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Year 1 > MCP > Flashcards

MCP Flashcards

1
Q

What is the central dogma?

A

Describes the flow of genetic info: replication, transcription translation

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2
Q

What is the purpose of golgi apparatus?

A

Sort/transport proteins

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3
Q

What is the purpose of the endoplasmic reticulum?

A

Where cell membrane components are made and where post transcriptional modification

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4
Q

What bases are pyrimidal and why?

A

Thymine, uracil and cytosine
Because they have a singular ring

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5
Q

What bases are purines and why?

A

Guanine and adenine
Because they have a double ring

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6
Q

How are nucletides joined together in DNA?

A

Phosphodiester bonds between 5’ and 3’ carbon on the deoxiribose sugar ring

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7
Q

What does antiparallel strands mean?

A

The strands are oriented with opposite polarities

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8
Q

What is a nuclesome?

A

Structure of beads of DNA in strings with histones

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9
Q

Why is the lagging strand known as that and what are the fragments called?

A

It is a discontinuous joining process which includes Okazaki fragments

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10
Q

What enzymes required in leading strand DNA replication?

A

Primase begins replication at fork and then followed by polymerase

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10
Q

What property of DNA polymerase leads to very few errors?

A

It is self correcting and any mistakes are cleaved and corrected (proof reading)
Has 2 sites for polymerizing and correcting

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11
Q

How does the lagging strand replication differ to leading?

A

Multiple primers required so Okazaki fragments can be formed, joined by DNA Ligase. DNA polymerase builds fragments on 3’ end of primer.

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12
Q

What are the proteins involved in DNA snyth known as?

A

The replication machine

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13
Q

What are the types of RNA and there purposes?

A

mRNA (proteins)
rRNA (Ribosomal structure and catalyze protein synth)
miRNA(Regulate gene expression)
tRNA (adaptor of mRNA and amino acid)

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14
Q

What are the uses of non coding RNA?

A

RNA splicing
Gene regulation
Telomere maintenance
More

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15
Q

What are similarities between RNA polymerase and DNA?

A

Catalyze Phosphodiester bonds
Only adds in 5’-3’ direction

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16
Q

What are differences between RNA polymerase and DNA?

A

RNA doesnt need helicases
No primase required RNA
New RNA not attached to DNA
RNA no proof reading
RNA less accurate (1 in 10^4 vs 10^7 error)

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17
Q

Where does RNA transcription begin and end?

A

Promoter (A/T) and terminator (G/C) regions cause RNA polymerase to act
Template strand always runs 3’-5’

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18
Q

How does the RNA polymerase recognize promoters and disconnect at terminators?

A

Sigma factor on polymerase regonises and detaches beginning transcription
Reaches terminator then RNA polymerase release RNA and DNA

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19
Q

What are the types of RNA polymerases and what do they synthesize production of?

A
  1. Most rRNA genes
  2. All protein coding genes, miRNA genes and other non coding DNA
  3. tRNA, 5S rRNA genes and other small RNA genes
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20
Q

What is the role of transcription factors in RNA polymerase and transcription?

A

They are groups of proteins that bind to promoter. They position the RNA polymerase and pull apart double helix.

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21
Q

What is the region that transcription factors bind to?

A

TATA box (promoter regions), DNA sequence rich in AT

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22
Q

How is produced mRNA processed?

A

1.RNA capping at 5’ end
2.RNA polyadenylation at 3’-end. Add poly-A tail
3. RNA splicing

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23
Q

When and where does capping occur in RNA?

A

After Roughly 25 nucleotides at 5’

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24
Q

What does RNA polyadenylation do?

A

Adds a tail of repeated adenine nucleotides at the 3’ end

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25
Q

What is another unit describing molecular weight of a protien?

A

Dalton (Da) (g/mol)

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26
Q

Where and how are amino acids attached to RNA molecule?

A

3’ end and they are covalently attached

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27
Q

What is a ribsome made of?

A

4 rRNA molecules and more than 80 proteins

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28
Q

What is the order of binding sites on a ribosome?

A

E , P, A

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29
Q

What is first step in addition of an amino acid to a forming polypeptide chain?

A

Appropriate tRNA enters the A binding site pairing with complementary codon, no bases in-between A and P sites

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30
Q

How is a peptide bond formed in translation?

A

Carboxyl end uncoupled from tRNA molecule of p site amino acid and a peptide bond formed between carboxyl of P and amino of A.

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31
Q

What catalyzes the formation of peptide bonds?

A

The enzymatic site in the large sub unit of the ribsome

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32
Q

When and how do the sites change in translation?

A

Once a peptide bond formed large sub unit shifts the P site t-RNA moves to E, A site moves to P

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33
Q

How does E site eject spent tRNA

A

Small sub unit moves along with large back to original position, and the e site is ejected and translation can repeat.

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34
Q

What can denature protiens?

A

Heat
pH
High Salt
Detergent

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35
Q

What interactions occur between proteins and amino acids molecules?

A

Disulfide bridges (cysteine)
H bonds
Electrostatic attraction
VDW forces
Covalent bonds

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36
Q

What are the cell-cycle times in early frog embryo, yeast, intestinal epithelial cells and mammalian fibroblasts in culture?

A

Frog 30 mins
Yeast 1.5 hours
Intestinal 12 hours
Fibroblasts 20 hours

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37
Q

What are the Stages of the cell cycle?

A

(G0)
G1 phase
S phase
G2 phase
M phase

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38
Q

What are the checkpoints for mitosis to begin?

A

Is all DNA replicated?
Is all DNA damage repaired?

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39
Q

What are the checkpoints for Anaphase and S phase to begin?

A

Anaphase: Are all chromosomes attached to mitotic spindles?
S Phase: Is the environment favorable

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40
Q

How do cyclin-dependent kinases cause cell cycle progression?

A

CDK activates cyclin, the cyclin accumulates and the cyclin conc is greater than that of active CDKs and next stage begins

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41
Q

What options are available to a cell between G1 and S phase?

A

Proceed to S
Pause
Withdraw to G0
Permanently withdraw and terminally differentiate

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42
Q

What is happening in phase G0?

A

G0 is the resting phase

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43
Q

What happens in G1 phase?

A

Mitogen stimulate cell proliferation. They do this by activating G-CDK and G1/S-CDKs.

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44
Q

How do G-CDK and G1/S-CDK stimulate proliferation?

A

They phosphorylate Rb protein (C1 cycle checkpoint), which then detach from transcription factors and lead to gene transcription

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45
Q

What happens in the M phase?

A

Mitosis and cytokinesis

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46
Q

What changes occur in interphase?

A

Interphase: Cells inc in size, DNA replicatied and centromeres duplicate

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47
Q

What happens in pro-metaphase?

A

Pro: Nuclear envelope disappears, chromosomes attach to mitotic spindle via kinetochores

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48
Q

What happens in anaphase?

A

Duplicated chromosomes separate and migrate toward poles of cells.

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49
Q

What happens during prophase?

A

Prophase: Chromosomes condense, mitotic spindle formed after reassembling microtubules

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50
Q

What happens in metaphase?

A

Meta: All chromosomes aligned at equator of spindle

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51
Q

What causes movement of chromosomes in Anaphase?

A

The kinetochores microtubules shortening and spindle poles moving outward.

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52
Q

What happens in Telophase?

A

Nuclear envelope reassembles and chromosomes reach spindle poles, 2 new nuclei developing

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53
Q

What happens during cytokinesis?

A

One cell divides into 2, an actin ring is formed which pinches cell into 2 daughter cells

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54
Q

How do cells communicate with eachother?

A

Sending cells release ligands which bind to receptors only found on target cells

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55
Q

What are the major components of tissues?

A

Cells and extracellular matrix proteins

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56
Q

What 3 things required for tissue engineering?

A

Scaffold, cells and growth factors/bioactive molecules

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57
Q

What is the purpose of Extracellular matrix proteins?

A

ECM proteins framework for tissues, cells receive adhesion cell signaling from ECM proteins (how cell are linked togther)

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58
Q

What is the most abundant Extracellular matrix protein and its organisation?

A

Collagen
Forms single polypeptide chains, then triple stranded molecules, then collagen fibrils and then fibers

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59
Q

How do cells bind to Extracellular matrix proteins?

A

Through integrin proteins and fibronectin. Fibronectin outside cell binds to collagen fibrils and integrin proteins in membrane bind to fibronectin.

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60
Q

Where are the stem cells in lumen located and what is there purpose?

A

4th cell from bottom
To be self renewable and differentiate into other cell types

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61
Q

What are embryonic stem cells and how can they be used in vitro?

A

Stem cells that can differentiate into any cell type and proliferate infinitely
They can be used to produce organs

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62
Q

What are induced pluripotent stem cells and their purpose?

A

Making embryonic stem cells from adult cells allowing production of non-proliferating cells without immune rejection

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63
Q

What is cancer and metastasis?

A

Cancer: The disruption of orchestrated tissue manner (UNREGULATED PROLIFERATION)
Metastasis: movement of cancer around the body

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64
Q

Why do cancer cells form?

A

1.Multiple hit hypothesis: mutations increases proliferation, leads to further mutation until it becomes invasive
2.DNA damage (UV/ageing)
3. DNA copy error

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65
Q

What genes effect cancer and how?

A

Oncogenic turning on increases cancer
Onco-suppressive turning off increases cancer
Immunosuppressive turning on inc cancer

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66
Q

What treatments are there for cancer and what is key for their success?

A
  1. Surgery (pre-metastasis)
  2. Radiotherapy
    3.Chemotherapy
  3. Immunotherapy
    EARLY DIAGNOSIS
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67
Q

How does immunotherapy help fight cancer?

A

1.Educate immune system to recognize cancer cells
2. Activate immune response to cancer cells
3. Cancer cells killed by immune system (usually does but is overwhelmed)

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68
Q

What are the shapes of bacteria?

A

Spherical (cocci)
Rod (bacilli)
Spiral (Spiralli)

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69
Q

What are the sizes of mammalian cells and Ecoli

A

Mammalian cell 10-20 um
E Coli 2um

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70
Q

What are the 4 ways of genes changing?

A

Intragenic mutation
Gene duplication
DNA segment shuffling (parts of genes swap)
Horizontal transfer (genes transferred among organisms)

71
Q

What is a gram negative cell wall?

A

Peptidoglycan cell wall in periplasmic space surrounded by outer membrane with O specific side chains

72
Q

What is a gram positive cell wall?

A

Lacks outer membrane but surrounded by Peptidoglycan layer thicker than gram negative

73
Q

What are some gram negative bacteria?

A

E.Coli
Pseudomonas aeruginosa (lung inf and uti)
Klebsiella (meningitis)
Gonorrhoeae
Acinetobacter baumanni (injured soldiers)
Enterbacteriaceae (uti, lung inf and blood inf)

74
Q

What are some gram positive bacteria?

A

Staphylococci
streptococci
Pneumococci
Corynebacterium diphtheriae (anthrax)

75
Q

What are cyanobacteria ?

A

Bacteria that fix nitrogen and CO2 from atmosphere, are photosynthetic and used to produce biofuels

76
Q

What is the purpose of a cytoskeleton in a cell?

A

For directed cell movements

77
Q

What are uses for insect cells in bioengineering?

A

More than 100 insect cell lines available for protein production and post translation modification of proteins also possible

78
Q

Amphipathic lipids and neutral lipids what are the differences?

A

Amphipathic are polar molecules (phospholipids)
Neutral and non polar (triglycerides)

79
Q

How are lipids classified and some examples?

A

COMPLEX LIPIDS: MEMBRANE (phospholipids, glycolipids and archaeal ether lipids)

STORAGE
(Triacylglycerols)

80
Q

What are the properties of fatty acids?

A

Solubility decreases as chain length increases
Melting point decrease as chain length inc or inc as C=C inc

81
Q

How can lipids structure themselves in water and how is it decided?

A

Micelle
Bilayer
Vesicle
By type of lipid and concentration

82
Q

What is the use of artificial membranes?

A

To create transport vessels for drug delivery/ gene therapy

83
Q

What is an integral and peripheral protein in the membrane?

A

Integral imbedded through full length of the membrane and peripheral doesn’t fully pass through

84
Q

How are peripheral proteins linked to the membrane?

A

Electrostatic/hydrogen bonds with lipids or integral proteins, at the polar head

85
Q

How are amphitropic and GPI linked proteins connected to membrane?

A

Conditionally attached by covalent interaction with lipids/carbohydrates or non covalently linked to lipids or proteins, these interactions are reversible

86
Q

What are the different types of integral proteins?

A

Monotopic: interact with one layer of membrane
Polytopic: Transverse (interact with both layers)

87
Q

How are integral proteins attached to membrane and how can they be removed?

A

Tightly associated with the hydrophobic region of membrane
Removed by detergents and exit with phospholipids attached.

88
Q

How do lateral and transverse diffusion of phospholipids in the membrane differ?

A

Lateral diffusion is very fast uncatalyzed
Transverse is very slow

89
Q

What enzymes catalyze the transverse diffusion and how to they differ in action?

A

Flippase: Moves phospholipid (PL) from outer to cytosolic leaf(inside) (ATP ACTIVE)
Flopase: Move PL from inside to out (ACTIVE)
Scarmblase: Moves lipids in either direction, controlled by eqb

90
Q

What is membrane fusion and what are some examples?

A

Membranes fusing without exposure of lipids to to aqueous solvent
Fusion of sperm and egg, viral infection, vesicles forming

91
Q

What causes membrane fusion?

A

It can be spontaneous or protein mediated

92
Q

What is the difference between primary and secondary active transport?

A

Both against electrochemical gradient but PRIMARY uses ATP and SECONDARY uses carrier molecules

93
Q

How to V0V1 and F0F1 ATPASE differ?

A

ATP used in V0V1 to pump protons into vacuoles and lysosomes
Electrochemical used in F0F1 for movement of protons

94
Q

What are the tools used to engineer biological processes?

A

DNA
RNA
Proteins
Enzymes
Metabolism (pathways)

95
Q

How is DNA edited?

A

DNA synthesis and chemical synthesis of the desired DNA

96
Q

How is DNA copied ?

A

Copied by polymerase chain reaction: lots of free nucleotides, primers DNA denatured into dtrands, primers attach then replicated DNA

97
Q

How is DNA cut, pasted and read?

A

CUT by restriction enzymes if different length end with P group (sticky) if both same (blunt), also done using CRISPRras9 to trim
PASTED using ligase to join cut molecules together
READ by sequencing

98
Q

How can RNA be bioengineered?

A

Transcription engineering by synthesising promoter
OR
Creating ribosome binding sites on RNA molecules

99
Q

How can E.Coli be altered to fix atmospheric CO2?

A

Introducing rubisco and PRK from organic sources along with enzyme to get energy from methanol

100
Q

How can Yeast be altered to fix atmospheric CO2?

A

Make the yeast preform the Calvin cycle (add enzymes) which used CO2 and produces useful organic products

101
Q

How can a drug be synthesized using metabolic engineering and an example?

A

Put specific genes in yeast which allow it follow metabolic pathway to produce drugs
Anti malaria drugs (artemisin)

102
Q

How can engineering improve enzyme efficiency?

A

Increase amount of native enzyme, overexpress enzyme with more promoters and increase the amount or truncated enzyme to prevent negative feedback

103
Q

What are the advantages of microbial oils vs plants bio oils?

A

Not competitive for food
Shorter process cycles
Independent of climate and season
Easily scalable vs plants
Easier to metabolically engineer

104
Q

What are microbial oils and their disadvantages?

A

Oils derived from microbial sources
Expensive sugars for food
Aseptic conditions

105
Q

What is the definition of metabolism, catabolism and anabolism?

A

Meta: All chemical reactions within a cell
Cata: Energy yielding metabolism
Ana: Biosynthetic metabolism

106
Q

What are examples of catabolism?

A

Sugar metabolism
Oxidative phosphorylation
Amino acid catabolism
Fatty acid catabolism
TCA cycle

107
Q

What are the role of ATP/ADP , GTP/GDP ,NADH/NAD+ and FAD,FADH

A

ATP, GTP are energy releasing molecules
NADH,FAD have reducing power/ electron source

108
Q

What are the processes that breakdown Fatty acids and Amino acids into products for TCA cycle?

A

AA: AA degradation either into the TCA cycle or Acteyl CoA
Lipids: Beta-oxidation into Acetyl-CoA

109
Q

What enzyme catalyzes conversion of Glucose to Glucose 6-phosphate and what regulates the amount?

A

Hexokinase
Regulated by if Pi conc inc then more converted if G6P conc inc then negative regulation

110
Q

What enzyme involed in conversion of G6P into Fructose 1,6-biphosphate and how is it regulated?

A

Phosphofructokinase-1
Positevly regulated by AMP and ADP
Negatively regulated by ATP and citrate

111
Q

What enzyme catalyzes last step of glycolysis Phosphoenolpyruvate into Pyruvate and how is it regulated?

A

Pyruvate Kinase
Positively regulated by ADP
Negatively regulated by ATP and NADH

112
Q

What molecule is used in glycogenesis and produced glycogenolysis?

A

G6P

113
Q

What is the yield of energy per glucose in glycolysis?

A

2 ATP molecules
2 NADH
2 pyruvate

114
Q

What does each pyruvate molecule produce in the citric acid cycle?

A

2 CO2
1 GTP
3 NADH
1 FADH2

115
Q

How is pyruvate converted to Acetyl CoA?

A

Catalyzed by pyruvate dehydrogenase complex

116
Q

Why does ADP -> ATP reaction need oxidative phosphorylation to occur?

A

It is thermodynamically very unfavorable

117
Q

What is the proton-motive force equation?

A

PMF = chemical potential (Delat pH) + elctrochemical potential

118
Q

How much ATP can be produced per NADH and FADH2 molecule

A

NADH = 10
FADH2 = 6

119
Q

What is the proton motive force used for?

A

To move protons across membrane down electrochemical gradient out of inner mitochondrial membrane

120
Q

What regulates oxidative phosphorylation?

A

Positively regulated by ADP and Pi conc

121
Q

What is a use of TCA for bioengineers?

A

To produce molecules (succinate) which can be used in other processes such as bioplastic production

122
Q

What is the difference between glucogenic and ketogenic amino acids?

A

Glucogenic: Enter straight into TCA cycle or pyruvate
Ketogenic: Converted into Acetyl-CoA

123
Q

How many Acetyl-CoA and Co-Enzymes produced by beta oxidation of fatty acids?

A

Produces amount of Acetyl-CoA equal to chain length over 2.
And equal amounts of FADH2 and NADH

124
Q

Why are enzymes > inorganic catalysts?

A

Greater reaction specificity
Milder reaction conditions
Capacity for regulation
Higher reaction rates
Control of biological pathways

125
Q

What are cofactors and coenzymes?

A

Factors: inorganic ions which are covalently linked as a prosthetic group
Enzyme: Organic or metalorganic ions

126
Q

What is the difference between holoenzyme and and apoenzyme?

A

Holoenzyme is a catalytically activated enzyme bound to its cofactor
Apoenzyme doesnt have the cofactor

127
Q

What effect do enzymes have on Delta G?

A

None as dont effect eqb

128
Q

What is Eyring equation?

A

k =(KbT)/ (exp -Delta G/RT)
h
Kb is Boltzmann constant
h is Planck’s number

129
Q

What are the 3 catalytic mechanisms?

A

Acid-base catalysis: giving/taking protons
Covalent: Forms temporary covalent bond
Metal ion catalysis: Facilitate binding, stabilize - charges ,redox reactions (1/3 enzymes need M+)

130
Q

What are the equations for total enzyme and substrate in a reaction mixture?

A

E tot = [E] + [ES]
S tot = [S] + [ES] ~ [S]

131
Q

What is the steady state assumption of enzyme kinetics?

A

Rate of change in [ES] is 0 as formation rate = breakdown rate

132
Q

What is the Km equation?

A

Km = (k-1 +k2 )/
k1

133
Q

What is the eqaution for the velocity of an enzymatic reaction?

A

v = vmax [S]
Km + [S]

134
Q

What do Kcat and Km represent?

A

Kcat is the number of substrate molecules an enzyme can convert per second (turnover number)
Km is the Michaelis constant and measures substrate affinity for the enzyme

135
Q

What is the catalytic efficiency equation?

A

Kcat/Km = catalytic eff

136
Q

How to determine Km graphically?

A

It is half of Vmax on a Michaelis Menten plot

137
Q

What does the gradient, y intercept and x intercept represent on a Lineweaver Burk plot?

A

Gradient = Km / Vmax
Y inter = 1/Vmax
X inter = -1/Km

138
Q

When would a Lineweaver-Burk plot be preferred to a Michaelis Menten?

A

Michaelis Menten good for calculating Km and Vmax but you would use a Lineweaver-Burk for 2 substrate data or inhibtion

139
Q

Why would the velocity equation for enzymatic reaction not be accurate?

A

Limitations of measurement
OR
Prescence of an inhibtor

140
Q

What is a reversible/irreversible inhibitor?

A

Reversible binds to and can dissociate from enzyme, often structurally similar to sub
Irreversible react with enzyme and permanently stop enzyme

141
Q

What are the properties of competitive inhibtor and its effect on Lineweaver-Burk plot?

A

Binds with active site but doesn’t affect function
No change in Vmax but increases Km
Changes x intercept as -1/km and gradient

142
Q

Properties of uncompetitive inhibition and how it effects LB plot?

A

Only binds to the E-S complex and inhibits enzyme function
Vmax decrease and Km decrease but gradient remains constant (Parallel lines)

143
Q

What is mixed inhibition and effect on LB plot?

A

Binds to enzyme w/o or with substrate at regulatory site
Inhibits binding and catalysis
Vmax decrease and Km inc

144
Q

How can enzymes activity be regulated by bioengineers?

A

Covalent modification
Non-covalent modification (allosteric): +/- effectors, generally small chemicals
Enzyme abundance (gene expression, enzyme degradation)
Substrate conc (Transporters or metabolism)

145
Q

What RNA does type 1 RNA polymerase produce?

A

Most rRNA

146
Q

What RNA does type 2 polymerase produce?

A

All protein coding genes, miRNA genes and other non coding DNA

147
Q

What RNA does type 3 RNA polymerase produce?

A

tRNA, 5S rRNA genes and other small RNA genes

148
Q

What happens to pyruvate produced in glycolysis in anaerobic conditions?

A

In animals fermented to lactate to regenerate 2 NAD+
Yeast 2 Ethanol + 2CO2

149
Q

When are the CO2 molecules released in TCA cycle?

A

Isocitrate -> Alpha ketoglutarate
Alpha Ketoglutarate -> succinyl coA

150
Q

When is GTP released in TCA cycle?

A

Succinyl-CoA -> Succinate

151
Q

What step in TCA cycle produces FADH2?

A

Succinate -> Fumarate

152
Q

What steps produce NADH in TCA cycle?

A

Isocitrate -> Alpha ketoglutarate
Alpha ketoglutarate -> Succinyl-CoA
Malate -> oxaloacetate

153
Q

What molecules positively regulate TCA cycle?

A

Ca2+, ADP, AMP, CoA all positively regulate

154
Q

What molecules negatively regulate TCA cycle?

A

ATP, Ach-CoA, NADH fatty acids and molecules involved negatively regulate

155
Q

What complexes involved in oxidative phosphorylation of NADH?

A

Complex 1 -> 4

156
Q

Complexed involved in FADH oxidative phosphorylation?

A

Complexes 2 -> 4

157
Q

What reaction happens at complex 1 in oxidative phosphorylation?

A

Electron from reduction of NADH releases energy to move 4H+ out of matrix and 2 H+ combine with carrier

158
Q

What reaction happens at complex 2 in oxidative phosphorylation?

A

FADH2 from succinate to fumarate releases energy to enter transport chain and add 2H to transport

159
Q

What reaction happens at complex 3 in oxidative phosphorylation?

A

Energy from redox reaction of carrier molecule moves 2H+ across membrane and the reaction releases the 2 added previously

160
Q

What reaction happens at complex 4 in oxidative phosphorylation?

A

Cyt c moves and provides energy for water synthesis and movement of 2H+

161
Q

What is the equation for gluconegenesis?

A

2 pyruvate + 4 ATP + 2GTP + 2NADH -> Glucose + 4 ADP+ 2GDP + 6 Pi + 2 NAD+

162
Q

Steps of sucrose synth?

A

UDP-Glu + F6P to
Sucrose-6-P (and UDP) to
Sucrose (and Pi)

162
Q

Steps of Starch synthesis?

A

G6P to G1P (+ATP) to ADPglc to starch and ADP

163
Q

What are the condensation and dehydration reactions involved in the catalyzed steps of fatty acids?

A

Condensation: of growing chain with activated acetate
Dehydration: Alcohol to trans-alkene

163
Q

What is the role of Thioesterase in fatty acid synth?

A

Releases the fatty acid from ACP

164
Q

What amino acid is the precursor for purines and pyrimidine synth and which provides amino groups?

A

Purine = Gly
Pyrimidines = Asp

Amino groups Glu

165
Q

What is the purpose of ACP’s in fatty acid synthesis?

A

To carry fatty acid molecule to the next step of cycle

166
Q

What are the reduction reactions in fatty acid syntehsis?

A

Reduction: carbonyl to hydroxyl
Reduction: C=C to C-C

167
Q

What version of glycerol is used in lipid synthesis and what are its sources?

A

Glycerol-3-Phosphate
Reduction of glycolysis product
Phosphoralyation of glycerol

168
Q

Where does lipid synthesis take place and why?

A

Endoplasmic reticulum the membrane contains enzymes required (GPAT,LPAAT,PAP,DGAT)

169
Q

What is the difference between phospholipid synthesis and Triglyceride?

A

Phospholipid has 2 fatty acids added at ER and Triglyceride 3

170
Q

What is the intermediate before formation of phospholipid?

A

Phosphatidic acid

171
Q

How does amino acid synthesis differ in bacteria and mammals?

A

Mammals cant synthesize all necessary amino acids

172
Q

What 5 molecules (involved in sugar anabolism) can make amino acids in mammals?

A

Erthyrose-4-phosphate
Ribose-5-Phosphate
Pyruvate
Alpha-ketoglutarate
Oxaloacetate

173
Q

What are the prosthetic group co-enzymes in pyruvate dehydrogenase?

A

FAD, TPP and lipollysine

174
Q

What are the co-substrates in Pyruvate Dehydrogenase complex?

A

NAD+ and CoA-SH

Year 1 (5 decks)

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