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Quan SG Flashcards

1
Q

a catalysts of biological reactions

A

Enzymes

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2
Q

what type of rxns do enzymes catalyze

A

thermodynamically possible

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3
Q

are enzymes used or changed during the rxn?

A

No

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4
Q

Do enzymes change the equilibrium or direction during the rxn?

A

No

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5
Q

what is the optimal temperature for most enzymes

A

37 C

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6
Q

every enzyme has its own optimal …

A

temperature & pH

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7
Q

what is trypsin’s optimal pH?

A

6-7

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8
Q

what is pepsin’s optimal pH?

A

2-3

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9
Q

because of the effect of pH on the ionic charge of AA side chains of an enzyme results in …

A

pH sensitivity

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10
Q

what kind of enzymes catalyze oxidation-reduction rxns

A

Oxidoreductases

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11
Q

what kind of enzymes catalyze group transfer rxns

A

Transferases

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12
Q

what kind of enzymes catalyze hydrolysis rxns where water is acceptor of transferred group

A

Hydrolases

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13
Q

what kind of enzymes catalyze lysis of a substrate, generating a double bond in a non-hydrolytic, non-oxidative elimination

A

Lysases (synthase)

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14
Q

what kid of enzymes catalyze isomerization rxns

A

Isomerases

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15
Q

what kind of enzymes catalyze ligation, or joining of 2 substrates

A

Ligases (synthase)

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16
Q

what kind of enzyme requires ATP?

A

Ligases (synthase)

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17
Q

what contains the function groups of the enzyme?

A

Active site

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18
Q

specific region in an enzyme to which substrate molecule is bound

A

Active site

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19
Q

at what part of the enzyme does the catalytic active occur?

A

Active site

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20
Q

what part of the enzyme contains the the functional group?

A

Active site

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21
Q

how do enzymes bind to substrates?

A

weak, non-covalent bonds

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22
Q

the theory that an active site of an enzymes only accepts a specific substrate

A

Lock & Key (Fischer theory)

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23
Q

one enzyme acts only on one substrate

A

absolute enzyme

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24
Q

one enzyme acts on different substrates that all have the same bond type

A

Relative

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25
Q

enzymes that catalyze the transformation of only substrates which are in certain geometrical configuration (cis or trans)

A

Stereospecific

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26
Q

One international unit (IU) catalyzes conversion of 1 mol of substrate to product per minute

A

Enzyme activity

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27
Q

the specific activity of an enzyme is a measure of the number of IU/mg protein

A

Enzyme activity

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28
Q

inhibitor has structure similar to the substrate, being able to bind to same active site and prevents binding of substrate

A

competitive inhibitor

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29
Q

How can the activity of a competitive inhibitor be reversed?

A

by increasing [s]

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30
Q

an inhibitor that binds to an enzyme site different from the active site & changes the shape of the enzyme active site so the substrate can no longer bind

A

Non-competeitive inhibitor

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31
Q

this type of inhibition cannot be overcome by increasing [s]

A

Non-competeitive inhibitor

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32
Q

an inhibitor that binds to the enzyme-substrate compels

A

uncompetitive inhibitor

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33
Q

type of inhibition that usually only occurs in multiple substrate rxns

A

uncompetitive inhibitor

34
Q

what class of inhibitors is non-covalently bound to the enzyme

A

reversible inhibitors

35
Q

tightly bound through covalent or non-covalent interactions

A

irreversible inhibitors

36
Q

react with specific R groups of AA’s

A

Group-specific reagent

37
Q

structurally similar to the substrate for the enzyme and covalently alter active site

A

Substrate Analogs

38
Q

enzyme participates in its own irreversible inhibition

A

Suicide Inhibitors

39
Q

bind non-covalently to allosteric site and regulate enzyme activity via conformational changes

A

allosteric modulators

40
Q

a type of enzyme regulation involving the binding of a non-substrate molecule at locations on the enzyme other than the active site.

A

allosteric control

41
Q

covalent attachment of a molecule to an AA side chain can modify the enzyme

A

reversible, covalent modification

42
Q

multiple forms of an enzyme which differ in AA sequence but can catalyze the same reaction

A

ISOENZYMES (ISOZYMES)

43
Q

many enzymes synthesized as inactive precursors (zymogens) that are activated by

A

proteolytic cleavage

44
Q

inactive enzyme activated upon cleavage

A

proteolytic cleavage

45
Q

three examples of proteolytic cleavage enzymes

A

digestive, blood clotting, and insulin

46
Q

cascade of proteolytic activations is used in what pathway

A

blood clotting

47
Q

synthesized as zymogens in stomach and pancreas

A

digestive enzymes

48
Q

proinsulin to insulin by removal of a peptide

A

proteolytic cleave, protein hormones

49
Q

glycolysis turns glucose into what

50
Q

ATP, glycogen, ribose, lipid molecules, and NADPH can be generated from

51
Q

stored in the cell as Glc-6-P

52
Q

what is the rate limiting step of glycolysis?

53
Q

Net gain of ATP from glycolysis?

A

4ATP - 2ATP = 2ATP

54
Q

pyruvate can be transformed to ______ to regenerate NAD+

55
Q

pyruvate + NADH2 –> lactate + NAD+

A

LACTATE DH RXN

56
Q

pyruvate + NADH2 –> lactate + NAD+ is catalyzed by

A

lactate DH

57
Q

glucose + ATP –> G6P + ADP

is catalyzed by

A

Hexokinase

58
Q

Hexokinase is inhibited by

59
Q

Pentose phosphate pathway is important for the generation of

A

NADPH and Ribose

60
Q

what is used as the building block for glycogen?

A

UDP-glucose

61
Q

used as immediate precursor for glycogen synthesis

A

UDP-glucose

62
Q

catalyzes elongation of chains glycogen is initiated by

A

glycogen synthase (glycogenin)

63
Q

catalyzes attachment of glucose molecule to one of its own tyrosine residues

A

glycogenin

64
Q

a type of covalent bond that joins anomeric C1 of a glucose molecule and OH of tyrosine side chain of glycogenin

A

glyosidic bond

65
Q

catalyzes phospohrolytic cleavage of 1-4 glycosidic linkages of glycogen, releasing G1P as rxn product

A

GLYCOGEN PHOSPHORYLASE

66
Q

glycogen (n residues) + Pi -> glycogen (n-1 resides) + G-1-P

A

GLYCOGEN PHOSPHORYLASE

67
Q

stimulated by Epinephrine and Glucagon

A

GLYCOGEN PHOSPHORYLASE

68
Q

Inhibition of glycogen phosphorylase can be used to treat what?

69
Q

inhibitors bind at the dimer interface, stabilizing the inactive (tense) conformation of GP

A

glycogen phosphorylase inhibition for treatment of diabetes

70
Q

almost the reverse of glycolysis

A

Gluconeogenesis

71
Q

3 IRREVERSIBLE STEPS OF GLYCOLYSIS THAT MUST BE BYPASSED IN GLUCONEOGENSIS

A

Hexokinase
Phosphofructokinase
Pyruvate Kinase

72
Q

triggered by the hormone glucagon when blood glucose is low

A

Glucagon-cAMP cascade in the liver

73
Q

inhibition of glycolysis and glycogen synthesis is the result of?

A

Glucagon-cAMP cascade in the liver

74
Q

stimulation of gluconeogenesis and glycogen breakdown

free glucose is formed for release to the blood is the result of?

A

Glucagon-cAMP cascade in the liver

75
Q

Cycle used during muscle exercising

A

Cori cycle

76
Q

Lactate produced from pyruvate passes via the blood to the liver, where it may be converted to glucose through gluconeogensis

A

Cori cycle

77
Q

the glucose released into the blood to travel back to the muscle to fuel glycolysis by what cycle

A

cori, during exercise

78
Q

costs 6~P in liver for ever 2~P made available in muscle (net 4~P)

A

cori cycle

79
Q

Where does TCA cycle occur

A

Mitochondrial matrix

80
Q

is derived from pyruvate via pyruvate carboxylase (1st step in gluconeogenesis)

A

oxaloacetate

81
Q

is derived from pyruvate. via PDH complex

A

Acetyl-CoA

82
Q

Pyruvate dehydrogenase catalyze the synthesis of

A

Acetyl-CoA

Biochem (2 decks)

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