Mitosporic Fungi / enzymology*
  • Molecular Weight
  • Oxidoreductases Acting on CH-NH Group Donors / isolation & purification
  • Oxidoreductases Acting on CH-NH Group Donors / metabolism*
  • Pipecolic Acids / metabolism*
  • Rhodotorula / enzymology*


  • Pipecolic Acids
  • Hydrogen Peroxide
  • Oxidoreductases Acting on CH-NH Group Donors
  • L-pipecolate dehydrogenase
  • pipecolic acid
  • Lysine