Enzymes Flashcards

1
Q

isozymes

A

different molecular forms of the same enzyme synthesized by different tissues of the same organism

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

classifications of enzymes

A
oxidoreductases (often names dehydrogenase) 
transferases 
hydrolases
lyases (cleave C-C, C-S and some C-N)
isomerases
ligases
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

enzyme kinetic curve compares what parameters?

A

the rate of reaction to the substrate concentration (how many molecules of subtrate are converted ever min)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What can speed up a reaction? (besides catalyst/enzymes)

A

Temperature - to an extent if its too hot it’ll denature the proteins

A particular pH that assist in the ionization of residues at the active site - extreme pH levels will denature

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Vmax and Km of emzymatic kinetics

A

higher Km means a weaker affinity for substrate and enzyme

the Km is equal to the concentration of subtrate at half the Vmax.

Vmax - the fastest the reaction will go regardless of substrate concentration

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

irreversibile inhibition

A

enzyme is destroyed when inhibitor reacts covalently with it

Aspirin inhibits prostaglandin synthetase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

reversible inhibition

A

nonconvalently interaction with enzyme, can be competitive inhibition and noncompetitive

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

competitive inhibitor

A

usually a substrate analog, binds in the active site where the substrate

affinity of enzyme for substrate decreases (Km inc)

ex. statins that competitively inhibit HMG-CoA (synthesis of cholesterol)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

non-competitive inhibition

A

binds enzyme at a different site than active site,

decreases Vmax

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

allosteric control of enzyme

A

allosteric enzyme have an allosteric site, effector binds noncovalently and reversibly at the allosteric site

allosteric binding changes the enzyme activity: increases - positive, decreases - negative

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

covalent modification

A

reversible

often phosphorylation, by kinase or dephosphorylation, phosphatase

quick

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

feedback control

A

feedback inhibition - when the final product of a pathway circulates back to inhibit an earlier enzyme in the pathway

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

hormonal control

A

hormones change the physiological state of target organs through activation or inactivation of enzymes in the organs.

ex - insulin, glucagon

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

nuclear receptor

A

intracellular receptor activation - steriod hormones, either enter nucleus to bind receptor or on membrane which detaches and relocates to neucles

ex - estrogen receptor, progesterone receptor, thyroid hormone receptor

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

how does cholera toxin work?

A

taken into cell and activated by proteolysis

transfers ADP-Ribosyl to G-alpha-s

this permanently activates G-protein

increase cAMP level intracellularly

keeps CFTR open, Cl- pours out of the cells and water follows

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

how does caffiene work?

A

increase metabolism by inhibiting breakdown of cAMP (by phosphodiesterase), higher cAMP means higher meta