Amanote Research
Register
Sign In
Dual Role of the Active Site Residues of Thermus Thermophilus 3Isopropylmalate Dehydrogenase: Chemical Catalysis and Domain Closure
doi 10.1021/acs.biochem.5b00839.s001
Full Text
Open PDF
Abstract
Available in
full text
Date
Unknown
Authors
Unknown
Publisher
American Chemical Society (ACS)
Related search
Structural Basis for the Inactivation of Thermus Thermophilus Proline Dehydrogenase byN-Propargylglycine†,‡
Biochemistry
Biochemistry
Roles of Active Site Residues and the NH(2)-terminal Domain in the Catalysis and Substrate Binding of Human Cdc25
Journal of Biological Chemistry
Biochemistry
Cell Biology
Molecular Biology
A Second Site Specific Endonuclease From Thermus Thermophilus 111, Tth111II
Nucleic Acids Research
Genetics
Role of Archaeal HerA Protein in the Biology of the Bacterium Thermus Thermophilus
Genes
Genetics
Proline Dehydrogenase From Thermus Thermophilus Does Not Discriminate Between FAD and FMN as Cofactor
Scientific Reports
Multidisciplinary
Role of the Anion-Binding Site in Catalysis and Regulation ofMycobacterium Tuberculosisd-3-Phosphoglycerate Dehydrogenase
Biochemistry
Biochemistry
Characterization of the Nitric Oxide Reductase From Thermus Thermophilus
Proceedings of the National Academy of Sciences of the United States of America
Multidisciplinary
Characterization of Glycerol Trinitrate Reductase (NerA) and the Catalytic Role of Active-Site Residues
Journal of Bacteriology
Microbiology
Molecular Biology
Functions of Amino Acid Residues in the Active Site ofEscherichia coliPyrroloquinoline Quinone-Containing Quinoprotein Glucose Dehydrogenase
Journal of Biological Chemistry
Biochemistry
Cell Biology
Molecular Biology