Abstract：
:Electrostatic interactions play a key role in enzyme catalytic function. At long range, electrostatics steer the incoming ligand/substrate to the active site, and at short distances, electrostatics provide the specific local interactions for catalysis. In cases in which electrostatics determine enzyme function, orthologs should share the electrostatic properties to maintain function. Often, electrostatic potential maps are employed to depict how conserved surface electrostatics preserve function. We expand on previous efforts to explain conservation of function, using novel electrostatic sequence and structure analyses of four enzyme families and one enzyme superfamily. We show that the spatial charge distribution is conserved within each family and superfamily. Conversely, phylogenetic analysis of key electrostatic residues provide the evolutionary origins of functionality.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Livesay DR,Jambeck P,Rojnuckarin A,Subramaniam Sdoi
10.1021/bi026918fsubject
Has Abstractpub_date
2003-04-01 00:00:00pages
3464-73issue
12eissn
0006-2960issn
1520-4995journal_volume
42pub_type
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