問題一覧
1
binds to the activate site and compete w/ the substrate for Active site
COMPETITIVE INHIBITOR
2
o Protein dentures at what temperature?
40C
3
interfere; not typically bad needed for regulation (ex. need a enzymatic reaction to occur may kailangan na process in the body, if it reaches its goal. If too much can cause damage)]
Inhibitors
4
site other than the active site; another regulatory wander will bind to the enzyme it can be regulatory molecule, inhibitor. When the substate come in contact with active it will now form enzyme/substrate com plex – enzyme slightly change its shape as the substrate binds & forming products. Product are form, leave the active site will go to the specific task.
Allosteric site
5
All actions in the body are mediated by?
Enzymes
6
______________ will fit to the enzyme and transforms and producing new products
Substrate
7
the organic cofactor and nonprotein portion (activator)
Coenzyme
8
this site is the cavity, where the reaction takes place; substrate interacts w/enzyme.
Active site
9
Enzyme are task to do specific actions come in contact with __________ and bind together
Substrate
10
What do you call when a substrate come contact with enzymes?
Enzyme substrate complex
11
This is the protein portion of the enzyme (inactive) come in contact w/ Cofactor
Apoenzyme
12
Not all substrate can fit in certain enzyme also enzyme. Enzyme have predetermined shape for the active site, only a substrate with specific shape can bind to an active site. WHat do u call this model?
Lock and Key Model
13
Oxidation-reductions. [link to one another requires Coenzyme either: oxidize or reduce as the substrate reaction]
OXIDOREDUCTASES
14
the same function it exist in diff. form either found in diff tse sources or can have diff. properties such as diff. electrophoretic mobility, solubility, resistance, they have the same function of CK]
Isoenzyme
15
This model allow minor changes to accommodate the substate
Induced fit model
16
Enzymes are _____________ they increased and speed-up the rate of reactions without being change in overall process
protein catalase
17
Enzymes optimum ph activity?
7-7.5 ph
18
Non-competitive inhibitor is what type? it occurs if the inhibitor will already destroy part of enzyme
IRREVERSIBLE TYPE
19
Removal of water to break H bonds. enzyme catalyze hydrolysis reaction, addition of water molecule to the bond to cause it to break; central to the process of digestion
HYDROLASES
20
Transfer of functional group
TRANSFERASES
21
Reactions involving bond formation coupled with ATP hydrolysis [energy hydrolysis]
LIGASES
22
Reaction rate depends only on enzyme concentration [the more enzyme the more reaction will occur]
ZERO-ORDER KINETICS
23
Addition of a group to a double bond or removal of a group to form a double bond [does not involve hydrolysis/oxidation reaction]
LYASES
24
Destroy at?
60 C
25
Inhibitor will not compete w/the substrate with active site, but it will look for another site called Allosteric site. Bind to allosteric site in which cause CHANGES.
NON-COMPETITIVE INHIBITOR
26
capable of binding to a substrate and eliciting a rection.
Active enzyme
27
TRUE OR FALSE. Enzymes are protein but not all protein are enzyme
TRUE
28
Rearrangement of atoms [mirror reaction]
ISOMERASES
29
Reaction rate is directly proportional to substrate concentration [maximum reaction rate, depends on substrate concentration. If it reaches maximum level]
FIRST-ORDER KINETICS
30
Binds to enzyme substrate complex. Even increased amount of substrate it will not be affected. The more substrate bind to enzyme the more it bind to enzyme substrate complex
UNCOMPETITIVE INHIBITOR
31
Competitive inhibitor is what type? it occurs when there is more substrate than inhibitors .If inhibitor (blocking the active site) come contact w/active site it will interfere leading to NO REACTION]
REVERSIBLE TYPE
32
When an apoenzyme come in contact with cofactor it will now form?
Haloenzyme
33
This is the compound which the enzyme works & speed up the reaction, acted upon enzyme.
Substrate