, Volume 5, Issue 3–4, pp 259–276

On the origins and functions of the enzymes of the 4-chlorobenzoate to 4-hydroxybenzoate converting pathway

  • Debra Dunaway-Mariano
  • Patricia C. Babbitt

DOI: 10.1007/BF00696464

Cite this article as:
Dunaway-Mariano, D. & Babbitt, P.C. Biodegradation (1994) 5: 259. doi:10.1007/BF00696464


This review examines the enzymes of 4-chlorobenzoate to 4-hydroxybenzoate converting pathway found in certain soil bacteria. This pathway consists of three enzymes: 4-chlorobenzoate: Coenzyme A ligase, 4-chlorobenzoyl-Coenzyme A dehalogenase and 4-hydroxybenzoyl-Coenzyme A thioesterase. Recent progress made in the cloning and expression of the pathway genes from assorted bacterial strains is described. Gene order and sequence found among these strains are compared to reveal independent enzyme recruitment strategies. Sequence alignments made between thePseudomonas sp. strain CBS3 4-chlorobenzoate pathway enzymes and structurally related proteins contained within the protein sequence data banks suggest possible origins in preexisting β-oxidation pathways. The purification and characterization of the physical and kinetic properties of the pathway enzymes are described. Where possible a comparison of these properties between like enzymes from different bacterial sources are made.

Key words

4-chlorobenzoate 4-hydroxybenzoate dehalogenase 4-chlorobenzoyl-CoA dehalogenase 4-chlorobenzoate CoA ligase 4-hydroxyl benzoyl-CoA thioesterase halogenated aromatic degradation nucleophilic aromatic substitution 

Copyright information

© Kluwer Academic Publishers 1994

Authors and Affiliations

  • Debra Dunaway-Mariano
    • 1
  • Patricia C. Babbitt
    • 2
  1. 1.Department of Chemistry and BiochemistryUniversity of MarylandCollege ParkUSA
  2. 2.Department of Pharmaceutical ChemistryUniversity of CaliforniaSan FranciscoUSA

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