Current Microbiology

, Volume 12, Issue 4, pp 235–239

Phenylglyoxylate decarboxylase and phenylpyruvate decarboxylase fromAcinetobacter calcoaceticus

  • Margaret M. Barrowman
  • Charles A. Fewson
Article

DOI: 10.1007/BF01573337

Cite this article as:
Barrowman, M.M. & Fewson, C.A. Current Microbiology (1985) 12: 235. doi:10.1007/BF01573337

Abstract

Phenylglyoxylate decarboxylase and phenylpyruvate decarboxylase were both purified from strains ofAcinetobacter calcoaceticus by very similar procedures involving ion-exchange chromatography, gel filtration, and hydrophobic chromatography. The enzymes were inducer- and substrate-specific, but in general had very similar properties. Both enzymes required thiamine pyrophosphate for activity. Phenylglyoxylate decarboxylase and phenylpyruvate decarboxylase both appeared to be tetrameric, with apparent subunit Mr values of 58,000 and 56,800 respectively.

Copyright information

© Springer-Verlag 1985

Authors and Affiliations

  • Margaret M. Barrowman
    • 1
  • Charles A. Fewson
    • 2
  1. 1.Department of Experimental Pathology, School of MedicineUniversity College LondonLondonUK
  2. 2.Department of BiochemistryUniversity of GlasgowGlasgowUK