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Biochem 2 > Final Exam > Flashcards

Final Exam Flashcards

1
Q

What are the other names for Pentose Phosphate Pathway?

A

Hexose Monophosphate Pathway

Phosphogluconate Pathway

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2
Q

What is the purpose of the PPP?

A

To generate NADPH + ribose

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3
Q

The PPP generates NADPH. What do we need this for?

A

It’s an electron donor for biosynthesis, detoxification, respiratory bursts, and antioxidant regeneration

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4
Q

The PPP produces ribose. Why do we need this?

A

For biosynthesis
- used to make nucleosides and nucleotides
- nucleosides and nucleotides are used to make ATP, coenzyme A, FAD, NAD, and NADP molecules

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5
Q

Where does the PPP take place?

A

Cytosol

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6
Q

What is the rate limiting enzyme of the PPP?

A

Glucose 6-Phosphate Dehydrogenase

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7
Q

How much ATP is produced and consumed in the PPP?

A

0 consumed. 0 produced.

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8
Q

What is a nucleoside?

A

Base + sugar

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9
Q

What is a nucleotide?

A

Base + sugar + phosphate

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10
Q

What are the purines?

A

Guanine and adenine

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11
Q

What are the pyrimidines?

A

Cytosine and thymine. Uracil in RNA.

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12
Q

The first part of the PPP is oxidative or non oxidative?

A

Oxidative

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13
Q

The first part of the PPP is reversible or irreversible?

A

Irreversible

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14
Q

What is the first step of the PPP called?

A

Dehydrogenation

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15
Q

In the dehydrogenation step of the PPP, ______ is converted to ______?

A

Glucose 6-Phosphate is converted to 6-Phosphogluconodelta-lactone

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16
Q

What enzyme is used in the dehydrogenation step of the PPP?

A

Glucose 6-phosphate dehydrogenase

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17
Q

What is produced in the dehydrogenation step of the PPP?

A

NADPH

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18
Q

What is the rate limiting step of the PPP?

A

Dehydrogenation (1st step)

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19
Q

What is the rate limiting enzyme of the PPP?

A

Glucose 6-Phosphate Dehydrogenase

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20
Q

What is the second step of the PPP called?

A

Hydrolysis

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21
Q

________ is converted to ________ during hydrolysis?

A

6-phosphoglucono delta-lactone is converted to 6-phosphogluconate

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22
Q

What enzyme is used during the hydrolysis step of PPP?

A

Lactonase

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23
Q

Lactonase uses what to break a bond?

A

Water

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24
Q

The third step of the PPP is called ________?

A

Oxidative Decarboxylation

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25
Q

__________ is converted to __________ during the oxidative decarboxylation step of PPP?

A

6-phosphogluconate is converted to ribulose 5-phosphate

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26
Q

What enzyme is used to turn 6-phosphogluconate into ribulose 5-phosphate?

A

6-phosphogluconate dehydrogenase

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27
Q

What are the products of the oxidative decarboxylation step of PPP?

A

NADPH and CO2

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28
Q

What is the name of the step that converts ribulose 5-phosphate to ribose 5-phosphate?

A

Isomerization

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29
Q

What enzyme is used when converting ribulose 5-phosphate into ribose 5-phosphate?

A

Isomerase

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30
Q

What is the step called when ribulose 5-phosphate is converted to xyulose 5-Phosphate?

A

Epimerization

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31
Q

What enzyme is used during epimerization?

A

Epimerase

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32
Q

During the isomerization step of the PPP, ________ is converted into _______?

A

Ribulose 5-phosphate is converted into ribose 5-phosphate

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33
Q

During the epimerization step of the PPP _______ is converted into _______?

A

Ribulose 5-phosphate is converted into xyulose 5-phosphate

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34
Q

Is the isomerization step of PPP oxidative?

A

No. It’s non-oxidative

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35
Q

Is the epimerization step of PPP reversible?

A

Yes. It’s non oxidative.

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36
Q

Is the oxidative decarboxylation step of PPP oxidative or non-oxidative?

A

Oxidative

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37
Q

The hydrolysis step of PPP is reversible or irreversible?

A

Irreversible. It’s oxidative.

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38
Q

Is the dehydrogenation step of PPP reversible?

A

No. It’s oxidative.

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39
Q

Is the oxidative decarboxylation step of PPP reversible?

A

No. It’s oxidative

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40
Q

The Transketolase 1 step uses what enzyme?

A

Transketolase

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41
Q

Transketolase removes how many carbons from xyulose 5-phosphate?

A

2 carbons

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42
Q

Xyulose 5-phosphate contains how many carbons?

A

5

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43
Q

When Transketolase removes 2 carbons from xyulose 5-phosphate, it becomes a 3 carbon structure called__________.

A

Glyceraldehyde 3-phosphate (G3P)

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44
Q

How many carbons does ribose 5-phosphate have?

A

5

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45
Q

When Transketolase adds 2 carbons to ribose 5-phosphate, it becomes what ______?

A

A 7 carbon molecule named sedoheptulose 7-phosphate

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46
Q

Explain what occurs in the Transketolase1 step of the PPP?

A

An enzyme called Transketolase takes 2 carbons from xyulose 5-phosphate (5C) making it a 3 carbon structure called glyceraldehyde 3-phosphate aka G3P. It then adds those 2 carbons to ribose 5-phosphate (5C) making it become a 7 carbon structure called sedoheptulose 7-phosphate.

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47
Q

Is the Transketolase 1 step of PPP reversible or irreversible?

A

Reversible. It’s non-oxidative

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48
Q

What enzyme is used during the transaldolase step of PPP?

A

Transaldolase

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49
Q

Transaldolase removes how many carbons?

A

3

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50
Q

Transaldolase removes carbons from what molecule?

A

Sedoheptulose 7-Phosphate

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51
Q

Transaldolase adds ___ carbons to _________.

A

3

G3P

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52
Q

When transaldolase removes 3 carbons from sedoheptulose 7-phosphate, it becomes what?

A

Erythrose 4-Phosphate

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53
Q

Erythrose 4-Phosphate has how many carbons?

A

4

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54
Q

When transaldolase adds 3 carbons to G3P, it becomes what?

A

Fructose 6-Phosphate

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55
Q

How many carbons does Fructose 6-Phosphate have?

A

6

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56
Q

Describe what transaldolase does

A

It takes 3 carbons from Sedoheptulose 7-Phosphate and adds them to G3P. Sedoheptulose 7-Phosphate becomes a 4 carbon structure called Erythrose 4-Phosphate. G3P becomes a 6 carbon structure called Fructose 6-Phosphate.

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57
Q

What enzyme is used in Transketolase 2?

A

Transketolase

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58
Q

T or F: Transketolase removes 2 carbons from xyulose 5-phosphate and adds them to ribose 5-phosphate during the Transketolase 2 step of PPP.

A

False. It does this in Transketolase 1. In Transketolase 2, the carbons are added to Erythrose 4-phosphate.

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59
Q

Describe what happens in the Transketolase 2 step of PPP.

A

Transketolase removes 2 carbons from xyulose 5-phosphate and adds them to Erythrose 4-phosphate making it fructose 6-phosphate. The xyulose 5-phosphate becomes G3P

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60
Q

How does the PPP connect to glycolysis?

A

PPP turns glucose 6-phosphate into ribose 5-phosphate. This can be turned into glycolysis intermediates such as fructose 6-phosphate and glyceraldehyde 3-phosphate.

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61
Q

3 ribulose 5-phosphates makes how many fructose 6-phosphates and glyceraldehyde 3-phosphates?

A

2 fructose 6-phosphates
1glyceraldehyde 3-phosphates

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62
Q

We make NADPH in the PPP. What can we synthesize using it?

A

Fat, cholesterol, steroid hormones, bile salts

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63
Q

Why do we use NADPH to synthesize things?

A

Because synthesis requires the addition of electrons. NADPH is the electron donor.

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64
Q

How do we use NADPH for detoxification?

A

We make toxins more water soluble by adding hydroxyl groups (OH) so we can excrete them in urine. This requires adding an electron from NADPH to oxygen to get H2O.

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65
Q

Where is NADPH used for detoxification?

A

The liver.

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66
Q

What enzyme is used to add electrons and oxygen to toxins to make them more water soluble for excretion?

A

Cytochrome P450

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67
Q

What is a respiratory burst?

A

The creation of “harsh chemistry” to kill pathogens

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68
Q

How do we make harsh chemistry?

A

We make it harsh by adding electrons from NADPH

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69
Q

Electrons + _______ =very reactive molecules

A

Oxygen

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70
Q

What are some examples or harsh chemistry formed in the body using NADPH?

A

Hydrogen peroxide

Myeloperoxidase

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71
Q

How is hydrogen peroxide used in the body?

A

It is used to create reactive oxygen species to destroy bacteria, viruses, and other pathogens

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72
Q

How is myeloperoxidase used in the body?

A

It’s an enzyme used to make hypochlorous acid (bleach) from hydrogen peroxide

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73
Q

Besides reactive oxygen species, what is the other reactice compound we talked about?

A

Reactive nitrogen species

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74
Q

What are free radicals?

A

Unpaired electrons

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75
Q

What makes free radicals extremely reactive?

A

They’re unpaired so they’re always trying to steal electrons

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76
Q

What are 3 common ROS?

A

Superoxide (free radical)
Hydrogen peroxide
Hydroxyl Radical

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77
Q

What is a superoxide radical?

A

A molecular oxygen with an extra electron. O2-

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78
Q

What are the 3 ways we get superoxide radicals?

A
  1. Mitochondrial processes such as ETC
  2. Cytochrome P450 reductive enzyme in the ER
  3. White blood cells undergoing respiratory bursts
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79
Q

What is quenching?

A

Inactivation of reactive free radicals

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80
Q

What usually quenches a reactive free radical?

A

An antioxidant

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81
Q

How do we reduced free radicals?

A

By oxidizing antioxidants

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82
Q

What enzyme quenches superoxide?

A

Superoxide dismutase

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83
Q

What enzymes quench hydrogen peroxide?

A

Catalase

Glutathione peroxidase

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84
Q

What is superoxide dismitase and where is it found?

A

An enzyme that removes superoxide (quenches it) and produces hydrogen peroxide. It’s found everywhere.

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85
Q

What is catalase and where do we find it?

A

It removes hydrogen peroxide (quenches it) and is found mostly in peroxisomes but there is a small amount in cytoplasm, mitochondria, and microsomes.

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86
Q

What is glutathione peroxidase and where is it found?

A

An enzyme that gets rid of hydrogen peroxide (quenches it) and it is found in the Cytosol and mitochondria

87
Q

How does glutathione peroxidase quench hydrogen peroxide?

A

It uses 2 glutathione molecules to turn hydrogen peroxide into water

88
Q

Glutathione peroxidase is a tripepride made of what 3 molecules?

A

Glutamate
Cystein
Glycine

89
Q

When glutathione peroxidase reduces hydrogen peroxide to make water, what does it lose?

A

An electron. Duh. It’s reducing it.

90
Q

When glutathione peroxidase gets oxidized to make water from hydrogen peroxide, what happens to the molecular structure of the glutathione peroxidase?

A

A sulfur bridge forms between the 2 glutathione molecules

91
Q

We know antioxidants quench reactive species but how do antioxidants get regenerated?

A

We add electrons back. They’re oxidized when quenching. Reduced when we need them.

92
Q

What provides the electrons needed to regenerate antioxidant?

A

NADPH. Which comes from where? The PPP.

93
Q

T or F: Alcohol is a CNS depressant

A

True

94
Q

In what ways is alcohol a CNS depressant?

A

Extreme intoxication leads to sedation, depressed tendon flexes, low bp, low body temp, and decreased respiration.

95
Q

What are some long term health risks of alcohol?

A

High blood pressure, heart disease, cancer, weakening of immune system, learning/memory problems

96
Q

What is alcoholic acidosis?

A

Lactic acidosis

97
Q

When is alcoholic ketoacidosis the most common?

A

After heavy drinking or in those with an alcohol use disorder

98
Q

What is the molecular structure of alcohol?

A

Ethyl alcohol/ethanol

99
Q

Alcohol is ___kcal/gram

A

7

100
Q

T or F: Alcohol is less calories than carbs and proteins?

A

False

101
Q

T or F: Alcohol is less calories than fat

A

True

102
Q

T or F: Alcohol is easily absorbed through the entire GI tract?

A

True

103
Q

T or F: alcohol is a volatile inorganic compound

A

False. It’s a volatile ORGANIC compound

104
Q

What are the 3 enzymes systems for Ethanol Oxidation?

A

Alcohol dehydrogenase

Microsomal ethanol oxidizing system (MEOS) / Cytochrome P450

Catalase

105
Q

Catalase oxidizes ethanol when _________ is present. Hint: what does catalase quench?

A

Hydrogen peroxide

106
Q

Which of the 3 enzyme systems for ethanol oxidation is the least active system?

A

Catalase

107
Q

How does alcohol dehydrogenase oxidize ethanol?

A

It reduces NAD + to turn the ethanol into acetaldehyde. Also giving us NADH.

108
Q

When alcohol dehydrogenase (ADH) oxidizes ethanol, we get Acetaldehyde. What do we do with the acetaldehyde?

A

Aldehyde dehydrogenase (ALDH) oxidizes it by reducing NAD+ giving us Acetate and NADH

109
Q

How does catalase oxidize ethanol?

A

It pairs the oxidation of ethanol with the reduction of hydrogen peroxide to make water. This makes sense bc catalase quenches hydrogen peroxide.

110
Q

When catalase reduces hydrogen peroxide to make water, ethanol becomes _________.

A

Acetaldehyde. Then ALDH will convert that to acetate.

111
Q

MEOS/ Cytochrome P450 is associated with what organelle?

A

Endoplasmic reticulum

112
Q

When do we use the MEOS system to oxidize ethanol?

A

When ADH is completely saturated the MEOS catches the spill over

113
Q

How does MEOS oxidize ethanol?

A

It does not use NAD+ like ADH did. It’s taking ethanol and making it into Acetaldehyde. The acetaldehyde is then broken down to acetate by ALDH (which produces an NADH).

114
Q

Are MEOS enzymes inducible?

A

Yes. High concentrations of ethanol induced synthesis of MEOS enzymes which allows for more effective metabolism of ethanol in hepatocytes.

115
Q

We know we produce NADH and acetate when oxidizing ethanol. Where does that NADH and Acetate go?

A

NADH: enters the ETC to produce ATP

Acetate: gets converted to acetyl CoA to enter the TCA/Krebs cycle

116
Q

When we oxidize ethanol, what pathways are inhibited?

A

Krebs/TCA
Fat burning (Beta Oxidation)
TCA prep step
Gluconeogenesis

117
Q

When we oxidize ethanol, what pathways are stimulated?

A

Fatty Acid and TAG synthesis
Lactate production
Ketone production

118
Q

Ethanol oxidation reduces gluconeogenesis and fat burning. What does this cause?

A

Hypoglycemia (low bp)

119
Q

How is the TCA cycle inhibited by ethanol oxidation?

A

NADH inhibits the TCA bc 3 steps of TCA (3, 4, 8) produce NADH using NAD+.

120
Q

How is the TCA prep step inhibited by ethanol oxidation?

A

It’s inhibited by high concentrations of NADH. Ethanol oxidation uses up the NAD+ which prevents pyruvate dehydrogenase from making NADH from NAD+.

121
Q

What are the coenzymes needed for TCA prep step (Pyruvate Dehydrogenase Complex)

A

Thiamine pyrophosphate
Lipoamide
Coenzyme A
FAD
NAD+

122
Q

Why is there a fat accumulation when ethanol gets oxidized?

A

There is increased lipid synthesis and decreases lipid removal

123
Q

How does ethanol oxidation stimulate lactate production?

A

We have a lot of pyruvate due to increased energy state and NADH which is inhibiting the TCA. This shifts the reaction of pyruvate to make more lactate.

124
Q

Ethanol oxidation stimulates lactate production. What happens when we have high lactate production?

A

Lactic acidosis

125
Q

How does ethanol oxidation stimulate malate production?

A

When malate dehydrogenase converts oxaloactetatw to malate, it produces more NAD+ to use for ethanol oxidation

126
Q

Low oxaloacetate leads to more or less ketone production?

A

More

127
Q

Why does low oxaloacetate lead to more ketone production?

A

Because we’re using acetyl CoA for ketone production instead of making citrate for the TCA cycle bc TCA is inhibited.

128
Q

How does ethanol oxidation increase ketone synthesis?

A

3-hydroxybutyrate dehydrogenase converts 3 hydroxybutyrate to acetoacetate. This conversion produces NAD+ to use for ethanol oxidation.

*it also uses excess acetyl CoA because TCA is inhibited

129
Q

What must an amino acid lose to become an alpha-ketoacid?

A

An amino group (NH3)

130
Q

Why would we want amino acids to become alpha-ketoacids?

A

Ketoacids can be used for other metabolic pathways (TCA, fatty acid synthesis, etc)

131
Q

What 4 things determine the destination of a ketoacid?

A

Energy charge (ATP)
Hormones (glucagon/insulin)
Glucose concentration
Tissue (muscle vs liver)

132
Q

Alanine=amino acid. What alpha-ketoacid does it become?

A

Pyruvate

133
Q

What amino acid forms alpha-ketoglutarate?

A

Glutamate

134
Q

What amino acid forms oxaloacetate?

A

Aspartate

135
Q

What ways do we metabolically use amino acids?

A

Protein synthesis
Oxidation to make ATP
Glucose production
Fat production

136
Q

What are amino acids initially used for?

A

Protein synthesis. However if we have an excess, we use them for fat synthesis

137
Q

What do we do with amino acids when we have low energy?

A

We oxidize them to make ATP

138
Q

When there is low glucose in the body, what do we do with amino acids?

A

Turn them into glucose and send them to the liver for gluconeogenesis

139
Q

When we have a high energy charge and lots of glucose, what do we with the left over amino acids?

A

We turn them into fat

140
Q

What are the BCAAs?

A

LIV
Leucine, isoleucine, valine

141
Q

What amino acids are glucogenic and ketogenic?

A

PITTT

Phenylalanine, isoleucine, tryptophan, threonine, tyrosine

142
Q

What amino acids are ketogenic only?

A

Leucine and lysine

143
Q

Each amino acid has its own _________to enter the aerobic system

A

Pathway

144
Q

What does amino acid oxidation mean?

A

It means we’re using them in the aerobic system (TCA cycle and ETC) to produce ATP

145
Q

When do we oxidize amino acids?

A

When the cell has low energy

146
Q

T or F: The liver can oxidize most of the 20 different amino acids?

A

True

147
Q

T or F: Muscle can oxidize most of the 20 different amino acids?

A

False

148
Q

What amino acids can muscle oxidize?

A

LIVGAA

Leucine, isoleucine, valine, glutamate, aspartate, asparagine

149
Q

Alanine has how many amine groups?

A

1

150
Q

Glutamine has how many amine groups?

A

2

151
Q

Asparagine has how many amine groups?

A

2

152
Q

Glutamate has how many amine groups?

A

1

153
Q

Aspartate has how many amine groups?

A

1

154
Q

Is the conversion of alanine to pyruvate direct? (Meaning does alanine have to be converted to something else before it becomes pyruvate?)

A

Yes it is direct

155
Q

Is glutamine to alpha ketoglutarate a direct conversion?

A

No.

Glutamine > glutamate > alpha ketoglutarate

156
Q

Is asparagine to oxaloacetate a direct conversion?

A

No.

Asparagine > Aspartate > oxaloacetate

157
Q

Where do we turn amino acids into glucose?

A

The liver via gluconeogenesis

158
Q

When do we turn amino acids into glucose?

A

When blood glucose is low.

Starvation, low carb intake, exercise

159
Q

What amino acids do we use when we need glucose?

A

Amino acids that are glucogenic so any except lysine and leucine.

160
Q

During exercise, muscle releases _________.

A

Alanine

161
Q

What do we do with the alanine released from muscle during exercise?

A

Take it to liver to make glucose

162
Q

When the liver makes glucose from alanine released from the muscle during exercise, what is the main product?

A

Urea waste

163
Q

What happens to glutamate concentrations in the blood during exercise?

A

They decrease bc it’s taken into muscle and gives up an NH3

164
Q

What happens to alanine concentrations in the blood during exercise?

A

They increase bc alanine is released from muscle and is traveling (in the blood) to liver for gluconeogenesis.

165
Q

Muscles can donate nitrogen to other tissues for what?

A

Building amino acids

Building nitrogenous bases and nucleotides
- which is needed for building new cells

166
Q

What must muscles produce to export nitrogen out of the muscle?

A

Glutamine

167
Q

What other systems rely on glutamine?

A

Immune system

Digestive system

168
Q

What role does glutamine have in the immune system?

A

It is an immunonutrient. It supplies nitrogen to the immune system for important processes.

169
Q

What does glutamine do for the digestive tract?

A

It prevents leaky gut by preserving the gut barrier function and tight junction integrity

170
Q

What is step 1 of the glutamine-glutamate cycle?

A

Muscle imports glutamate from blood

171
Q

What is step 2 of the glutamine-Glutamate cycle? What enzyme is used?

A

Muscle takes a nitrogen from an amino acid (LIVGAA) and adds it to glutamate to produce glutamine.

Enzyme used- glutamine synthetase

Requires ATP

172
Q

What is step 3 of the glutamine-Glutamate cycle?

A

Glutamine is release from the muscle into the blood and travels to other cells that need nitrogen (digestive and immune)

173
Q

What is step 5 of the glutamine-Glutamate cycle? What enzyme is used?

A

Glutamine drops off the nitrogen which means it turns back into glutamate.

Enzyme used- glutaminase

174
Q

Process of turning Amino acid into fat

Amino acid > ___________

A

Alpha-ketoacid

175
Q

Process of turning Amino acid into fat

__________> acetyl CoA

A

Alpha-ketoacid

176
Q

Process of turning Amino acid into fat

Acetyl CoA> __________

A

Malonyl CoA

177
Q

Process of turning Amino acid into fat

What enzyme is used to convert Acetyl CoA to malonyl CoA?

A

Acetyl CoA carboxylase

178
Q

Process of turning Amino acid into fat

Malonyl CoA > _________

A

Fatty acid

179
Q

Process of turning Amino acid into fat

Malonyl CoA to fatty acid uses what enzyme?

A

Fatty acid synthase

180
Q

Nitrogen excretion is also called what ______

A

Urea cycle

181
Q

Why must we excrete nitrogen from the body?

A

We can’t store it

182
Q

If you eat too much protein meaning you have extra amino acids, what happens to them?

A

They get sent to the liver where they’re degraded to be excreted as urea (pee)

183
Q

How are excess amino acids degraded?

A

Transamination: amino groups are transferred to alpha ketoglutarate

Deamination: amino group is removed

184
Q

Every amino acid is degraded using transamination except 2. These 2 used deamination instead. What 2 amino acids are they?

A

Lysine and threonine

185
Q

Where does the urea cycle take place?

A

Liver. Partially in the mitochondrial matrix and partially in the Cytosol

186
Q

What is the purpose of the urea cycle?

A

To eliminate ammonia by producing urea

187
Q

How many ATP is used to make urea from ammonia?

A

3

188
Q

There are 2 ways glutamate can enter the urea cycle. What is the first one?

A

Glutamate dehydrogenase.

It removes the nitrogen (amino group) from glutamate.

189
Q

There are 2 ways glutamate can enter the urea cycle. What is the second way?

A

Aspartate aminotransferase aka glutamate oxaloacetate transaminase

Transfers the amino group from glutamate to oxaloacetate making Aspartate.

190
Q

What are the reactants of the rate limiting step of the urea cycle?

This is a pre step

A

HCO3 and NH3 and 2 ATP
Aka
Bicarbonate and an amino group

191
Q

What are the products of the rate limiting step of the urea cycle?

This is a pre step

A

Carbamoyl Phosphate

2 ADP

192
Q

What enzyme is used in the rate limiting step of the urea cycle?

This is a pre step

A

Carbamoyl Phosphate Synthetase-1

193
Q

What are the reactants of step 1 of the urea cycle?

A

Carbamoyl phosphate + ornithine

194
Q

What is the product of step 1 of the urea cycle?

A

Citrulline

195
Q

What is the enzyme used in step 1 of the urea cycle?

A

Ornithine transcarbamoylase

196
Q

What are the reactants of step 2 of the urea cycle?

A

Citrulline + Aspartate

And ATP

197
Q

What is the product of step 2 of the urea cycle?

A

argininosuccinate

And AMP and pyrophosphate

198
Q

What enzyme is used in step 2 of the urea cycle?

A

Argininosuccinate synthetase

199
Q

What is the reactant of step 3 of the urea cycle?

A

Argininosuccinate - fumarate

200
Q

What is the product of step 3 of the urea cycle?

A

Arginine

201
Q

What enzyme is used for step 3 of the urea cycle

A

Argininosuccinate lyase

202
Q

What are the reactants of step 4 of the urea cycle?

A

Arginine and water

203
Q

What are the products of step 4 of the urea cycle?

A

Ornithine and urea

204
Q

What makes up urea?

A

2 amino groups
-1 comes from free ammonia
- 1 comes from Aspartate
1 carboxyl group
- comes from CO2

205
Q

How is the urea cycle regulated?

A

N-acetylglutaminate activates carbamoyl phosphate synthetase-1 (CPS-1)

206
Q

Do purines have 1 ring or 2?

A

2

207
Q

Do pyramidines have 1 ring or 2?

A

1

208
Q

What are the purines?

A

Adenine and guanine

209
Q

What are the pyrimidines?

A

Cytosine, thymine, uracil (RNA)

210
Q

What are examples of nucleosides?

A

Adenosine, guanosine, inosine, uridine, cytidine, and thymidine

211
Q

What are examples of nucleotides?

A

AMP, GDP, CTP, etc…

212
Q

What are the 2 methods for nucleotide synthesis?

A

De Novo Synthesis

Salvage Pathway

213
Q

T or F: We need ATP for nucleotide synthesis?

A

True

214
Q

What do we start with when making nucleotides?

A

Ribose 5-phosphate
*We get this from PPP

Biochem 2 (1 decks)

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