Summary: The gene encoding cyclohexadienyl dehydratase from , designated , was cloned in and sequenced recently by Zhao . ( 267, 2487–2493, 1992). N-Terminal sequencing of the purified cyclohexadienyl dehydratase yielded a run of 11 residues which matched perfectly with the deduced amino acid residues 26–36. This showed that a 25 residue peptide was cleaved from the N-terminus of a preprotein formed in . The amino acid composition of the 25 residue peptide was typical of signal sequences for periplasmic proteins. Most or all of the cyclohexadienyl dehydratase was released from and carrying the gene following spheroplast formation, osmotic shock or chloroform treatment. The location of the enzyme in the periplasm of both and was confirmed by Western blotting analysis using antibody prepared against PheC. Electron microscopy using immunogold labelling showed an apparent localization of cyclohexadienyl dehydratase at the polar regions of the periplasmic space in .


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