A thermostable manganese‐containing superoxide dismutase from pathogen Chlamydia pneumoniae

FEBS Letters

Liu, Jianhua¹  Yu, Xiaomin¹  Yu, Jing¹ 

[1] College of Life Sciences and Technology, Shanghai Jiaotong University, 1954 Hua-shan Road, Shanghai 200030, PR China

关键词: Superoxide dismutase;    Expression;    Purification;    Thermostability;    Chlamydia pneumoniae;    CpSOD;    superoxide dismutase of Chlamydia pneumoniae AR39;    PsSOD;    superoxide dismutase of Propionibacterium shermanii;    MnSOD;    manganese-containing superoxide dismutase;    PCR;    polymerase chain reaction;    IPTG;    isopropyl-1-thio-β-D-galactopyranoside;    Ni-NTA;    nickel-nitrilotriacetic acid;   

DOI  :  10.1016/S0014-5793(04)00170-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The gene CP0718 encoding a putative manganese-containing superoxide dismutase of Chlamydia pneumoniae AR39 was cloned and expressed in Escherichia coli. Characterization showed that the expressed protein with a monomeric molecular mass of 23.1 kDa had superoxide dismutase (SOD) activity and the cofactor of CpSOD was a bivalent manganese cation. It is unexpected that this enzyme was hyperthermostable, and maintained about 90% activity after incubation at 70°C for 60 min. Manganese binding residues found in the SOD sequences from different species are conserved in CpSOD. Bioinformatics analysis compared with Propionibacterium shermanii MnSOD was performed to elucidate the CpSOD hyperthermostability based on amino acid sequences.

【 授权许可】

Unknown