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Purification and Characterization of a 4-Hydroxybenzoate Decarboxylase from Chlamydophila pneumoniae AR39

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Abstract

Chlamydophila pneumoniae AR39 is an obligate intracellular pathogen that causes human acute and chronic respiratory tract diseases. One protein from C. pneumoniae AR39 was assigned as 4-hydroxybenzoate decarboxylase (HBDC). Assays done with the purified oxygen-sensitive protein showed that the optimum pH and temperature were 7.5 and 30°C, respectively. The Km and Vmax obtained for 4-hydroxybenzoate were approximately 0.21 mM and 11.9 nM min−1 mg−1, respectively. During the period of 4-hydroxybenzoate decarboxylation, overall activity of the thermal-sensitive protein was 5.06 nM min−1 mg−1 protein. The 4-hydroxybenzoate decarboxylation was promoted by Mg2+, Fe2+, Mn2+, and Ca2+ but not by Cu2+ or Zn2+. The enzyme also slowly catalyzed the reverse reaction, which was phenol carboxylation.

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Authors and Affiliations

  1. College of Life Sciences and Technology, Shanghai Jiaotong University, 800 Dong-Chuan Road, Shanghai, 200240, China

    J. Liu, X. Zhang, S. Zhou & J. Liu

  2. Instrumental Analysis Center, Shanghai Jiaotong University, 1954 Hua-Shan Road, Shanghai, 200030, China

    P. Tao

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Liu, J., Zhang, X., Zhou, S. et al. Purification and Characterization of a 4-Hydroxybenzoate Decarboxylase from Chlamydophila pneumoniae AR39. Curr Microbiol 54, 102–107 (2007). https://doi.org/10.1007/s00284-006-0153-z

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