title: Divergent evolution in enolase superfamily: strategies for assigning functions.
abstract: Nature's strategies for evolving catalytic functions can be deciphered from the information contained in the rapidly expanding protein sequence databases. However, the functions of many proteins in the protein sequence and structure databases are either uncertain (too divergent to assign function based on homology) or unknown (no homologs), thereby limiting the utility of the databases. The mechanistically diverse enolase superfamily is a paradigm for understanding the structural bases for evolution of enzymatic function. We describe strategies for assigning functions to members of the enolase superfamily that should be applicable to other superfamilies.
authors: Departments of Biochemistry and Chemistry and The Institute for Genomic Biology, University of Illinois, Urbana, Illinois 61801. Electronic address: j-gerlt@uiuc.edu.
authors: John A
authors: JA
authors: Gerlt
authors: Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, California, 94143.
authors: Patricia C
authors: PC
authors: Babbitt
authors: Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco, California 94143.
authors: Matthew P
authors: MP
authors: Jacobson
authors: Department of Biochemistry, Albert Einstein College of Medicine, Yeshiva University, Bronx, New York 10461.
authors: Steven C
authors: SC
authors: Almo
mesh_terms: D019295:Computational Biology / Q000379:methods*; D004353:Drug Evaluation, Preclinical; D019143:Evolution, Molecular; D006801:Humans; D010751:Phosphopyruvate Hydratase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D054852:Small Molecule Libraries / Q000378:metabolism; D013329:Structure-Activity Relationship
chemical_list: D054852:Small Molecule Libraries; D010751:Phosphopyruvate Hydratase