A role for flexible loops in enzyme catalysis
- 13 October 2010
- journal article
- review article
- Published by Elsevier BV in Current Opinion in Structural Biology
- Vol. 20 (6), 702-710
- https://doi.org/10.1016/j.sbi.2010.09.005
Abstract
No abstract availableKeywords
Funding Information
- NI (GM39754)
This publication has 62 references indexed in Scilit:
- Rescue of K12G Triosephosphate Isomerase by Ammonium Cations: The Reaction of an Enzyme in PiecesJournal of the American Chemical Society, 2010
- Role of Lys-12 in Catalysis by Triosephosphate Isomerase: A Two-Part Substrate ApproachBiochemistry, 2010
- Activation of R235A Mutant Orotidine 5′-Monophosphate Decarboxylase by the Guanidinium Cation: Effective Molarity of the Cationic Side Chain of Arg-235Biochemistry, 2010
- Hydron Transfer Catalyzed by Triosephosphate Isomerase. Products of the Direct and Phosphite-Activated Isomerization of [1-13C]-Glycolaldehyde in D2OBiochemistry, 2009
- Role of Loop−Loop Interactions in Coordinating Motions and Enzymatic Function in Triosephosphate IsomeraseBiochemistry, 2009
- A Substrate in Pieces: Allosteric Activation of Glycerol 3-Phosphate Dehydrogenase (NAD+) by Phosphite DianionBiochemistry, 2008
- Phosphate Binding Energy and Catalysis by Small and Large MoleculesAccounts of Chemical Research, 2008
- Enzymatic Catalysis of Proton Transfer at Carbon: Activation of Triosephosphate Isomerase by Phosphite DianionBiochemistry, 2007
- Dynamic Requirements for a Functional Protein HingeJournal of Molecular Biology, 2007
- Crystal Structures of Human Glycerol 3-phosphate Dehydrogenase 1 (GPD1)Journal of Molecular Biology, 2006