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CH6 Enzyme - Coggle Diagram
CH6 Enzyme
酵素動力學
Michaelis-Menten equation
kcat (turnover number)
how many substrate molecules one enzyme molecule
can convert per second
Km (Michaelis constant)
an approximate measure of a substrate’s affinity for an
enzyme
Two-Substrate Reactions
order bi bi
random order
ping-pong
order
Sequential Kinetic Mechanism
Lineweaver-Burk: lines intersect
Ping-Pong Kinetic Mechanism
Lineweaver-Burk: lines are parallel
影響催化速率的因子
substrate
enzyme
effectors
temperature
Enzyme Inhibition
Competitive Inhibition
No change in Vmax; apparent increase in KM
Lineweaver-Burk: lines intersect at the y-axis
不可逆
permanently shut off one enzyme molecule
Mixed Inhibition
Decrease in Vmax; apparent change in KM
Lineweaver-Burk: lines intersect left from the y-axis
Uncompetitive Inhibition
No change in KM / Vmax
Lineweaver-Burk: lines are parallel
調節酵素活性
covalent modification
irreversible
noncovalent modification (allosteric)
reversible
活化能
Imaginary Stickase
Enzymes do not affect equilibrium
Enzymes bind transition states best
催化方式
covalent
change reaction paths
acid-base
give and take protons
metal ion
use redox cofactors