bilogical catalyst , provides active site and brings reactant toegther
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decribe lock and key theory
active site rigid, enzyme substrate complex. products realsed from AS
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induced fit theory
active site flexible,enzyme, AS and substate ajust to maximise fit
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pH effecting enzyme activity
aa have basic and acidic side chains. 3 0 bonds distrupted as ph alters ionsiation state
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tempeture effecting enzyme activity
low activity ayt low. denatured at high
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what is cofactor
gives enzyme correct AS configuraion, inorganic non protien
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what is coenzyme
binds via H bonds to enzyme and provides something for reation. organic
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oxioreductase fucntion
catalyses transfare of e-
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transfarease function
catalyses transfare of functional groups between molecules. kinase transfare phosphates
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hydrolases function
catalyse cleavage of bonds by additon of water
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lysases fucntion
catalyses additon/ removal of ammonia, carbon dioixe or water to break/create double bonds
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isomerase function
catalyses conversion of molecule in its differnt isomeric forms by transfaring groups
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ligases
catalyses synthesis of covelant bonds using ATP
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types of enzyme specificity description 3
absolute-one type of recation one substrate. group- one type of recation, mutiple similar substares. linkage- one type of recation for a specific bond type
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what is isoenzyme
different forms of the same enzymes cataysling the same reaction in different tissues. slight variation in AA sequence
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what is alloesrtic regulation and postive vs negitive
effector(product) changing enzyme activity by binding at allosteric site. postive- speed up. negitive-slows down
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what is feedback inhibition
product later in reaction series can act as inhibitor for earlier enzyme. negivite alloserim as blocks active site slowing reaction
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Other cards in this set
Card 2
Front
decribe lock and key theory
Back
active site rigid, enzyme substrate complex. products realsed from AS
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