Functional evolution of PLP-dependent enzymes based on active-site structural similarities.

ABSTRACT: Families of distantly related proteins typically have very low sequence identity, which hinders evolutionary analysis and functional annotation. Slowly evolving features of proteins, such as an active site, are therefore valuable for annotating putative and distantly related proteins. To date, a complete evolutionary analysis of the functional relationship of an entire enzyme family based on active-site structural similarities has not yet been undertaken. Pyridoxal-5'-phosphate (PLP) dependent enzymes are primordial enzymes that diversified in the last universal ancestor. Using the comparison of protein active site structures (CPASS) software and database, we show that the active site structures of PLP-dependent enzymes can be used to infer evolutionary relationships based on functional si

SUBMITTER: Catazaro J 

PROVIDER: S-EPMC4177364 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature