title: Purification and characterization of a 4-hydroxybenzoate decarboxylase from Chlamydophila pneumoniae AR39.
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 degrees 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 Mg(2+), Fe(2+), Mn(2+), and Ca(2+) but not by Cu(2+) or Zn(2+). The enzyme also slowly catalyzed the reverse reaction, which was phenol carboxylation.
authors.affiliation: College of Life Sciences and Technology, Shanghai Jiaotong University, 800 Dong-Chuan Road, Shanghai, 200240, China. jianhuaLiudl@sjtu.edu.cn
authors.forename: J
authors.initials: J
authors.lastname: Liu
authors.forename: X
authors.initials: X
authors.lastname: Zhang
authors.forename: S
authors.initials: S
authors.lastname: Zhou
authors.forename: P
authors.initials: P
authors.lastname: Tao
authors.forename: J
authors.initials: J
authors.lastname: Liu
mesh_terms: D000595:Amino Acid Sequence; D002262:Carboxy-Lyases / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D016993:Chlamydophila pneumoniae / Q000201:enzymology* / Q000235:genetics; D004795:Enzyme Stability; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D010226:Parabens / Q000378:metabolism*; D016415:Sequence Alignment; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D010226:Parabens; D002262:Carboxy-Lyases; C038193:4-hydroxybenzoic acid