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J. Bacteriol., Jul 1995, 3885-3889, Vol 177, No. 13
T Kasberg, DL Daubaras, AM Chakrabarty, D Kinzelt and W Reineke
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.
Copyright © 1995, American Society for Microbiology
Evidence that operons tcb, tfd, and clc encode maleylacetate reductase, the fourth enzyme of the modified ortho pathway
Bergische Universitat-Gesamthochschule Wuppertal, Germany.
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