Abstract
The maleylacetate reductase from Pseudomonas sp. strain B13 functioning in the modified ortho pathway was purified and digested with trypsin. The polypeptides separated by high-performance liquid chromatography were sequenced. Alignments with the polypeptides predicted from the tfdF and tcbF genes located on plasmids pJP4 of the 2,4-dichlorophenoxyacetate-degrading Alcaligenes eutrophus JMP134 and pP51 of the 1,2,4-trichlorobenzene-degrading Pseudomonas sp. strain P51 as well as polypeptides predicted from the tftE gene located on the chromosome of the 2,4,5-trichlorophenoxyacetate-degrading Burkholderia cepacia AC1100 were obtained. In addition, the deduced protein sequence encoded by the nucleotide sequence downstream of clcD on plasmid pAC27 of the 3-chlorobenzoate-degrading Pseudomonas putida AC866 was tested for homology. Significant sequence similarities with the polypeptides encoded by the tfdF, tcbF, and tftE genes as well as the nucleotide sequence downstream of the clcD gene gave evidence that these genes might encode maleylacetate reductases. A NAD-binding motif in a beta alpha beta-element was detected.
MeSH Terms
2,4-Dichlorophenoxyacetic Acid/metabolism
Amino Acid Sequence
Biodegradation, Environmental
Chlorobenzenes/metabolism
Chlorobenzoates/metabolism
Dioxygenases
Genes, Bacterial/genetics
Molecular Sequence Data
Operon/genetics
Oxidoreductases/chemistry,genetics,metabolism
Oxidoreductases Acting on CH-CH Group Donors
Oxygenases/metabolism
Peptide Fragments/chemistry
Pseudomonas/enzymology,genetics,metabolism
Sequence Analysis
Sequence Homology, Amino Acid
Chemicals
Chlorobenzenes
Chlorobenzoates
Peptide Fragments
3-chlorobenzoic acid
1,2,4-trichlorobenzene
2,4-Dichlorophenoxyacetic Acid
4-dichlorobenzene
Oxidoreductases
Oxygenases
Dioxygenases
chlorocatechol 1,2-dioxygenase
Oxidoreductases Acting on CH-CH Group Donors
maleylacetate reductase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Kasberg T
Bergische Universität-Gesamthochschule Wuppertal, Germany.
Daubaras D L
Chakrabarty A M
Kinzelt D
Reineke W
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