Multiple substrate binding states and chiral recognition in cofactor-independent glutamate racemase: a molecular dynamics study.

Möbitz, Henrik

Multiple substrate binding states and chiral recognition in cofactor-independent glutamate racemase: a molecular dynamics study. [electronic resource] - Biochemistry Aug 2004 - 9685-94 p. digital

Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.

0006-2960

10.1021/bi049580t doi


Amino Acid Isomerases--chemistry
Bacterial Proteins--chemistry
Binding Sites
Catalysis
Coenzymes--chemistry
Computer Simulation
Crystallography, X-Ray
Cysteine--chemistry
Lactobacillus--enzymology
Models, Molecular
Protein Binding
Protein Conformation
Protons
Stereoisomerism
Substrate Specificity
Thermodynamics