Fig. 3

3′,5′-Cyclic nucleotide phosphodiesterase function of MrPDE. a Blocks of sequences conserved in MrPDE and several fungal PDEs. Pentagram indicates the possible catalytic amino acid residues. Identical amino acids are on a black background. b SDS-PAGE analysis and purification of MrPDE. M lane, protein marker; C lane, supernatant of E. coli BL21 (DE3) harboring control pET30a(+); S lane, supernatant of E. coli BL21 (DE3) containing pET30a(+)-mrPDE induced by IPTG; P lane, purified MrPDE protein. c Specific activity of MrPDE. The PDE activity of MrPDE was determined at 30 °C in 50 mM Tris–HCl buffer (pH 8.0) using 3′,5′-cAMP as the substrate. Results were reported as mean value of three replicates ± standard deviation