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21 Cards in this Set
- Front
- Back
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major purpose of enzyme inhibition
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regulate [E] from -->ing to much [P], homeostasis
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two cats of enzyme inhibition
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competitive
noncompetitive |
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competitive inhibition
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1. reversible
2. structure sim to [S] 3. competes for active site w/ [S] 4. changes shape of active site 5. changes shape of [S] 6. no [P] |
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how is competitive inhib overcome
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increase amt of [S]
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non competitive inhib
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1.NON REVERS
2. not struct sim to [S] 3. changes shape of [E] --> changes conformation --> changes func 4. metals ex: HG 5. binds allosteric site 6. destroys enzyme |
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allosteric regulation
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1 + binding site
second binding site |
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2 cats of allosteric enzymes
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stimulators
inhibitors |
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allosteric enzymes: active
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R state - relaxed
->es stabilizes active form --> no change, binds to active site postage -- easier others to bind stimulator --> [S] still bind and -->es [P] -->es stabilizer most stable |
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allosteric enzymes: inactive
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T state,
inhibitor inactive --> [S] can't bind --> stability most common |
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what other mols can stabilize the [E]
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[S] and allosteric [E]
activator |
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co enzyme
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A nonprotein organic molecule that plays a role in catalysis by an enzyme.
microele NOT [E]!!! don't perm bind to [E] considered a [S] b/c changes chem during rxns and seps to go to other rxns move from [E] mol to [E] mol contain C ex: ATP and ADP |
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co factor
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An inorganic ion that is weakly bound to an enzyme and required for its activity
changes shape of [E] for efficiency non protein bind to active site and considered a [S] no change form metall [E] Hg, Fe, Cu, Zn |
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Feedback inhibition
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final [P] of metals
final [P] of alosterically inhibits [E] from commitment step prevents overprod of [P] also called "end product" product of rxn becomes inhibitor |
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M&M displays ___ binding
has ___ kind enzymes |
M&M displays allosteric binding
has single subunit kind enzymes |
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prosthetic group
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changes shape of [E] for efficiency
nonprotein bound to protein ex: heme |
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M&M enzymes have a ___ curve
allosteric enzymes have ___ curve |
M&M enzymes have a HYPERBOLIC curve
allosteric enzymes have SIGMOUD "S" curve |
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sigmoud "s" curve
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for allosteric [E]
starts off slow b/c binding |
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cooperativity
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catalystic [S] binds --> other subunit can take [S] to completion
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cooperativity
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catalystic [S] binds --> other subunit can take [S] to completion
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enzymes have 3 roles:
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1. [E] orient [S]s
2. [E] --> strain on [S] --> less stable and more reactive 3. [E] temp add chem groups, aka charges to [S] --> imp in O-R rxns (invovling + or - of e-s) |
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why are [E] so large?
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1. induced fit
2. provides framework so a.acids of actie site properly placed in relation to [S] 3. works in small but imp changes in protein shape/structure that --> induced fit |
