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introduction
1.1. Definition
A. Biochemistry: Biological Chemistry, Physiological Chemistry
Chemistry
General Chemistry
Organic ChemistryLast parts
Inorganic Chemistry
Physical Chemistry
Quantum Chemistry
B. Biochemistry
Structures of Biomolecules
Bioenergetics
Functions of Biomolecutes
Biomolecules: Large and small molecules
Large ones: Macromolecules like DNA, RNA , proteins and polysaccharides
Bioenergetics: Energy flow in the living cells
C. Conformation: 2 conformations of ethane
Eclipsed
Staggered
1.2. Road to modern biochemistry: Page 8 Fig 1.2
1.3. Biological Macromolecules: Page 12 Fig. 1.6
A. Starch and Cellulose: Homopolymers of Glucose
B. Proteins: Heteropolymers of Amino Acids :
Acids containing amine groups
C. Nucleic Acids: Heteropolymers of Nucleotides( dAMP AMP, dGMP GMP, dTMP
UMP, dCMP, CMP)
1.4. Organelles, Cells and Organisms
A. Archaebacteria: Methane bacteria
B. Prokaryotes: Pro-Before, Karyon- nuts or kernel
Page 16 Table 1.1
C. Eukaryotes: Eu- Good or well
Human body digestive system Liver Hepatocytes Nucleus Chromatin
DNA Nucleotides Base, sugar and phosphate C, H, O, N Page 19 Fig. 1.11
Page 21 Table 1.2
1.5 Life at the Extremes: Page 16 Window on Biochemistry
1.6 Handling cell components: Page 24 Window
Chapter 2. The flow of biological
information: Cell communication
2.1. Brief Image of information flow: Page 30 Fig. 2.1
Transcription
Translation
2.2. Storage of Biological information in DNA
Genome: The total genetic informational content for each
cell
Exact duplication
Expression of stored information
DNA molecules
Watson and Crick in 1952: Double helix structure
Complementary base pairs by specific hydrogen bondings: C-G and A-T
C-G: triple hydrogen bonds A-T: double hydrogen bonds
Bases: inside the helix , the backbone : sugar and phosphate
Human Genome Project
To map and sequence the estimated 3 billion nucleotide base pairs
Other living organisams: Bacillus subtilis, Caenorhabditis elegans, Yeast,
Arabdopsis thaliana, Rice
30,000-40,000 genes in the human genome
Proteomics: The name given to the broad field investigating the thousands
of protein products from the genome
Bioinformatics: Computer applications to organize the mass of nucleic
acid sequence data and studying relationships between protein sequence and
structure.
2.3 Replication
5 to 3, Semi conservative replication
DNA polymerases
Polymerase Chain Reaction (PCR)
2.4 Transcription
Double helix DNA, RNA polymerase
rRNA, mRNA, tRNA: Page 35 Table 2.1
2.5 Translation
Genetic code: triplet code Page 38 Fig. 2.7
Exons and introns
Introns are absent in prokaryotes
RNA processing: Page 38 Fig. 2.8
Catalytic RNA
2.6 Errors in DNA Processing
DNA mutations: sickle cell anemia and other inborn metabolic errors
2.7 Information flow through cell membranes
A. Signal transduction:
B. Second Messengers: cAMP, cGMP, Ca2+
2.8 Drug design:
Page 44 Fig 2.11
A. Interference of Protein synthesis including transcription and translation
B. Receptor binding to block the initiation
C. Disruption of Signal pathway
Chapter 3 Biomolecules in Water
Water content: Page 48 Table 3.1, 71-83%
3.1 Water the Biological Solvent
Weaker interactions: noncovalent bonds- 1-30kj/mole (cf.
350kj/mole for C-C bond) Page 50 Table 3.2
Neutral 1 1 0 +1 0 + + Second
D. Quaternary structure
Monomeric, oligomeric
Subunits
4.4. Hemoglobin
A. Heme globin
B. Heme binding to globin
C. Oxygen binding: Page 115, Fig. 5.19
Sigmoidal curvePositive cooperation( Myoglobin: Hyperbolic)
D. Bohr effect: Page 115 Fig. 5.20
H+ and CO2 decrease the affinity of hemoglobin for oxygen molecule
4.5. Fashionable hair: Page 114, Windo
Chapter 5. 6. Enzymes 1
6.1 Biological catalysts
A. Catalysts: Page 127 Fig
6.2
B. Cofactor- in addition to the protein component, another
chemical entity , in order to function properly.
Metal ions- Zn+2, Mg+2
Coenzymes: Orgnometallic molecules
C. Prosthetic groups: cofactor covalently bonded to the proteins
Holoenzyme: protein + cofactor
Apoenzyme: without cofactor
E. Classification : Page 129 Table 6.2
6.2 Enzyme Kinetics
A. Michaelis Menten equation derivatisation
k2 k4
E + S ES E + P
k1 k3
ES formation rate: k1[E][S] + k4[E][P], often k4 is very small to be neglected.
ES degradation rate: k3[ES] + k2[ES]
At Steady state: Rate of formation = rate of degradation
k1[E][S] = k3[ES] + k2[ES]
[E]total = [E] + [ES]
k1([E]total-[ES]) [S] = [ES](k3 + k2)
k1[E]total[S]-k1[ES][S] = [ES](k3 + k2)
k1[E]total[S]= [ES](k3 + k2) + k1[ES][S]
[ES]( k3 + k2 + k1[S]) = k1[E]total[S]
[ES] = k1[E]total[S] / ( k3 + k2 + k1[S])
[ES] =[E]total[S] / ( k3 + k2)/k1 +[S])
(k3 + k2)/k1 = Km
[ES] =[E]total [S] / ( Km +[S])
dP/dt = Vo = k3[ES] =k3[E]total[S] / ( Km +[S])
k2[E]total = Vmax
Vo= Vmax [S]/(Km + [S])
B. Km: If V = 1/2 Vmax, Km =[S]
C. Turnover number = Vmax/[E]total
D. Lineweaver-Burk Equation
From Vo= Vmax [S]/(Km + [S])
1/Vo = (Km + [S])/Vmax[S]
1/Vo = Km/Vmax 1/Vmax + 1/Vmax Page 134 Fig. 6.5
E. Characteristics of enzyme reactions
Enzyme concentration, pH, Temperature
6.3 Substrate binding and enzyme action
A. Active site
Lock and Key model; Page 137 Fig 6.10
Induced fit model: page 138Fig. 6.11
Transition state analog model: Page 138 Fig. 6.12
B. General Acid-Base catalysis: An Enzyme donates a proton and accept it in the
final step
Proton transfer to the carbonyl group
Water attack to from a tetrahedral intermediate
Acceptance of the proton from the intermediate
C. Metal ion catalysis:
Alkali metal ( Na+, K+) and transition metals ( Mg+2, Mn+2, Cu+2 Zn+2 Fe+2
Fe+3 Ni+2)
Hold a substrate properly oriented by coordinate covalent bonds ,
Page 140 Fig. 6.14 a
Polarize the scissile bond or stabilize a negatively charge intermediate. Fig. 6.14 a
Participate in biological oxidation-reduction reactions by reversible electron
transfer between metal ions and substrate. Fig. 6.14 a
D. Covalent catalysis
A nucleophilic functional group on an enzyme reacts to form a covalent bond with
the substrate. Page 140, Step 1 and 2
6.4 Enzyme inhibition
A. Reversible and irreversible inhibitors
DIFP, Pesticides
B. Reversible inhibitors: Page 145 Fig 6.19
Competitive inhibitors: Resemble the structure of normal substrate and
binds
to the active site of the enzyme
E+S ES E+P
+
I
EI
D. rRNA
Much larger than tRNA but shares many of the same elements as tRNA
10.4. Cleavage of DNA and RNA by nucleases
A. DNases, Rnases
B. Exonucleases, Endonucleases
C. DNA restriction enzymes
Recognize specific base sequences in double-stranded DNA : Palindrome
sequences
Eco R1, Hpa1 Bam H1
A. Spontaneous Mutations:
Mismatching of base pairs: 1/1010
The actual error rate of base incorporation during replication: 1/104-105
( Repair systems correct most mismatched base)
Base modifications caused by hydrolytic reactions
Nucleotieds containing purine bases can undergo spontaneous hydrolysis at the N-
glycosidc bond to remove the purine ring.
Deamination reaction: The conversion of cytosine to uracil
B. Induced mutations
Ionizing radiation
Chemicals: Heterocyclic base analogs : Page 286 Fig. 11.14
Alkylating agents: Page 286 Fig. 11.15
Intercalating agents: Flat, hydrophobic molecules that insert between stacked base
pairs in DNA: Page 287 Fig. 11.17
11.4. Synthesis of RNA:
The molecular vehicle carrying the genetic information from
DNA to protein synthesis.
A. Template strand: Sense strand: The strand of duplex DNA used as a template for
RNA synthesis
B. DNA-directed RNA synthesis
DNA-directed RNA polymerase: RNA polymerase
In Eukaryotic cells: RNA polymerase 1. II and III
large ribosomal RNA genes,
II. Protein-encoding genes,
III. Small RNAs including tRNA and 5S rRNA
Three steps: Page 291 Fig. 11.19
Initiation: subunit binds to RNA polymerase
subunit recognizes promotor
RNA polymerase binds to DNA
subunit dissociates from RNA polymerase
RNA polymerase begins to movealong the template strand
Elongation: Ribonucleoside triphosphates
Termination: factor interacts with RNA polymerase. Transcriptiion is terminated.
protein independent-GC-rich region, followed by an AT-rich region and a poly
A region
RNA, DNA, RNA polymerase and factor are released.
C. RNA-directed RNA synthesis: in RNA viruses( Q, MS2, TMV and R17)
11.5. Post-transcriptional modification of RNA
A. tRNA
Trimming of the ends by phosphoester bond cleavage
Ribonuclease P near the 5end of pre-tRNA,
An endonuclease remove a small section from the 3end of the tRNA
Splicing to remove an intron
Addition of terminal sequences: CCA
Heterocyclic base modification, usually methylation
B. mRNA
Capping: Page 295 Fig. 11.24
Almost immediately after synthesis, the 5 end of the mRNA is modified by hydrolytic
removal of a phosphate from the triphosphate functional group.
GMP addition via GTP to the 5end resulting in an unusual 5-5triphosphae covalent
linkage.
Methylation
Poly A addition
Addition of a poly A tail to the 3end of mRNA after removal of a few 3 base
residues
Splicing of coding sequences
Exons: Coding regions on the gene
Introns: noncoding regions
SnRNP and catalytic RNA participate in the splicing
11.6. Base sequences in DNA
A. Maxam-Gilbert chemical cleavage method
B. Sanger chain-termination sequencing method-
Dideoxy method Page 299 Fig. 11.27
Strands to be sequenced + short primer strand
DNA polymerase
dATP + dd ATP , dGTP + ddGTP, dCTP + ddCTP, dTTP + ddTTP Page 298
Fig. 11.26
Electorphoresis separating the reaction mixture according to the base size
Chapter 12. Translation of RNA : The
genetic code and protein metabolism
12.1. Process of protein synthesis
A. Characteristics of protein synthesis
Location: Ribosomal particles
Ribosomes :25nm, 2500 kDaltons, around 15,000 ribosomes in E coli cell
70S ( 30S + 50S) { Eukaryotes: 80S ( 60S +
40S)]
66% RNA and 34% protein Page 307 Fig. 12.1
Move along mRNA templates deciphering the code for conversion from
nucleotide to amino acid sequence
Bring to the template the tRNA charged with the properamino acid
Catalyze the formation of peptide bonds between amino acids using
ATP or GTP.
Protein synthesis begins at the N-terminus.
Aminoacyl-tRNA synthetases: an amino acid is covalently linked by an eser
bond to the 2 or 3OH end of a specific tRNA.
20 aminoacyl-tRNA synthetases, one for each amino acid.
Genetic codes: Page 311 Table 12.2
Triplets
Degenerative
Universal
12.2. Three stages of protein synthesis
A. Initiation:
Ribosomal recognition of the starting point on the mRNA and entry of tRNA-activated N-
formylmethionine(fMet)
mRNA + IF + 30S subunit GTP-IF + fMet on AUG of mRNA: 30S initiation complex
50S subunit attachment with hydrolysis of GTP and IF detachment.: 70S initiation
complex
B. Elongation
70S initiation complex, the next amminoacyl tRNA in the A ribosomal bind site and EF
Formation of the first peptide bond: Peptidyl transferase a ribozyme associated with the 50S
ribosome
Translocation using GTP hydrolysis and removal of deacylated tRNA from the codon region
The 3rd charged tRNA + GTP hydrolysis on the new formed A site
C. Termination
RF on stop codon and activation of peptidyl tranferase
Hydrolysis of the ester bond liknking the carboxyl group the newly synthesized protein to the
tRNA in the P site
70S ribosome dissociated into its subunits
D. Polysomes: Clusters of ribosomes on a mRNA molecule Making many identical proteins
molecules from a single copy of mRNA
E. Protein synthesis and Energy
Two anhydride bonds in ATP for aminoacyl-tRNA formation
One GTP for entry of each amino acid into the A site
One GTP during each translocation step
12.3. Post-translational processing of proteins
A. Protein folding
Chaperones: Catalysts to guide and facilitate folding
Some chaperones are enzymes that couple ATP hydrolysis to the protein
folding process.
B. Biochemical modifications
Proteolytic cleavage: N-formylmethionine removal
Zymogens
Amino acid modification: Phosphorylation and hydroxylation
Attachment of carbohydrates: Glycoproteins
-Serine or threonine
-amide nitrogen of asparagines
Addition of prosthetic groups: Heme, FAD, biotin and pantothenic acids
C. Protein targeting: How are proteins sorted and transported to their final
destination?
Signal sequence: -14-26 amino acids at the amino terminus
usually removed when the protein reaches its final destination
Basic region + Hydrophobic region + Nonhelical region Page 324 Fig. 12.12
D. Proteasome and protein degradation
Proteins are continuously being degraded and replaced by newly synthesized protein
molecules
Biological meanings:
-removal of damaged or misfolded proteins.
-Destruction of regulatory proteins not needed at the time
-Adaptation to changing conditions
Half life
-RNA polymerase: 1.3 minutes
-Hemoglobin: 100 days
Proteasome: Page 325 Fig. 12.14
-Degradation of unwanted intracellular proteins by ATP-dependent proteases associated
with large protein complexes
-26S complex (20S + 19S )
-Ubiquitin pathway: 76 Amino acids, covalent attachment by an ATP-dependent process
12.4. Regulation of protein synthesis and gene expression
A. E. coli: 4000 genes, Humans: 30,000-40,000 genes.
B. A fraction of genes is expressed at any given time.
C. Regulation steps of protein synthesis: page 326 Fig.12.15
But most gene expression is controlled a the level of transcription initiation-The number
of mRNA molecules
D. 2 types of gene expression
-Constitutive expression: continuous transcription, resulting in a constant level of certain
protein products- House keeping genes for general cell maintenance and central
metabolism
-Inducible or repressible expression: Activation and deactivation, resulting in an increase
or a decrease in mRNA and protein levels.
E. Principles of regulating gene expression
Operon model in prokaryotes: Page 326 Fig. 12.16
Operons: Genes for proteins that are related in
function are clustered into units on the
chromosome
Components of an operon
Structural genes: Genes to be transcribed
and translated
Promoter region: RNA polymerase binding
site
Regulatory protein binding sites
Activator binding site
Repressor binding site( Operator)
Binding domain of regulatory proteins
20-100 AA, Hydrogen bonds between
Lys, Arg, Glu, Asn,Gln and the bases in Major
groove in DNA
Three classes of regulatory proteins
Helix Turn Helix motif: Most
common in prokaryotes Page 329 Fig. 12.19
Zinc finger motif: found only in eukaryotes, Page 330 Fig.12.20
Leucine Zipper motif: Page 331 Fig. 12.22
Chapter 13: Recombinant DNA and
other topics in Biotechnology
Biotechnology:
Application of our understanding of the intricate workings of the cell to the solution of
practical problems
Examples:
Making of cheese, wine and other food commodities
Use of bacterial cells to produce large quantities of scarce proteins needed to treat
disease
Using enzymes to catalyze reaction steps in the industrial production of speciality
chemicals or biochemicals
Plant gene modification
Production of fuel alcohol from plant material
Using bacteria and plants for cleanup of chemical waste site: remediation
Mining of metals
Gene therapy: Gene replacement in individuals with genetic disorders
Forensic medicine
13.1. Recombinant DNA Technology
A. Molecular cloning
The covalent insertion of a DNA fragment
fro one type of cell or organism into the
replicating DNA of another type of cell
If the inserted fragment is a functional
gene carrying the code for a specific protein
and an upstream promoter region is present
in the DNA, Many copies of that gene and
translated protein are produced in the host
cell
Page 340 Fig. 13.1
B. Cloning Vectors
Vector: Carrier for the foreign DNA
Plasmid: Self-replicating , extrachromosomal DNA molecules
Circular, double stranded, 3000-30,000 base pairs
Contains genetic information for the translation of
proteins that confer a specialized and sometimes protective characteristic on the
organism
Under antibiotics, many copiesmay accumulate 30-
40% of the total cellular DNA
The typical plasmid will accept foreign DNA inserts
up to 15,000 base pairs.
PBR 322: 4363 base pairs are sequenced.
1 EcoR1 site, different restriction sites
Bacterophage DNA
Lamda phage
50,000 base pairs, double stranded
Many copies of recombinant phage DNA can be
replicated in the host cell
Efficient package of recombinant phage DNA into
virus particle
Lamda phage can accepts DNA fragments up to 23,000
base pairs
Yeast artificial chromosome (YAC), Bacterial Artificial
chromosomes (BAC)
13.2 Preparing recombinant DNA
A. Design of recombinant DNA Page 343 Fig. 13.4
Formation of poly T tail in Foreign DNA to be inserted
Linearization of plasmid and Poly A tails on it
Mixing the two and ligation with DNA ligases
B. Transformation and Selection
Incorporation of recombinant DNA into the host cell: 1/10,000 molecules is successful.
Selection markers: Drug resistances Page 345 Fig. 13.5 and 13.6
C. Isolation and cloning of a single gene
Identify, locate and sequence a specific gene that occurs only once in a chromosome.
-Genomic DNA is cut into many thousands of large fragments using restriction
endonucleases- a random population of overlapping DNA fragments
-Isolation of similar size fragments by EP or ultracentrifugation
- Formation of poly T tail in Foreign DNA to be inserted
Linearization of plasmid and Poly A tails on it
Mixing the two and ligation with DNA ligases
D. Transformation and Selection
Incorporation of recombinant DNA into the host cell: 1/10,000 molecules is successful.
Selection markers: Drug resistances Page 345 Fig. 13.8
E. Biochips: Page 348 Window
Microarray analysis
An orderly arrangement of experimental samples
Data interpretation
Nucleic acids:
Ordered sets of DNA( 1,000 samples) with fluorescent tag fixed at discrete locations
on the solid surface of a glass (silicon) chip by robotical deposition
Formation of a hybrid generates a fluorescent spot at a definite site on the chip
Identification of paired sequences in cDNA and mRNA
Proteins: Protein microarray
Specific protein protein interactions ( Antibodies)
Protein Drug interactions
Determination of expressed level of the genes
13.3 DNA amplification by Polymerase chain reaction
Requirements
2 synthetic oligonucleotide primers about 20 bases, which are complementary to the flanking
sequences II and IV
A heat stable DNA Polymerase: Taq (Thermus aquaticus) DNA polymerase
dATP. dGTP, dCTP, dTTP
DNA template
Protocol Page 350 Fig. 13.10
5---CCCGGG------------TTTAAA---3
AAATTT:
3---GGGCCC------------AAATTT---5 CCCGGG
5--CCCGGG-------------TTTAAA---3
3---GGGCCC------------AAATTT-5
3--GGGCCC-------------AAATTT--- 5 5CCCGGG------------TTTAAA---3-
5--CCCGGG-------------TTTAAA---3
3---GGGCCC------------AAATTT-5
CCCGGG
3--GGGCCC-------------AAATTT--- 5 5CCCGGG------------TTTAAA---3-
AAATTT
3---GGGCCC------------AAATTT-5
CCCGGG------------TTTAAA
5CCCGGG------------TTTAAA---3-
GGGCCC------------AAATTT
Results: 2n
C. Applications of PCR
Forensics: DNA finger printing
Restriction Fragment Length Polymorphisms ( RFLPs); Each personss DNA has
a unique sequence pattern, the restriction enzymes cut differently and lead to different
sized fragments
PCR-based Analysis: Faster, simpler and no requirement fro radioactive probes
13.4. Applications of recombinant DNA technology
A. Recombinant protein products
Human insulin expressed E. coli
Growth hormone Page 355 Table 13.1
Bacterial Host:
Lack in posttranslational modifications
Unable to carry out important exon splicing reactions
Animal cell as host
Endocytotic up take of clacim phosphate precipitated DNA
Electroporation: a brief high voltage pulse
Microinjection
B. Genetically altered(Modified) organism (GMO)
Bacteria:
Pseudomonas: complex chlorinated hydrocarbons for bioremediation
Thiobacillus ferrooxidans: Desulfurization of coal
Plants: Using Ti plasmid of Agrobacterium
Tumefaciens
Tomato, Soybean, Corn
Plants in high salinity, drought and extreme cold
Animals: Transfer into germ cells
Ethnic problems
Dolly, Giant mouse
C. Human gene therapy
The attempt to correct a genetic defect by inserting the normal gene into the cells
of an organism
AIDS, Brain cancer, obesity, multiple sclerosis,
Page 358, Table 13.2.
Chapter 14. Basic concepts of cellular
metabolism and bioenergetics
Metabolism: Sum total of all chemical reactions in an organism
Autotrophs: Energy from sun and CO2 in most cases
Heterotrophs: Obtain energy by ingesting complex carbon containg compounds
14.1. Intermediary metabolism
A. Two paths of metabolism
Catabolism: the degradative path, Releasing the potential energy from food into ATP
Page 369 Table 14.1
Anabolism: Biosynthesis, Using the free energy stored in ATP
Page 369 Table 14.1
B. Possible sequential arrangements for metabolic pathways
Page 368 Fig. 14.3.
D. ATP cycle Page 370 Fig. 14.4
D. Stages of metabolism
Catabolism
Stage 1: Breakdown of macromolecules into their respective building blocks
Stage 2: Building blocks are oxidized to a common metabolite Acetyl CoA
Stage 3: Acetyl CoA enters into Citric Acid Cycle , Respiratory assembly, Oxidative
phsphorylation
Anabolism:
Three stages like catabolism, but divergent.
Requires energy in the form of ATP and NADPH
The two processes are similar in terms of intermediates and enzymes but they are not
identical.
14.2. The chemistry of metabolism: Page 372 Table 14.2
14.3. Concepts of bioenergetics
Mitochondria Chloroplasts
Electron flow NADH(FADH2) O2 H2O NADP+
Proton flow during Innermembrane Inter membrane space
elctron transport Intermembrane space Inner membrane
O2 Consumed Generated
E. Photophosphorylation
Proton movement from stroma to lumen ( from outside to inside
17.6 Synthesis of carbohydrates by the Calvin cycle
A. Stage 1: Addition of CO2 to an acceptor molecule ( Ribulose 1,5-bis phosphate) Page
479 Fig. 17.29
In summary,
Palmitoyl ScoA + 7 FAD + 7 NAD + 7CoASH + 7 H2O
8acetyl ScoA + 7FADH2 + 7NADH + 7H+
C. ATP balance Page 499 Table 18.2
D. Beta oxidation of unsaturated fatty acids
Double bonds in the intermediate enoyl CoA: Trans
Double bonds in naturally occurring fatty acids: Cis
Metabolism of 16:29,12: Page 500 Fig. 18.10
E. Beta oxidation of fatty acids with odd numbers of carbons: End product is
Propionyl CoA
Degradation of Propionyl CoA: Page 501 Fig. 18.12
18.3 Biosynthesis of fatty acids
A. Comparison of both processes ( Cata- and Anabolism). Page 503 Table 18.3
B. Transport of citrate from mitochondria to cytoplasm : Page 503 Fig. 18.14
C. Fatty acid synthase: Multi enzyme complex in mammals:
Page 505 Table 18.4
Malonyl CoA formation is the rate limiting step in fatty acid synthesis.
D. Biosynthesis of unsaturated fatty acids
In endoplasmic reticulum by faty acyl-CoA desaturases
E. Regulation of fatty acid metabolism
-oxidation and syntheis must be coordinated so they do not occur simultaneously.
The availability of carbohydrates and fatty acids.
Abundant glucose High production of citrate
Positive modulator for aceyl-CoA carboxylase Increase in
Malonyl CoA formation Blocking the action of carnitine acyltransferase I Turn off
of fatty acid degradation
The increase of fatty acid in the mitorchodria enhances -oxidation under conditions
of low blood glucose.
18.4 Cholesterol
A. Roles
Essential component of animal membrane
Precursor for steroid hormones, bile salts and vitamin
D
B. Cholesterol biosynthesis Page 508 Fig. 18.20
Step 1. Acetyl CoA mevalonate:
HMG CoA reductase :major regulatory step in cholesterol biosynthesis
Step 2: Activated isoprenes : Page 509 Fig. 18.21