Biochemistry Flashcards

1
Q

A molecule with a net charge of zero with a positive and negative charge rendering it isoelectric

A

Zwitterion

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

Linear polymers of amino acids

A

Proteins

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

Functions of protein

A
Regulate METABOLISM
facilitate CONTRACTION in muscle
Provide structural FRAMEWORK 
SHUTTLE molecules in blood stream
component of IMMUNE SYSTEM
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

The set of all the proteins expressed by an individual at a particular time

A

proteome

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

Major goal is to identify proteins and their postranslational modification which correlates with disease, physiologic phenomena and aging

A

Proteomics

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

Which part of its structur dictates function of amino acid

A

R group

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

Nonpolar vs polar

A

Nonpolar is hydrophobic

Polar hydrophilic

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

Amino acid that has the smallest side chain

Used in first step of heme synthesis

A

Glycine

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

Major neurotransmitter in the spinal cord

A

Glycine

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

Carries ammonia and carbons of pyruvate from skeletal muscle to liver

A

Alanine

Together with glycine constitutes major fraction of ammino acid in blood

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

3 ammino acids that accumulate in maple syrup disease

A

Valine leucine isoleucine

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

Phenylalanine

A

Precursor of tyrosine

Differ in only in side ring

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

Accumulates in phenylketonuria

A

Phenylalanine

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

Largest side chain

A

Tryptophan

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

Tryptophan prescursor of

A

Tryp mo siya no (toni)?

Tryptophan = melatonin, serotonin, niacin

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

Precursor of homocysteine

A

MetHionine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q
Actually an imino acid
Pasaway
Contributes to fibrous structure of collagen
Causes kinks 
No charge
A

Free si Proline na pasaway

Proline

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

Tyrosine is the precursor of

A

L dopa > dopamine >norepinephrine >epinephrine

Thyroxine
Melanin

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

Glutamine is deamminated to ammonia by

A

Glutaminase

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

Major carrier of nitrogen to liver from peripheral tissues

A

Glutamine

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

Site of n linked glycolsylation of proteins

A

Asparagine

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

Ammino acid with sulfhydryl group

A

Cysteine
- participates in biosynthesis of co enzyme a
Cysteine + cysteine = cystine through a covalent disulfide bond

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

Precursor of gaba and glutathione

A

Glutamate

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

Enzyme that turns glutamate to gaba

A

Glutamate decarboxylase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

Strongest base

A

Arginine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

Weak base

A

Histidine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

Precursor of histamine

A

Histidine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

Used in diagnosis of FOLIC ACID DEFICIENCY thru FIGLU EXCREATION TEST

A

Histidine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

Arginine is the precursors of

A

Creatinine , urea , nitric oxide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

The 21st amino acid

A

Selenocysteine

Selenium atom replaces sulfur if cysteine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

Lathyrus seeds
Nuerolathyrism
Progressive and irreversible spastic paralysis of lower extremities

A

Homoartinine and beta-N-oxalyldiaminopropionic acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

Cycad seeds
Neurotoxic
Implicated in disease such as ALS, Parkinson dementia complex in natives of Guam

A

Beta-Methylaminoalanine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

Except for _____ all amino acids are chiral

A

Glycine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

All ammino acids in proteins are in

A

L-configuration

D-configuration: bacterial cell walls and antibiotics

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

Essential ammino acids

A

PVT TIM HALL always ARGues never TYRs

Phenylalanine
Valine
Tryptophan

Threonine
Isoleucine
Methionine

Histidine
Arginine
Leucine
Lysine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

Primary structure :_______________
Secondary structure : ______________
Tertiary structure: ________________
Quarternary structure: _____________

A

1- sequencing (peptide bonds attach alpha amino group to alpha carbonyl group of another)

  1. Folding (folding of short ,30-30 residue, contiguous segments of polypeptide into geometrically ordered units — hydrogen bond)
  2. 3D shape (globular vs fibrous)
  3. If more than 1 polypeptide chain
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

Most common secondary structure

And examples

A

Alpha helix

Keratin 100%
Hemoglobin 80%

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

Non repetitive secondary structure

A

Loops and coils

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

Supersecondary structures with no actual function

A

Motifs

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

First protein sequenced

A

Insulin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

Specialized group of proteins required for proper folding

Prevents aggregation
Rescue proteins trapped in misfolded deadend

A

Chaperones

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

Resluts in unfolding and disorganization of proteins secondary and tertiary structures

A

Denaturation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

PrPsc

A

Prion

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

Factors causing shift to the right

p50 is increased

A

Circumstances that needs more oxygen in tissues

Increase in (5)
CO2
Acidity thus decrease in ph
Temp
2,3 BPG
Exercise

Shift to left lower p50

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

Release of oxygen from hgb is enhanced when it is acidic (lowered ph and increase in carbon dioxide)

A

Bohr effect

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

Effect of changes in oxyhemoglobin on the CO2 content of pCO2

A

Haldane effect

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

Hb gower 1:_____;conception
HbF :_______;_______
Hgb A: bone marrow; _________
Hgb A2: ________;shortly after birth onwards

A

Yolk sac, conception
Liver, first few months to after birth
Marrow, 8months onwards
Marrow, shortly after birth

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

Chains
hbf :________
Hbg A:_________
Hbg A2:________

A

Alpha 2 gamma 2
Alpha 2 beta
Alpha 2 delata 2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

Major hgb found in fetus

A

Fetal hemoglobin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

HbAIC goal for non pregnant adults

A

<7%

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

Car, cherry pink
Unconscious

Dx?
Treatment?

A

Carboxyhemoglobin

Give 100% oxygen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
Q

Anxiety headache and dyspnea
“Chocolate cyanosis” with O2 saturation of 85%

Dx? Treatment?

A

Methemoglobinemia
Mild: oral methylene blue or ascorbic acid (reducing agents)
Acute massive: iv. Methylene blue

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q

Ankyrin mutation as the most common
Inherited defect in rbc membrane

Anemia
Splenomegaly
Jaundice

Diagnostic test? Dx?
Treatment?

A

Osmotic fragility test
Hereditary Spherocytosis
Splenectomy for symptomatic patients

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
54
Q

Point mutation in both genes for the beta chain that results in valine rather than glutamate

It causes painful crises due to occlusion of the misshapen RBCs however it is protective against malaria

A

Sickle cell disease

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

In hemoglobin C disease which amino acids are substituted?

A

Lysine is substituted for glutamate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
56
Q

Inadequate synthesis of alpha chains that leads to anemia and accumulation of Hb Bart (gamma 4) and Hb H (Beta 4)

Symptoms appear at birth

A

Alpha thalassemia

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
57
Q

Inadequate synthesis of beta chains accumulation of Hb Barts and alpha chain percipitation

Symptoms seen 6months after birth

A

Beta thalassemia

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
58
Q

Most abundant protein in the body?

Most common form?

A

Collagen

Type 1 collagen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
59
Q

What vitamin is needed in the hydroxylation of collagen?

A

Vitamin C

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
60
Q

Collagen is rich in ______ and ________

______ facilitates kinking

A

Glycine and proline

Proline

61
Q
Collagen type I: \_\_\_\_\_\_\_\_\_
Collagen type II: \_\_\_\_\_\_\_\_\_
Collagen type III:\_\_\_\_\_\_\_\_\_
Collagen type IV:\_\_\_\_\_\_\_\_
Collagen type VII:\_\_\_\_\_\_\_\_
A

bONE, tendONE, dentin, fascia, cOrNEa,late wound repair

carTWOlage, vitreous bidy, nucleus pulposus

ReTHREEculin, skin, blood vessels, uterus, fetal tissue, granulation tissue

Four=floor ; basement membrane or basal lamina

VII : stratified squamous epithelium

62
Q

Most common type of Ehlers-Danlos syndrome

A

Hypermobility - defect is in type III

There is hypermobile joints, skin abn, OA and severe pain

63
Q

Collagen defect in classical Ehlers-Danlos syndrome

A

Classical -type I and V

Hypermobility - type III (most common)
vascular - type III (most serious)

64
Q

Mutation in collagen genes result to brittle bones

Most common collagen defect?

A

Osteogenesis Imperfecta
Collagen type 1

Blue sclerae
Hearing loss
Multiple fx
Dental imperfections

65
Q

Genetic disorder affecting structure of collagen type IV: manifestations include hematuria, sensorineural hearing loss, ocular lesions

A

Alport syndrome “alFOURt”

66
Q

Skin breaks and blisters as a result of minor trauma

A

Epidermolysis bullosa

Type VII defect

67
Q

A pirate came to you for poor wound healing. What is your impression?

A

Vitamin C deficiency

Scurvy

68
Q

Patient presents with kinky hair (non familial) and growth retardation. What could be included in your impression if this is a nutrient deficiency?

A

Menkes disease due to copper deficiency

Copper is required by lysyl oxidase

69
Q

Elastin is rich in

A

Proline and lysine

Precursor tropoelastin deposited into irregular fibrilln scaffold crosslinked by DESMOSINE

70
Q
Mutation in fibrillin gene
Presents as tall per and thinner than family members
Arachnodactyly
Dolichostenimelia
Ectopic lentis
A

Autosomal dominant connective tissue disorder - marfan syndrome

71
Q

Most common cardiovascular defect in Marfan syndrome

A

Aortic dilatation in 79-80% and dissection

72
Q

Alpha 1 antitrypsin deficiency results in

A

PAN EMPHYSEMA

73
Q

Protein catalysts that increase the velocity of chemical reaction and are not consumed by the reaction they catalyze
They are highly specific and highly efficient
Can be inhibited or regulated

A

Enymes

74
Q

___________ are physically distinct versions of given enzyme, each of which catalyzes the same reaction

A

Isozymes

75
Q

Recyclable shuttles that transports substrates from point of gen to point of utilization

A

Coenzyme

76
Q

This describes how reaction velocity varies with substrate concentration

Assumes that:
s>e
ek
Low P

What equation? What curve?

A

Michael-Meneten equation

Hyperbolic curve

77
Q

Km is ______of Vmax

A

1/2 of VMax
Increase in substrate will increase in velocity until Vmax is reached
Even if substrate continues to rise Vmax will not change

78
Q

Increase in Km will _______affinity

A

⬆️ km ⬇️affinity

⬇️ km ⬆️ affinity

79
Q

Factors that affect rate of reaction (increase or decrease in reaction)

A

Concentration of substrate
Temprature
pH

80
Q

For a reaction to be spontaneous and favorable the change in energy shoul be

A

Negative

81
Q

Enthalpy :_________

Entropy: __________

A

Heat

Randomness

82
Q

How is atp produced?

A

Substrate level phosphorylation

Oxidative phosphorylation

83
Q

Two requirements for oxidative phosphorylation

A

Oxygen

Mitochondria

84
Q

NAD is derived from?

FAD is derived from?

A

Nicotinamide Adenine Dinucleotide- Niacin Vitamin B 3

Flavin Adenine Dinucleotide- riboflavin vitamin B2

85
Q

In electron transport chain, which is the final electron acceptor?

A

Oxygen

86
Q

In electron transport chain which enzyme is used to produce atp from adp after oxidative phosphorylation?

A

Atp synthase in complex V

87
Q

How many atps are yeild in one electron transport chain?

A

Nadh- 2.5

Fadh-1.5

88
Q

Which complex in the etc is succinate converted to fumarate?

A

Complex II

89
Q

Hypothesis re etc to produce ATP from ADP+Pi

A

Mitchell hypothesis

90
Q

Complex inhibitors

Barbiturates
Amytal
Rotenone
Piercidin A

A

Complex I

91
Q

Complex II inhibitors

A

*Malonate
Carboxin
TTFA

92
Q

Complex III inhibitors

A

Antimycin A

*Dimercaprol

93
Q

Complex IV

A

CaSHCy

Carbon monoxide
Sodium azide
Hydrogen sulfide
Cyanide

94
Q

If the mitochondria has a defect, which gene is it from? Mother or father

A

Mother for mitochondria

95
Q

Uncoupling protein important in babies

A

Thermogenin (brown fat)

96
Q

Synthetic uncouplers

A

2,4 dinitrophenol, aspirin

97
Q

Only atp synthase inhibitor

A

Oligomycin

98
Q

Inhibits oxidative phosphorylation by inhibiting adp and atp transporter

A

Atractyloside

99
Q

Name 3 ROS

A

Superoxide
Hydrogen peroxide
Hydroxyl radical

100
Q

Defenses against ROS accumulation

A

Catalase
Peroxidase
Superoxide desmutase

101
Q

Neither catabolic or anabolic. This process is amphibolic

A

Cirtic acid cycle

102
Q

What is the first substrate in krebs?

A

Acetyl co-a

103
Q

Second messenger of glucagon and epi (B,a2) ?Protein kinase?

A

cAMP -protein kinase A

104
Q

Second messenger of insulin and insulin growth factor ? Protein kinase

A

Tyrosine kinase

Tyrosine kinase/JAK -STAT

105
Q

Second messenger of nitric oxide and ANP? Protein kinase?

A

cGMP

Protein kinase G

106
Q

Second messenger of epinephrine (a1) and protein kinase?

A

IP3 /DAG protein kinase C

107
Q

Activates cAMP?

A

Adenylate cyclase

108
Q

Functions of carbohydrates

A

Major energy source
Storage of energy
Component of cell membrane
Structural components of plants and bacteria

109
Q

Glucose is reduced to ___________

Glucose is oxidized to ____________

A

Sorbitol

Glucoronic acid

110
Q

What are examples of monosaccharides?

A

Hexoses

Glucose (aldehyde) - sorbitol - glucoronic acid
Fructose (ketone)
Galactose (aldehyde)
Mannose

Pentoses

Ribose
Ribulose
Xylulose

111
Q

Examples of dissachrides

A

Sucrose (glucose +fructose)
Maltose (glucose+glucose)
Lactose (glucose + galactose)

112
Q

When a hydroxyl group is removed in C2 of ribose, this yeilds what?

A

Deoxyribose

113
Q

Storage polysaccharides in animals?

A

Glycogen

114
Q

Chief constituent of plant cell walls?

A

Cellulose

115
Q

Most important dietary carbohydrate in cereals and potatoes?

A

Starch

116
Q

Polysaccharide of fructose that is soluble in water and is used to determine GFR?

A

Inulin

117
Q

Where is glucose absorbed?

A

Jejunum and duodenum

118
Q

Glucose transporters and their functions

A

Needed for transport thru cell membrane because glucose is polar

GLUT 1 : BRAIN, colon, placenta, rbcs, kidneys
GLUT 2 : LIVER, PANCREAS, small intestines and kidneys
GLUT 3: BRAIN, kidneys, placenta
GLUT 4: MUSCLE AND ADIPOSE TISSUE (insulin stimulated glucose uptake)
GLUT 5: LUMEN OF small intestine (absorption of FRUCTOSE)

119
Q

Sodium dependent active uptake of glucose against a concentration gradient?

A

SGLT 1 in small intestines and kidneys

120
Q

Breakdown of glucose

A

GLYCOLYSIS

121
Q

What activates glucose?

A

Insulin

Fed state= increase glucose= insulin release= glycolysis

122
Q

Glycolysis

What for?

Where does it occur?

Substrate?

End products?

Rate limiting step?

A

What for?
Major pathway of glucose metabolism to provide energy

Where does it occur? Cytosol

Substrate? Glucose

End products? 2 molecules of either pyruvate or lactate

Rate limiting step? Phosphorylation of fructose-6-phosphate to fructose-1,6-biphosphate

ENZYME IS PHOSPHOFRUCTOKINASE-1

123
Q

Irreversible and important steps in glycolysis

A

Step 1: glucose to glucose-6-phosphate thru hexokinase or glucokinase

Step 3: fructose 6 phosphate to fructose 1,6 bisphosphate thru phospho-fructokinase -1

Step 10: Phosphoenolpyruvate to pyruvate thru pyruvate kinase

124
Q

Hexokinase vs glucokinase

A
Hexokinase present in most tissues
-Inhibited by glucose 6-p
-Low Km thus high affinity
-Low VMax
Meet cell need now
Glucokinase
- liver and the pancreas
- inhibited by fructose -6-p
- high Km low affinity
- high Vmax
For storage
125
Q

Product of PFK1? PFK2?

Activator? Inhibitor?

A

Product : Fructose 1,6 biphos : fructose 2,6 biphos
Activator: fructose 2,6 BP : well fed state
Inhibitor: citrate and ATP : fasting state

126
Q

Well fed state vs fasting state

A

Well fed state increase in insulin decrease in glucagon

Fasting state decrease insulin increase glucagon

127
Q

What are the two steps in glycolysis that produces ATP via substrate level phosphorylation?

A

1,3 Biphosphoglycerate to 3-phosphoglycerate

ENZYME: PHOSPHOGLYCERATE KINASE

phosphoenolpyruvate to pyruvate

ENZYME IS PYRUVATE KINASE

128
Q

ATP yeild of aerobic GLYCOLYSIS?

A

Consumed : -2
Substrate level yeild: 4
NADH : 3 (Glycerophosphate) 5(malate aspartate)

NET YEILD: 5 or 7

129
Q

Anaerobic glycolysis will yeild how many ATPs?

A

Consumed :-2
Substrate level :4
= 2

130
Q

End product of anaerobic glycolyis?

End product of aerobic glycolysis?

A

Lactate by lactate dehydrogenase

Pyruvate by

131
Q

Fate of pyruvate

A

Lactate -> Anaerobic glycolysis
Acetyl coa –> krebs cycle
Oxaloacetate -> gluconeogensis
Ethanol -> fermentation

132
Q

Coenzymes of pyruvate dehydrogenase

A

All 5 MUST BE PRESENT

Thiamine pyrophosphate (B1)
FAD (B2)
NAD (B3)
CoA (pantothenic acid) B5
Lipoic acid
133
Q

Most common enzyme defect in glycolysis

A

Pyruvate kinase deficiency which presents as hemolytic anemia

134
Q

Most common cause of congenital lactic acidosis

A

Pyruvate dehydrogenase deficiency

Treat with ketogenic diet

135
Q

Disease caused by a mutation that decrease the activity of glucokinase

A

MATURITY ONSET DIABETES OF THE YOUNG TYPE 2

136
Q

What vitamin is deficient in chronic alcoholism?

A

Vitamin B 1 or thiamine

Alcohol inhibits absorption of B1

137
Q

Final common pathway for aerobic oxidation of carbs, protein and lipids

A

Citric acid cycle

138
Q

TCA

what for?
Where does it occur?
Products?
Substrate?
Rate limiting step?
A

TCA

what for? Major pahway for formation of ATP

Where does it occur? MITOCHONDRIAL MATRIX IN MOST except for succinate dehydrogenase that occurs in the inner mitochondrial membrane

Substrate? Acetyl-Coa

Product? 2 CO2; 1GTP; 3NADH; 1FADH

Rate limiting step? ISOCITRATE TO ALPHA KETOGLUTARATE

ENZYME: isocitrate dehdrogenase

139
Q

Steps in the TCA CYCLE?

A

CINDY IS KIND SO SHE FORGIVES MORE OFTEN

citrate > isocitrate > alpha KETOGLUTARATE > succinyl COA > succinate>fumarate>malate>oxaloacetate

140
Q

ATP YIELD FOR TCA

A
NADH (2.5x3) = 7.5 ATP
FADH (1.5x1) =1.5 ATP
GTP = 1 ATP
\_\_\_\_\_\_\_\_\_\_\_\_\_\_\_\_\_\_\_\_\_\_\_\_\_
10 ATPs
141
Q

How many ATPs in Complete oxidation of glucose?

A

30 anaerobic

32 aerobic

142
Q

Pathways that occur in both mitochondria and cytosol?

A

Heme synthesis
Gluconeogenesis
Urea cycle

143
Q

Gluconeogensis

What for?
Where does it occur?
Product?
Rate limiting step?

A

Gluconeogensis

What for? To synthesize glucose from non carb source to Prevent hypoglycemia
Where does it occur? Mitochondria and cytosol
Product? GLUCOSE
Rate limiting step?
FRUCTOSE 1,6 BISPHOSPHATE TO FRUCTOSE 6-phosphate

144
Q

Carboxylase needs what vitamin to function?

A

BIOTIN

145
Q

Lactate formed in skeletal muscle is transported to the liver to be converted back to glucose

A

CORI CYCLE

146
Q

Enzyme responsible for converting ethanol to acetaldehyde?

A

Alcohol dehydrogenase

147
Q

Glycogenesis

What for?
Where does it occur?
Substrate?
Product?
Rate limiting?
A

Glycogenesis

What for? Synthesis of glycogen
Where does it occur? Liver, muscle and cytosol
Substrate? Alpha D glucose
Product? Glycogen
Rate limiting? Elongation of glycogen chains
Enzyme: glycogen synthase

148
Q

What structure is needed to start glycogenesis? It serves as a primer for glycogen synthesis.

A

Glycogenin