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21 Cards in this Set

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major purpose of enzyme inhibition
regulate [E] from -->ing to much [P], homeostasis
two cats of enzyme inhibition
competitive


noncompetitive
competitive inhibition
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]
how is competitive inhib overcome
increase amt of [S]
non competitive inhib
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
allosteric regulation
1 + binding site

second binding site
2 cats of allosteric enzymes
stimulators

inhibitors
allosteric enzymes: active
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
allosteric enzymes: inactive
T state,

inhibitor

inactive --> [S] can't bind
--> stability

most common
what other mols can stabilize the [E]
[S] and allosteric [E]

activator
co enzyme
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
co factor
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
Feedback inhibition
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
M&M displays ___ binding

has ___ kind enzymes
M&M displays allosteric binding

has single subunit kind enzymes
prosthetic group
changes shape of [E] for efficiency

nonprotein

bound to protein

ex: heme
M&M enzymes have a ___ curve

allosteric enzymes have ___ curve
M&M enzymes have a HYPERBOLIC curve

allosteric enzymes have SIGMOUD "S" curve
sigmoud "s" curve
for allosteric [E]

starts off slow b/c binding
cooperativity
catalystic [S] binds --> other subunit can take [S] to completion
cooperativity
catalystic [S] binds --> other subunit can take [S] to completion
enzymes have 3 roles:
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)
why are [E] so large?
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