Abstract
Corynebacterium glutamicum assimilated phenol, benzoate, 4-hydroxybenzoate p-cresol and 3,4-dihydroxybenzoate. Ring cleavage was by catechol 1,2-dioxygenase when phenol or benzoate was used and by protocatechuate 3,4-dioxygenase when the others were used as substrate. The locus ncg12319 of its genome was cloned and expressed in Escherichia coli. Enzyme assays showed that ncg12319 encodes a catechol 1,2-dioxygenase. This catechol 1,2-dioxygenase was purified and accepted catechol, 3-, or 4-methylcatechols, but not chlorinated catechols, as substrates. The optimal temperature and pH for catechol cleavage catalyzed by the enzyme were 30 °C and 9, respectively, and the K m and V max were determined to be 4.24 μmol l−1 and 3.7 μmol l−1 min−1 mg−1 protein, respectively.
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Liu, XH.S.ZP., Liu, SJ. Functional identification of the gene locus (ncg12319 and characterization of catechol 1,2-dioxygenase in Corynebacterium glutamicum . Biotechnology Letters 26, 575–580 (2004). https://doi.org/10.1023/B:BILE.0000021958.86258.08
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DOI: https://doi.org/10.1023/B:BILE.0000021958.86258.08