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MCM: Cardio > Enzyme Categories > Flashcards

Enzyme Categories Flashcards

1
Q

6 classes of enzymes

A
  1. oxidoreductases
  2. transferase
  3. hydrolase
  4. lyase
  5. isomerase
  6. ligase
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2
Q

oxidoreductase formula

A

Aox+Bred–> Ared + B ox

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3
Q

oxidoreductase common co-enzymes

A

NADH, NADPH, FADH2

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4
Q

oxidoreductase common enzyme names

A
  1. dehydrogenase
  2. peroxidase
  3. reductase
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5
Q

oxidoreductase special names

A
  1. oxidase or hydroxylase
    * transfer O2 atoms to water or to substrate and water
  2. cytochrome p450
  3. oxygenases: transfer both O2 atoms to substrate
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6
Q

transferase formula

A

AB + C –> A + BC

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7
Q

transferase enzyme name meaning

A

the name is the chemical group that is transferred or what chemical is synthesized

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8
Q

transferase special names

A
  1. aminotransferases–> transfer an amine group
  2. kinase–> transfer a phosphate group
  3. synthase–> indicates what kind of product is formed (glycogen synthase)
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9
Q

hydrolase formula

A

CX+ H20 –> C-H + X-OH
where X= O, N, or S
**all split bonds by splitting water

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10
Q

hydrolase special names

A
  1. protease
  2. esterase
  3. phosphatase
  4. peptidase
  5. urease
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11
Q

what do lyases do?

A

the “catch all:”

  1. cleave C-C, C-O, C-S, and C-N bonds by means other than oxidation or hydrolysis
  2. form C=C bonds by removing H2O from COH-CH
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12
Q

lyase example common names

A
  1. decarboxylase

2. aldolase

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13
Q

lyase reverse reaction to form bonds

A

synthases

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14
Q

what do isomerases do

A

no atoms lost or added, only rearranged

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15
Q

common isomerase names

A
  1. epimerase
  2. racemase
  3. mutase
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16
Q

ligase formula

A

A + B + ATP–> AB + ADP + Pi

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17
Q

what do ligases do?

A

form C-C, C-S, C-O, and C-N bonds

*require ATP or another nucleotide

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18
Q

ligase common name

A

synthetase

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19
Q

cofactors

A

cofactors often derived from vitamins, metal ions can also serve as catalystic co-factors

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20
Q

group carried by ATP, ADP/Pi, and AMP/PPi

A
  1. phosphoryl groups
  2. very high energy bond stores chemical energy
  3. protein phosphorylation
21
Q

group carried by NADH/NAD+

A
  • shuttle electrons for redox of biological fuels

- -> help produce ATP

22
Q

group carried by NADPH/NADP+

A

-shuttle electrons for oxidation in biosynthesis reactions

23
Q

groups carried by FADH2/FAD or FMNH2/FMN

A
  • shuttle electrons for redox of biological fuels
  • more powerful than NAD
  • always bound to a protein
24
Q

coenzyme A is a carrier molecule for…

A

acyl groups

R=CH3 and longer

25
Q

biotin is a carrier molecule for…

A

CO2

carboxylation

26
Q

tetrahydrofolate amino acid metabolism is a carrier for…

A

1 carbon unit

-CH3, =CH2, -COO-, to carbon or sulfur

27
Q

S-adenosylmethionine is a carrier molecule for…

A

methyl to oxygen or nitrogen

28
Q

pyridoxal phosphate reaction with…to catalyze….

A

amines, NH2 =NH to catalyze amino acid metabolism, transamination reactions

29
Q

thiamine pyrophosphate reacts with…to catalyze…

A

aldhydes/ketones to form decarboxylation at the R group

30
Q

4 classes or proteases

A
  1. cysteine proteases
  2. aspartic proteases
  3. metalloproteases
  4. serine proteases
31
Q

cysteine proteases active site

A

cysteine

32
Q

cysteine proteases examples

A
  1. papain (meat tenderizer)

2. cathepsin B (lysosome)

33
Q

aspartic proteases active site

A

aspartate

**active at low pH

34
Q

aspartic protease examples

A
  1. pepsin

2. HIV protease

35
Q

metalloprotease active site requirement

A
  • metal ion usually Zn2+

- sometimes CO2+

36
Q

metalloprotease examples

A
  1. collagenase

2. matrix metalloproteases (MMPS)

37
Q

serine protease active site

A

catalytic triad: asp, ser, his

38
Q

serine protease examples

A
  1. trypsin, chymotrysin
  2. elastase (connective tissue)
  3. thrombin (blood clotting)
39
Q

serine proteases are inhibited by

A

serpins

ex: alpha-1-antitrypsin

40
Q

how do serpins inhibit proteases

A
  1. normal catalysis involves temporary covalent attachment between protease and substrate
  2. serpin mimics the normal subsrate
  3. serpin binds covalently and then changes conformation to inactive the serine protease
41
Q

serpin is a suicide inhibitor

A

meaning that one serpin per one enzyme

** can counteract irreversibly active proteases

42
Q

anti-thrombin

A

-inhibits coagulation in blood clotting cascade

43
Q

alpha-1-anti-trypsin

A
  • inhibits neutrophil elastase in lungs (protective)
  • inactivated by cigarette smoke
  • low levels pre-dispose towards emphysema nd cirrhosis
44
Q

prepro-enzyme

A

inactive enzyme as translated from mRNA that has a leader sequence for location

45
Q

pro-enzyme (zymogen)

A

in the right location and leader sequence cleaved but is inactive

46
Q

mature protease

A

other region of the protease cleaved and is active

47
Q

metal ions can have two seperate roles

A
  1. cofactors

2. structural ligands

48
Q

structural ligands

A

can help protein stay folded

49
Q

catalystic ion

A

in the active site participates in the chemistry

MCM: Cardio (4 decks)

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