Sisällysluettelo:
“…Stopped-flow spectroscopy measurements revealed that the dehydration activity of CA VI is moderate (maximum kcat = 3.0 × 105 · s-1).
The finding that CA VI is a potent catalyst of acid neutralisation emphasizes the possible role of the pellicle bound CA VI in local neutralisation of the acidic metabolic products of dental biofilm. …”
Sisällysluettelo:
“…Enzyme Reaction Mechanisms.2.1 Initial Binding of Substrate.2.2 Noncovalent Forces in Reversible Ligand Binding to Enzymes.2.2.1 Electrostatic Forces.2.2.2 Hydrogen Bonds.2.2.3 Hydrophobic Forces.2.2.4 van der Waals Forces.2.3 Transformations of the Bond Substrate.2.3.1 Strategies for Transition State Stabilization.2.3.2 Enzyme Active Sites Are Most Complementary to the Transition State Structure.2.4 Steady State Analysis of Enzyme Kinetics.2.4.1 Factors Affecting the Steady State Kinetic Constants.2.5 Graphical Determination of kcat and KM2.6 Reactions Involving Multiple Substates.2.6.1 Bisubstrate Reaction Mechanisms.2.7 Summary.References.3. …”
Sisällysluettelo:
“…The new enzyme, GsaCAβ has a significant catalytic activity for the physiological reaction, CO2 + H2O ⇋ HCO3− + H+ with a kcat of 1.1 × 105 s−1 and a kcat/Km of 7.58 × 106 M−1 × s−1. This activity was inhibited by acetazolamide (KI of 0.46 μM), a sulphonamide in clinical use, as well as by selected inorganic anions and small molecules. …”