Crystallization and properties of aromatic amine dehydrogenase from Pseudomonas sp

Arch Biochem Biophys. 1983 Jan;220(1):253-62. doi: 10.1016/0003-9861(83)90408-3.

Abstract

An amine dehydrogenase was purified to homogeneity from an extract of a bacterium of the genus Pseudomonas grown in a medium containing beta-phenylethylamine as a sole carbon source and obtained in a crystalline form with about 100-fold purification. The purified enzyme catalyzed the oxidative deamination of various aromatic amines as well as some aliphatic amines to a lesser extent. An artificial electron acceptor such as phenazine methosulfate was required for the catalysis. The molecular weight determined by sedimentation equilibrium was 103,000 and the molecule seemed to be composed of two pairs of two nonidentical subunits (Mr 46,000 and 8000). The enzyme had a dull yellow-green color with an absorption maximum at 445 nm and this chromophore appeared to be involved in the catalytic action of the enzyme.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Catalysis
  • Chemical Phenomena
  • Chemistry
  • Crystallization
  • Kinetics
  • Molecular Weight
  • Oxidoreductases Acting on CH-NH Group Donors / isolation & purification*
  • Oxidoreductases Acting on CH-NH Group Donors / metabolism
  • Pseudomonas / enzymology*

Substances

  • Amino Acids
  • Oxidoreductases Acting on CH-NH Group Donors
  • aromatic amine dehydrogenase