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An analysis of the 70kbp pEST 4002-derived pETS4011 reveals that the plasmid is homologous with the degradative and regulatory gene-encoding domains in the 2-4-dichlorophenoxyacetic acid (2-4D) degrading pJP4 gene. DNA-DNA hybridization tests reveal the location of three 2-4D degradation pathway step encoding genes. Regulatory gene tfdR occurs to the right of pEST 4011's Bam HI-B fragment.

The purification and characterization of enantiomeric monooxygenases was discussed and it was compared with 2,5-diketocamphane 1,2-monooxygenase. Pseudomonas putida ATCC 17453 showed growth in either isomer of camphor in the growth medium. The pure enzyme showed a symmetrical protein peak upon elution and gave a single protein band that migrated ahead of 2,5-diketocamphane 1,2-monooxygenase during PAGE runs. The isoelectric focusing technique gave a pI value of 5.5 for the enzyme and a value of 4.6 for 2,5-diketocamphane.

A previously described gene involved in the degradation of halogenated aliphatic hydrocarbons (hadL gene) was sequenced. The gene was within a 10 kb fragment and contained an open reading frame of 681 bp. The protein encoded by this gene was isolated and purified, and was shown to degrade 2-monochloropropionic acid to D-lactate. The protein probably exists as a tetramer with subunits of M(sub R) of 25,686. Three conserved regions were observed when compared with two L-haloalkanoic acid dehalogenases of Pseudomonas sp. strain CBS3.