Article
Domain closure, substrate specificity and catalysis of D-lactate dehydrogenase from Lactobacillus bulgaricus.
Journal of molecular biology - 19 Apr 2002
Razeto Adelia, Kochhar Sunil, Hottinger Herbert, Dauter Miroslava, Wilson Keith S, Lamzin Victor S
Abstract excerpt
NAD-dependent Lactobacillus bulgaricus D-Lactate dehydrogenase (D-LDHb) catalyses the reversible conversion of pyruvate into D-lactate. Crystals of D-LDHb complexed with NADH were grown and X-ray data collected to 2.2 A. The structure of D-LDHb was solved by molecular replacement using the dimeric Lactobacillus helveticus D-LDH as a model and was refined to an R-factor of 20.7%. The two subunits of the enzyme...
Topics
- Binding Sites
- Catalysis
- Dimerization
- Enzyme Activation
- Escherichia coli
- Kinetics
- L-Lactate Dehydrogenase
- Lactate Dehydrogenases
- Lactobacillus
- Lysine
- Models, Molecular
- Mutation
- NAD
- Protein Conformation