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Christopher Boga
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more than 1 year ago
Enzyme kinetics maps
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km
michaelis-menten
michaelis constant
substrate
enzyme
inhibitior
allosteric
feedback
cooperativity
Criado por
Christopher Boga
quase 9 anos atrás
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4934094
mind_map
2016-04-08T00:32:41Z
Enzyme
Kinetics
Michaelis
Constant
(Km)
[Substrate]
when rxn rate
= 1/2 Vmax
Indicates
[Substrate]
needed to
speed up
rxn
High
[substrate]
means low
affinity for
substrate
Km inversely
proportional to
enzyme-substrate
affinity
Vmax
Maximum
rxn rate
Saturation
Kinetics
[Substrate]
increase,
rate of rxn
increases
until Vmax
is achieved
Cofactor
Non-protein
component
required by
some
enzymes to
reach
optimal
activity
Can be
coenzymes
or metal ions
Coenzymes
Metal Ions
Organic
molecules
Water-soluble
vitamins
Cosubstrates
Prosthetic
groups
Reversibly bind to an enzyme, transfer a chemical group to another substrate
Reverts to original form via other enzymatic rxn
Example: ATP
Binds covalently to enzyme during rxn
Emerges from rxn unchanged
Example: Heme
Heme binds to Catalase in peroxisomes to degrade H2O2
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4934094
mind_map
2016-04-08T00:32:41Z
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