問題一覧
1
Enzymes are _____________ they increased and speed-up the rate of reactions without being change in overall process
protein catalase
2
Enzyme are task to do specific actions come in contact with __________ and bind together
Substrate
3
______________ will fit to the enzyme and transforms and producing new products
Substrate
4
What do you call when a substrate come contact with enzymes?
Enzyme substrate complex
5
this site is the cavity, where the reaction takes place; substrate interacts w/enzyme.
Active site
6
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
7
This is the compound which the enzyme works & speed up the reaction, acted upon enzyme.
Substrate
8
This is the protein portion of the enzyme (inactive) come in contact w/ Cofactor
Apoenzyme
9
the organic cofactor and nonprotein portion (activator)
Coenzyme
10
When an apoenzyme come in contact with cofactor it will now form?
Haloenzyme
11
capable of binding to a substrate and eliciting a rection.
Active enzyme
12
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
13
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
14
This model allow minor changes to accommodate the substate
Induced fit model
15
Oxidation-reductions. [link to one another requires Coenzyme either: oxidize or reduce as the substrate reaction]
OXIDOREDUCTASES
16
Transfer of functional group
TRANSFERASES
17
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
18
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
19
Rearrangement of atoms [mirror reaction]
ISOMERASES
20
Reactions involving bond formation coupled with ATP hydrolysis [energy hydrolysis]
LIGASES
21
TRUE OR FALSE. Enzymes are protein but not all protein are enzyme
TRUE
22
o Protein dentures at what temperature?
40C
23
Destroy at?
60 C
24
Enzymes optimum ph activity?
7-7.5 ph
25
Reaction rate is directly proportional to substrate concentration [maximum reaction rate, depends on substrate concentration. If it reaches maximum level]
FIRST-ORDER KINETICS
26
Reaction rate depends only on enzyme concentration [the more enzyme the more reaction will occur]
ZERO-ORDER KINETICS
27
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
28
binds to the activate site and compete w/ the substrate for Active site
COMPETITIVE INHIBITOR
29
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
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
Non-competitive inhibitor is what type? it occurs if the inhibitor will already destroy part of enzyme
IRREVERSIBLE TYPE
33
All actions in the body are mediated by?
Enzymes