Mowbray, Sherry
- Department of Molecular Biosciences, Swedish University of Agricultural Sciences
Research article2004Peer reviewedOpen access
Henriksson, LM; Johansson, P; Unge, T; Mowbray, SL
Peptidyl-prolyl cis-trans isomerases (EC 5.2.1.8) catalyse the interconversion of cis and trans peptide bonds and are therefore considered to be important for protein folding. They are also thought to participate in processes such as signalling, cell surface recognition, chaperoning and heat-shock response. Here we report the soluble expression of recombinant Mycobacterium tuberculosis peptidyl-prolyl cis-trans isomerase PpiA in Escherichia coli, together with an investigation of its structure and biochemical properties. The protein was shown to be active in a spectrophotometric assay, with an estimated k(cat)/K-m of 2.0 x 10(6)
European Journal of Biochemistry
2004, volume: 271, number: 20, pages: 4107-4113
Publisher: BLACKWELL PUBLISHING LTD
https://res.slu.se/id/publ/4824