Can sequence determine function?
Open Access
- 1 January 2000
- journal article
- review article
- Published by Springer Nature in Genome Biology
- Vol. 1 (5) , 000-10
- https://doi.org/10.1186/gb-2000-1-5-reviews0005
Abstract
The functional annotation of proteins identified in genome sequencing projects is based on similarities to homologs in the databases. As a result of the possible strategies for divergent evolution, homologous enzymes frequently do not catalyze the same reaction, and we conclude that assignment of function from sequence information alone should be viewed with some skepticism.Keywords
This publication has 57 references indexed in Scilit:
- The Chemistry of the Reaction Determines the Invariant Amino Acids during the Evolution and Divergence of Orotidine 5′-Monophosphate DecarboxylaseJournal of Biological Chemistry, 2000
- Evolution of Enzymatic Activity in the Enolase Superfamily: Structure of o-Succinylbenzoate Synthase from Escherichia coli in Complex with Mg2+ and o-Succinylbenzoate,Biochemistry, 2000
- New Reactions in the Crotonase Superfamily: Structure of Methylmalonyl CoA Decarboxylase from Escherichia coli,Biochemistry, 2000
- No Metal Cofactor in Orotidine 5′-Monophosphate DecarboxylaseBiochemical and Biophysical Research Communications, 1999
- Evolution of Enzymatic Activities in the Enolase Superfamily: Identification of a “New” General Acid Catalyst in the Active Site of d-Galactonate Dehydratase from Escherichia coliJournal of the American Chemical Society, 1999
- Unexpected Divergence of Enzyme Function and Sequence: “N-Acylamino Acid Racemase” Is o-Succinylbenzoate SynthaseBiochemistry, 1999
- The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule 1 1Edited by D. ReesJournal of Molecular Biology, 1998
- The Complete Genome Sequence of Escherichia coli K-12Science, 1997
- A Proficient EnzymeScience, 1995
- Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: Indoleglycerolphosphate synthase from Escherichia coli refined at 2.0 Å resolutionJournal of Molecular Biology, 1992