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NUCLEIC ACIDS

CHAPTER 17
STRUCTURE

Sugar: 2-deoxy α–D ribofuranose


STRUCTURE
Base Component of a Nucleoside:

1. Purine

2. Pyrimidine base
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BIOSYNTHESIS AND DEGRADATION OF
NUCLEIC ACIDS
CHAPTER 18
BIOSYNTHESIS
- Is a chemical task of the cells that requires energy

Central dogma in the biosynthesis of nucleic acid:

replication

Transcription translation
DNA RNA PROTEINS
reverse transcription

CHAPTER 18: BIOSYNTHESIS AND DEGRADATION OF NUCLEIC ACIDS


REPLICATION
Process by which each strand of the parental DNA is copied precisely to produce
2 daughter DNAs which are identical with the parent DNA

TRANSCRIPTION
Process by which the information contained in DNA is copied, forming an RNA
chain with bases that are complementary to the DNA template

REVERSE TRANSCRIPTION
Involves the use of RNA as the bearer of genetic information, instead of DNA. It
results in the formation of new duplex DNA.

TRANSLATION
Complex process by which the information transcribed from DNA into a special
strand of m-RNA directs the ordered polymerization of specific amino acids into
the formation of proteins

CHAPTER 18: BIOSYNTHESIS AND DEGRADATION OF NUCLEIC ACIDS


BIOSYNTHESIS OF DNA (REPLICATION)
-Takes place in the nucleus

-Requires:
•Template dATP
•Primer dTTP
•4 deoxyribonucleotides dCTP
•Mg+2 dGTP

EUKARYOTIC DNA
•Replicated semi-conservatively
•Starts at multiple origins – to ensure that the chromosomal DNA is replicated
within a certain time period
•Proceeds bi-directionally from each starting point

Complex process by which the information transcribed from DNA into a special
strand of m-RNA directs the ordered polymerization of specific amino acids into
the formation of proteins

CHAPTER 18: BIOSYNTHESIS AND DEGRADATION OF NUCLEIC ACIDS


BIOSYNTHESIS OF DNA (REPLICATION)

CHAPTER 18: BIOSYNTHESIS AND DEGRADATION OF NUCLEIC ACIDS


BIOSYNTHESIS OF RNA
(TRANSCRIPTION)

1. INITIATION 2. ELONGATION
Binding of enzyme RNA polymerase to a Process moves along the gene,
promoter site upstream of the gene synthesizing a complementary RNA
copy of the DNA template using
ribonucleoside 5’ triphosphates as
precursors

RNA
3. TERMINATION
•RNA synthesis does not require a Causes the biosynthetic process to stop,
primer releasing the completed RNA and
•Methylated guanine cap is added to the dissociating from the RNA
5’ end of the new RNA

CHAPTER 18: BIOSYNTHESIS AND DEGRADATION OF NUCLEIC ACIDS


BIOSYNTHESIS OF RNA (TRANSCRIPTION)

CHAPTER 18: BIOSYNTHESIS AND DEGRADATION OF NUCLEIC ACIDS


BIOSYNTHESIS OF RNA (TRANSCRIPTION)

CHAPTER 18: BIOSYNTHESIS AND DEGRADATION OF NUCLEIC ACIDS


CATABOLISM OF NUCLEIC ACIDS

Nucleotide nucleosides free base

deamination
Guanine xanthine uric acid excreted

deamination
Nucleotide nucleosides free base

CHAPTER 18: BIOSYNTHESIS AND DEGRADATION OF NUCLEIC ACIDS


PROTEIN SYNTHESIS
(TRANSLATION)
CHAPTER 19
TRANSLATION
-is the process of reading the sequence of an m-RNA molecule from the 5 end
to the 3 end by ribosomes, which then synthesize the appropriate polypeptide

GENETIC CODE
Embodiment of the relationship between the base sequence in the
polynucleotide and the order of amino acids composing the polypeptide

CODONS – the sequence of the mRNA read in groups of 3 nucleotides

STOP CODONS – 3 codons code for termination of CHON synthesis & does
not code for any amino acid
UAG
UGA
UAA

START CODON / INITIATION CODON – codon AUG code for methionine

CHAPTER 19: PROTEIN SYNTHESIS (TRANSLATION)


2nd base

1st base (5 end) 3rd base (3’ end)

CHAPTER 19: PROTEIN SYNTHESIS (TRANSLATION)


SYNTHESIS OF
AMINO ACYL t-RNA

Typical t-RNA:
o70-90 nucleotides
oCloverleaf secondary
structure
oAnticodon accessible at
the end of the anticodon
stem loop

CHAPTER 19: PROTEIN SYNTHESIS (TRANSLATION)


PROTEIN SYNTHESIS IN EUKARYOTES
1st step:
Transcription of mRNA from a DNA gene in the nucleus.

At some other prior time, the various other types of RNA have been synthesized
using the appropriate DNA. The RNAs migrate from the nucleus into the
cytoplasm.

Prior to the beginning of the protein synthesis, all of the component parts are
assembled in the ribosome which is the brown/tan structure in the left graphic.

CHAPTER 19: PROTEIN SYNTHESIS (TRANSLATION)


CHAPTER 19: PROTEIN SYNTHESIS (TRANSLATION)
PROTEIN SYNTHESIS IN EUKARYOTES
2nd step: INITIATION

In the cytoplasm, protein synthesis is actually initiated by the AUG codon on mRNA.

The AUG codon signals both the interaction of the ribosome with m-RNA and also the
tRNA with the anticodons (UAC).

The tRNA which initiates the protein synthesis has N-formyl-methionine attached.

The formyl group is really formic acid converted to an amide using the -NH2 group on
methionine

The next step is for a second tRNA to approach the mRNA (codon - CCG). This is the
code for proline. The anticodon of the proline tRNA which reads this is GGC.

The final process is to start growing peptide chain by having amine of proline to bond
to the carboxyl acid group of methinone (met) in order to elongate the peptide.
CHAPTER 19: PROTEIN SYNTHESIS (TRANSLATION)
CHAPTER 19: PROTEIN SYNTHESIS (TRANSLATION)
PROTEIN SYNTHESIS IN EUKARYOTES
3RD step: ELONGATION

Elongation of the peptide begins as various tRNA's read the next codon.

When the correct match with the anticodons of a tRNA has been found, the tyrosine
forms a peptide bond with the growing peptide chain .

The proline is now hydrolyzed from the tRNA. The proline tRNA now moves away from
the ribosome and back into the cytoplasm to reattach another proline amino acid.

CHAPTER 19: PROTEIN SYNTHESIS (TRANSLATION)


CHAPTER 19: PROTEIN SYNTHESIS (TRANSLATION)
PROTEIN SYNTHESIS IN EUKARYOTES
4th step: TERMINATION

When the stop signal on mRNA is reached, the protein synthesis is terminated. The
last amino acid is hydrolyzed from its t-RNA.

The peptide chain leaves the ribosome. The N-formyl-methionine that was used to
initiate the protein synthesis is also hydrolyzed from the completed peptide at this
time.

The ribosome is now ready to repeat the synthesis several more times.

CHAPTER 19: PROTEIN SYNTHESIS (TRANSLATION)


CHAPTER 19: PROTEIN SYNTHESIS (TRANSLATION)
PROTEIN DEGRADATION
CHAPTER 20
DEGRADATION OF AMINO GROUP
IN AMINO ACIDS
Involves 2 processes:

TRANSAMINATION
- removal or transfer of the α amino group

Catalyzation of aminotransferases or transaminases which require pyridoxal


phosphate or Vitamin B6 as co-enzyme

α-KGA – usual acceptor of the amino group

L-amino acid + pyridoxal PO4 α-keto acid + pyridoxamine PO4


(substrate 1) (product 1)

Pyridoxamine PO4 + α-KGA L-glutamate + pyridoxal PO4


(substrate 2) (product 2)

CHAPTER 20: PROTEIN DEGRADATION


TRANSPORT OF AMINO GROUPS
TO THE LIVER
2 carriers:

1. GLUTAMATE – collects amino acids for excretion in most extrahepatic tissues of


man
Amino acids are released as NH4+
Attached to a carrier for transport to the liver

OXIDATIVE DEAMINATION – catalyzed by mitochondrial L-glutamate DHG


removes the amino groups
oxidizes carbon skeletons to α-KGA by NAD+

NH4+ reacts with glutamate to form glutamine


Glutamine enters the blood, transported to the liver

Amino acids attached to glutamine is converted back to NH4+

CHAPTER 20: PROTEIN DEGRADATION


TRANSPORT OF AMINO GROUPS
TO THE LIVER
2 carriers:

2. ALANINE – serves as amino group transporter in the muscle


produced as amino groups collected by glutamate
transferred to pyruvate
passes into the blood
carries the amino group into the liver

alanine transfers the amino group to α KGA = glutamate & pyruvate


oxidative deamination of glutamate = release of amino groups as NH4+

CHAPTER 20: PROTEIN DEGRADATION


TRANSPORT OF AMINO GROUPS
TO THE LIVER

CHAPTER 20: PROTEIN DEGRADATION


UREA
CYCLE

CHAPTER 20: PROTEIN DEGRADATION


CHAPTER 20: PROTEIN DEGRADATION
CHAPTER 20: PROTEIN DEGRADATION
CHAPTER 20: PROTEIN DEGRADATION
AMINO ACIDS AND THEIR METABOLITES
NEUROTRANSMITTERS & BIOLOGICAL REGULATORS

NEUROTRANSMISSION – involves movement across a synapse between 2


adjacent cells

HORMONAL TRANSMISSION – occurs over a distance with a hormonal


messenger being transported through the blood stream to the effector cell

CHAPTER 20: PROTEIN DEGRADATION


AMINO ACIDS AND THEIR METABOLITES
NEUROTRANSMITTERS

2 TYPES OF SYNAPSES

CHOLINERGIC SYNAPSES
Involve acetylcholine as neurotransmitter
Choline is synthesized principally as part of phosphatidyl choline

CHAPTER 20: PROTEIN DEGRADATION


CHAPTER 20: PROTEIN DEGRADATION
CHAPTER 20: PROTEIN DEGRADATION
INTEGRATION OF CYCLES
CHAPTER 21
DIETARY ASPECTS OF METABOLISM:
NITROGEN BALANCE
Dietary proteins are digested and absorbed in the small intestines to yield free
amino acids.

These amino acids may have any of the following fates:


1. Reassembled peptides and proteins
2. Utilized as fuels
3. Converted to other compounds
4. Degraded and excreted as NH4+ in aquatic vertebrates; as urea in terrestrial
organisms or as uric acid for birds and reptiles

CHAPTER 20: PROTEIN DEGRADATION


CHAPTER 20: PROTEIN DEGRADATION
CHAPTER 20: PROTEIN DEGRADATION
CHAPTER 20: PROTEIN DEGRADATION
ESSENTIAL DIETARY NUTRIENTS

AMINO ACIDS MICRONUTRIENTS


Ile Vitamins:
His Water soluble
Thr Fat soluble
Val
Met Minerals
Trp
Arg*
Phe
Lys
Leu

CHAPTER 20: PROTEIN DEGRADATION


ESSENTIAL DIETARY NUTRIENTS

MACRONUTRIENTS MICRONUTRIENTS
Principal cation in the ECF
Na+ Maintains osmotic pressure of ECF
Controls water retention
Helps in BP maintenance
Maintains acid-base balance
Regulates nerve & heart muscle tissue irritability
Principal cation in the ICF
K+ Maintains osmotic pressure
Maintains electrical component of the cells
Maintains size of cells
Maintains proper contraction of the heart
Proper transmission of nerve impulses

CHAPTER 20: PROTEIN DEGRADATION


ESSENTIAL DIETARY NUTRIENTS

MACRONUTRIENTS MICRONUTRIENTS
Found in bones & teeth
Ca++ Important for clotting of blood
Regulation of membrane permeability
Normal functioning of the nerves, heart & muscle
tissues
Found in ICF
Mg++ Essential for the proper functioning of the
neuromuscular system
Primary anion of ICF
Cl- Component of gastric HCl
Helps in the transport of O2 and CO2 in blood

CHAPTER 20: PROTEIN DEGRADATION


ESSENTIAL DIETARY NUTRIENTS

MACRONUTRIENTS MICRONUTRIENTS
Primary anion of ICF
Phosphate Important in acid-base balance
ATP production
Involved in cellular respiration
Iron ion Part of hemoglobin, myoglobin & cytochromes
Required for the synthesis of hemoglobin and some
Copper ion oxidative enzymes
Needed for normal growth & reproduction
Zinc ion Helps in wound healing & tissue repair
Constituent of Vitamin B12
Cobalt ion Needed for the formation of RBC

CHAPTER 20: PROTEIN DEGRADATION


ESSENTIAL DIETARY NUTRIENTS

MACRONUTRIENTS MICRONUTRIENTS
Essential for normal bone structure
Mn ion Reproduction
Normal functioning of CNS
Metabolism of glucose and proper activity of
Chromium insulin
Production of thyroid hormones
Iodine
Metabolism of nucleic acids
Molybdenum
Treatment of manic-depressive psychoses
Lithium salts Anti-depressant for psychiatric patients

CHAPTER 20: PROTEIN DEGRADATION