Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity
- 1 January 2005
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 433 (1) , 59-70
- https://doi.org/10.1016/j.abb.2004.07.034
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- The structure of Pseudomonas P51 Cl‐muconate lactonizing enzyme: Co‐evolution of structure and dynamics with the dehalogenation functionProtein Science, 2003
- Evolution of Enzymatic Activities in the Enolase Superfamily: Crystal Structure of (D)-Glucarate Dehydratase from Pseudomonas putida,Biochemistry, 1998
- Evolution of an enzyme active site: The structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolaseProceedings of the National Academy of Sciences, 1998
- The Enolase Superfamily: A General Strategy for Enzyme-Catalyzed Abstraction of the α-Protons of Carboxylic Acids†Biochemistry, 1996
- A Carboxylate Oxygen of the Substrate Bridges the Magnesium Ions at the Active Site of Enolase: Structure of the Yeast Enzyme Complexed with the Equilibrium Mixture of 2-Phosphoglycerate and Phosphoenolpyruvate at 1.8 Å Resolution,Biochemistry, 1996
- The Refined X-ray Structure of Muconate Lactonizing Enzyme fromPseudomonas putidaPRS2000 at 1.85 Å ResolutionJournal of Molecular Biology, 1995
- Octahedral coordination at the high-affinity metal site in enolase: Crystallographic analysis of the MgII-enzyme complex from yeast at 1.9 .ANG. resolutionBiochemistry, 1995
- Mechanism of the reaction catalyzed by mandelate racemase. 2. Crystal structure of mandelate racemase at 2.5-.ANG. resolution: identification of the active site and possible catalytic residuesBiochemistry, 1991
- Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologousNature, 1990
- Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestorNature, 1988