Enzymes Flashcards

1
Q

What are enzymes?

A

biological catalysts that increase rxn without changing/consuming
they alter the rate but not chemical equalibrium

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

T/F: catalyze reactions are specific and essential to things such as DNA synthesis and energy

A

true

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

T/F: without enzymes, the body could still function normally, probably

A

false

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

what are cofactors?

A

also called activators, non-protein substances essential for enzyme activity (INORGANIC)
Ex: Mg, Cl, K, Zn

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

What are Coenzymes?

A

organic substances loosely binded to protein, participate but not substrate
Ex. NADH, dehydrogenase (ORGANIC)

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

Apoenzyme definition

A

protein portion of an enzyme

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

holoenzyme definition

A

the complete, active enzyme complex (apoenzyme w coenzyme)

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

T/F: Zymogen is the inactivated secreted form of an enzyme

A

true

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

What are prosthetic groups?

A

tightly bound non-protein molecules

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

Active site

A

where substance is acted on substrate, specificity

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

What is an allosteric site?

A

cavity other than the active site, may also bind with enzyme

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

T/F: the Enzyme substrate complex is bound non covalently

A

true

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

What is another name for the ES complex?

A

adduct

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

What do oxldoreductases do?

A

transfer hydrogen and oxygen atoms from one substrate to another

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

what do transferases do?

A

transfer specific group from one enzyme to another

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

what do hydrolases do?

A

hydrolysis of a substrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

what do isomerases do?

A

change the molecular form of substrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

what do lyases do?

A

nonhydrolytic removal or addition of a group to substrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

what to ligases do?

A

joining of two molecules to form a new bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

What are some enzyme reaction conditions?

A

temperature specific
Temp/pH most at body temp. NO HIGHER THAN 40 c (this denatures the protein)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

T/F: at -5 c enzymes are inactivated and can be stored

A

true

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

Substrate concentration: concentration of an enzyme with steadily increasing concentration of substrate refers to which order?

A

first order kinetics

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

T/F: concentration is not a rate limiting step

A

false it is limiting

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

What is another name for excess substrate?

A

post zone phenomenon

25
Q

Describe the transition state

A

substance is converted to a product, must reach a higher level of free energy to convert substrate to product

26
Q

T/F: by lowering the activation energy the transition state can be easily overcome

A

true

27
Q

T/F: When determining enzyme concentration- enzyme concentration must always exceed the substrate concentration

A

FALSE

28
Q

Describe zero order kinetics. What is excess called?

A

reaction where an active site of an enzyme is saturated with substrate.
Excess –> pro zone phenomena

29
Q

T/F: in the michalis menten curve, the 1st order is directly proportional to amount of substrate

A

true

30
Q

What is Km in the michalis menten curve

A

reaction velocity is half of maximum level

31
Q

T/F: you must over come first order to get to zero order

A

true

32
Q

T/F: line weaver burk plot is a more accurate Vmax and Km than MM?

A

true

33
Q

What is competitive inhibition?

A

compound shares structural similarities, binds and competes w substrate

34
Q

What is non competitive inhibition?

A

associate w places other than the active spot, allows substrate binding, inhibits products

35
Q

what is uncompetitive inhibition?

A

binds to enzyme substrate complex, doesnt allow products

36
Q

What is the hook effect?

A

high concentration altered and false low signals, too high is no longer accurate

37
Q

Aminotransferases: AKA transaminises, catalyze the transfer of amino groups to form AST and ALT found in all major organ tissues

A

just wanted one nice one you dont have to answer :)

38
Q

what is the functional unit of the liver? Cells present?

A

liver lobular, has hepatocytes that create proteins and help detox

39
Q

describe AST, location..etc

A

primary in heart and skeletal tissues
intracellular –> cytoplasm/mitochondria
short half life
AVOID HEMOLYSIS

40
Q

T/F: AST is almost always lower than ALT

A

true

41
Q

AST ref range
ALT ref range

A

5-35 Ul/L
7-45 Ul/L

42
Q

Describe ALT, location…etc

A

liver and kidney tissues
found in cytoplasm
less concentrated intracellularly so hemolysis isnt as bad as AST

43
Q

T/F: ALT is a predictor of liver damage, viral hepatitis, fatty liver and hepatitis drug abuse

A

true

44
Q

What are the coupled assay enzymes used in AST vs ALT?

A

AST –> malate
ALT –> lactate

45
Q

describe ALP briefly, what is catalyzes, activators…etc

A

catalyzes alkaline pH
isoforms specific to locations of body
liver > bone> intestine
MAGENSIUM ACTIVATOR
yellow colo

46
Q

T/F: for ALP you should use citrate, oxalate, or EDTA

A

false, they can cause false increases in testing

47
Q

What is acid phosphotase?

A

pH below 7.0
prostate, liver..etc
used for metastatic prostate carcinoma

48
Q

Briefly describe GGT

A

found in cell membrane and cytoplams
secondary to hepatobility
increased in pt with alcoholism/drugs
normal in preggos and bone disorders

49
Q

What is the functional unit of pancreatic enzymes?

A

pancreatic ductal cells

50
Q

What are acinar cells?
Centroacinar cells?

A

acinar –> zygo. granules, precursors to lipase and amylase
Centroacinar cells –> create fluid in bicarb ions (alkaline)

51
Q

What are the two isoezymes of amylase and briefly define them

A

S-amylase: secreted by salivary glands
p-amylase: secreted by pancreatic acinar cells

52
Q

Ref range of amylase

A

23-85 Ul/L

53
Q

T/F: high carbs, potatoes and rice cause high amylase
T/F: as amylase decreases it is more probably for pancreatitis

A

true for both

54
Q

Acute pancreatitis: amylase activity after 5 to 8 hrs and only in heparinized plasma, what is the lab protocol take away?

A

NAD+ —> NADH thats it lol

55
Q

Lipase reference range

A

0-160 Ul/L

56
Q

T/F: lipase levels can stay elevated for 14 days

A

true

57
Q

Lactate dehydrogenase ref range and 5 isoenzymes

A

ref: 140 -280 Ul/L
iso enzymes LD1-LD5

58
Q

Order of lactate dehydrogenase enzymes in normal pt vs when AMI is present

A

LD2>LD1>LD3>LD4>LD5 norm
LD1>LD2 with AMI
(acute myocardial infarction)