Exam 2 Flashcards

1
Q

What extracellular enzyme hydrolyzes TAG’s?

A

lipoprotein lipase (LPL)

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2
Q

What is LPL produced by?

A

fat and muscle cells

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3
Q

Where does hydrolization of TAG occur?

A

capillary beds

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4
Q

Exercise can result in an increase in what enzyme?

A

skeletal muscle LPL

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5
Q

What is the most common storage site for TAG?

A

adipose tissue

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6
Q

FA synthesis is stimulated by what?

A

insulin

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7
Q

What does insulin strongly inhibit that hydrolyzes stored TAG?

A

HSL

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8
Q

During fasting insulin is ______ and glucagon is _______

A

decreased, increased

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9
Q

What gets lipids into the target cell?

A

LPL

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10
Q

What lipase converts TAG to DAG?

A

ATGL

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11
Q

What lipase converts DAG to MAG?

A

HSL

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12
Q

What lipase converts MAG to FFA?

A

MGL

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13
Q

Intracellular lipase is stimulated by?

A

Hormones (epinephrine, glucagon, adrenocorticotropic)

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14
Q

Once a hormone attaches to the Beta-1 receptor on a TAG, what phosphorylates TAG to the active form?

A

cAMP and adenyl cyclase (2nd messengers)

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15
Q

What would PKA stimulate when associate with a TAG?

A

lipolysis (fat burning)

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16
Q

Besides lipolysis, what does PKA stimulate in catabolism of TAG?

A

HSL

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17
Q

If HSL is inhibited, what other lipase is also inhibited?

A

ATGL

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18
Q

What enzyme converts G-3-P to DHAP

A

G-3-P dehydrogenase

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19
Q

Where in the cell does beta oxidation occur?

A

mitochondrial matrix

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20
Q

When the FA first enters the cell, what is activated by to form Acyl-CoA?

A

Acyl-CoA synthetase

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21
Q

What is the location of a FA activated to Acyl-CoA?

A

outer mitochondrial matrix

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22
Q

What is considered the rate limiting step of beta oxidation?

A

CPT

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23
Q

What inhibits CPT?

A

Malonyl-CoA

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24
Q

What is the main enzyme of CPT?

A

acyl-carnitine translocase

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25
Q

What 2 additional enzymes are required for unsaturated FA degradation?

A

reductase, isomerase

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26
Q

Isomerase will break down _____ numbered double bonds

A

odd

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27
Q

Reductase AND isomerase will break down _____ numbered bonds

A

even

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28
Q

What cofactor couples with reductase in unsaturated FA degradation?

A

NADPH

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29
Q

In unsaturated FA degradation, isomerase will convert what enzyme?

A

trans-Enoyl CoA

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30
Q

What is the final product of unsaturated FA degradation?

A

propionyl CoA

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31
Q

What does propionyl CoA get converted to?

A

succinyl CoA

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32
Q

What is the location of ketogenesis?

A

mitochondrial matrix of the LIVER

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33
Q

What is considered the rate limiting step of ketogenesis?

A

HMG CoA synthase

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34
Q

What would stimulate mitochondrial HMG CoA synthase?

A

prolonged fasting, no/low carbs

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35
Q

Cytosolic HMG CoA synthase is used in what pathway?

A

cholesterol synthesis

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36
Q

No carbs, low ATP, and in the liver would stimulate what pathway?

A

ketogenesis

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37
Q

Besides low carbs/starvation, what would create a high concentrations of ketones in the system?

A

accelerated Beta-oxidation and uncontrolled Type 1 diabetes

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38
Q

In ketogenesis, glucagon stimulates what process?

A

fat burning

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39
Q

In ketogenesis, glucagon inhibits what process?

A

liver glycolysis

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40
Q

In ketogenesis, Acetyl CoA inhibits enzyme?

A

pyruvate dehydrogenase

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41
Q

Functional ketone bodies are converted into what to be used to make energy?

A

acetyl CoA

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42
Q

What are the primary sites of glycogen storage?

A

liver and skeletal muscle

43
Q

Where in the cell is glycogen stored?

A

cytosol

44
Q

What enzymes breaks alpha(1-4) bonds?

A

glycogen phosphorylase

45
Q

What is the coenzyme with glycogen phosphorylase?

A

pyridoxal phosphate

46
Q

What is the product of glycogen phosphorylase breaking the alpha(1-4) bond?

A

glucose-1-phosphate

47
Q

What enzyme converts glucose -1-phosphate to glucose-6-phosphate?

A

phosphoglucomutase

48
Q

What enzyme removes outer 3 glucose molecules on glycogen?

A

glucosyl 4:4 transferase

49
Q

What enzyme removes the last glucose of the branch?

A

amylo-alpha-1,6-glucosidase

50
Q

What is the key regulatory enzyme of glycogenolysis?

A

glycogen phosphorylase

51
Q

What hormones are involved in the regulation of glycogen breakdown?

A

glucagon, epinephrine and norepinephrine

52
Q

What are the allosteric regulators of glycogenolysis?

A

AMP and calcium

53
Q

On what tissue would glucagon have an effect?

A

the liver

54
Q

On what tissues would epinephrine and norepinephrine have an effect?

A

muscle and liver

55
Q

What is adenylyl cyclase activated by in glycogen breakdown?

A

glucagon, epinephrine and norepinephrine

56
Q

What enzyme is stimulated by the presence of cAMP?

A

PKA/AMPK

57
Q

In general, what does AMPK inhibit?

A

synthesis pathways

58
Q

In general, what does AMPK stimulate?

A

breakdown pathways

59
Q

What would activate glycogen phosphorylase?

A

AMP

60
Q

What is a subunit of glycogen phosphorylase kinase complex?

A

calmodulin

61
Q

What are the final products of AA catabolism when creating an alpha-keto acid?

A

ATP, Glucose, FA

62
Q

What is the main site for AA catabolism?

A

liver

63
Q

Where are branched chain AA more often catabolized?

A

skeletal muscle

64
Q

What are the AA that skeletal muscle can oxidize?

A

LIV (branched) GAA (glutamate, aspartate, asparaine)

65
Q

What coenzyme is required for transamination?

A

pyridoxal phosphate

66
Q

What is the enzyme used to deaminate glutamate?

A

glutamate dehydrogenase

67
Q

What cofactor is coupled with glutamate dehydrogenase?

A

NAD+

68
Q

What is the a-ketoacid of alanine?

A

pyruvate

69
Q

What is the a-ketoacid of aspartate?

A

oxaloacetate

70
Q

What is the a-ketoacid of glutamine and glutamate?

A

a-ketoglutarate

71
Q

What enzyme is used to stick an extra amino group on glutamate?

A

glutamate synthetase

72
Q

What enzyme in the muscle turns glutamate into glutamine by adding a nitrogen/ammonia?

A

glutamine synthase

73
Q

In the muscle, what hydrolyzes glutamine back to glutamate?

A

glutaminase

74
Q

In skeletal muscle, what makes alanine from pyruvate?

A

ALT or glutamate-pyruvate transaminase (GPT)

75
Q

What enzyme transfers an amino group from glutamate to oxaloacetate to make aspartate?

A

AST or glutamate-oxaloacetate transaminase (GOT)

76
Q

What does the first NH3 on urea come from?

A

glutamate dehydrogenase (GDH)

77
Q

Where does the second NH3 on urea come from?

A

aspartate aminotransferase (AST)

78
Q

What enzyme would create carbamoyl phosphate from Co2, NH3, and 2 ATP?

A

carbamoyl phosphatase

79
Q

Where in the cell is carbamoyl phosphatase active?

A

mitochondrial matrix

80
Q

What 2 places in the cell does the urea cycle take place?

A

cytosol and mitochondrial matrix

81
Q

What can be considered the prep step of the urea cycle?

A

carbamoyl phosphatase

82
Q

What enzyme cleaves off 2 amino groups to create urea?

A

arginase

83
Q

A-ketoglutarate entering krebs cycle can be called what process?

A

anaplerosis

84
Q

Glutamate concentrations in the plasma during exercise tend to?

A

decrease

85
Q

Alanine concentrations in the plasma during exercise tend to?

A

increase

86
Q

What is over 90% of muscle amino acid uptake after a meal?

A

LIV and glutamate

87
Q

What amino acids are released in amounts MORE than they are taken in?

A

glutamine and alanine (transporters)

88
Q

What amino acids are released in LESS amounts than they are taken in?

A

LIV GAA

89
Q

What energy charge stimulates oxidation of amino acids?

A

low energy

90
Q

What enzyme does high energy and plenty of glycogen storage inhibit?

A

PFK (glycolysis)

91
Q

What enzyme does glucose-6-phosphate accumulation inhibit?

A

hexokinase

92
Q

What stimulates glucokinase?

A

insulin and fructose

93
Q

After going through the fructose-1-phosphate pathway, how will fructose enter glycolysis?

A

as G-3-P

94
Q

Where in the cell does FA synthesis occur?

A

cytosol

95
Q

What is the main coenzyme of FA synthesis?

A

NADPH

96
Q

What enzyme combines acetyl-CoA and oxaloacetate to make citrate?

A

citrate synthase

97
Q

What enzyme creates OAA and Acetly-CoA from cytosolic citrate?

A

citrate lyase

98
Q

What enzyme creates Malonyl CoA from Acetyl CoA?

A

Acetyl CoA Carboxylase (ACC)

99
Q

What is the rate limiting step of FA synthesis?

A

Acetyl CoA Carboxylase (ACC)

100
Q

What is the final step of FA synthesis?

A

Palmitate

101
Q

Which 2 steps of FA synthesis will use NADPH?

A

the reduction steps

102
Q

What enzyme will release Palmitate from FA synthesis?

A

palmitoyl thioesterase

103
Q

What coenzyme is required for elongases?

A

NADPH

104
Q

What enzyme adds double bonds to Palmitate?

A

desaturases