Exploring local flexibility/rigidity in psychrophilic and mesophilic carbonic anhydrases.

ABSTRACT: Molecular flexibility and rigidity are required to determine the function and specificity of protein molecules. Some psychrophilic enzymes demonstrate a higher catalytic efficiency at low temperatures, compared to the efficiency demonstrated by their meso/thermophilic homologous. The emerging picture suggests that such enzymes have an improved flexibility of the structural catalytic components, whereas other protein regions far from functional sites may be even more rigid than those of their mesophilic counterparts. To gain a deeper insight in the analysis of the activity-flexibility/rigidity relationship in protein structure, psychrophilic carbonic anhydrase of the Antarctic teleost Chionodraco hamatus has been compared with carbonic anhydrase II of Bos taurus through fluorescence studies

SUBMITTER: Chiuri R 

PROVIDER: S-EPMC2717254 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature