PROTEIN METABOLISM

PROTEIN METABOLISM DENOTES THE VARIOUS BIOCHEMICAL PROCESSES

RESPONSIBLE FOR THE SYNTHESIS OF PROTEINS AND AMINO ACIDS
(ANABOLISM), AND THE BREAKDOWN OF PROTEINS BY CATABOLISM. THE
STEPS OF PROTEIN SYNTHESIS INCLUDE TRANSCRIPTION, TRANSLATION,
AND POST TRANSLATIONAL MODIFICATIONS.
Protein anabolism
Transcription
 POST-TRANSCRIPTIONAL MODIFICATION
Changes in eukaryotic mRNA, tRNA or other RNAs made after transcription has
been completed. Post-transcriptional modifications of RNA play an important role
in a wide range of biological processes.
In ribosomal RNA (rRNA), methylation of nucleotide bases is the predominant
modification.
Post-transcriptional modifications of pre-mRNA, such as capping, splicing,
and polyadenylation, take place in the nucleus. After these modifications have
been completed, the mature mRNA molecules have to be translocated into the
cytoplasm, where protein synthesis occurs. 
Post Transcriptional processing in tRNA processing steps include removal of
transcribed leader and trailer sequences, addition of CCA to the 3′ mature sequence.
 MRNA POST TRANSCRIPTIONAL
MODIFICATIONS
1. 5’ Cap
2. Splicing
3. 3’ Polyadenylation
Translation
Translation involves “decoding” a messenger RNA (mRNA)
and using its information to build a polypeptide, or chain of
amino acids.
 Translation

• Initiation ("beginning"): in
this stage, the ribosome
gets together with the
mRNA and the first tRNA
so translation can begin.
 TRANSLATION
•Elongation ("middle"):
in this stage, amino acids
are brought to the
ribosome by tRNAs and
linked together to form a
chain.
•Termination ("end"): in
the last stage, the finished
polypeptide is released to
go and do its job in the
cell.
 TRANSLATION

•Termination ("end"): in
the last stage, the finished
polypeptide is released to
go and do its job in the
cell.
POST TRANSLATIONAL
MODIFICATIONS
 PROTEIN TARGETING 
Protein targeting or protein sorting is the biological mechanism by which proteins are
transported to their appropriate destinations within or outside the cell.

Targeting signals that direct polypeptides synthesized on cytoplasmic ribosomes to chloroplasts,

mitochondria, and peroxisomes
The digestion of proteins begins in the stomach. When protein-rich
foods enter the stomach, they are greeted by a mixture of the enzyme pepsin and
hydrochloric acid (HCl; 0.5 percent).
The latter produces an environmental pH of 1.5–3.5 that denatures proteins within food.
Pepsin cuts proteins into smaller polypeptides and their constituent amino acids.
When the food-gastric juice mixture (chyme) enters the small intestine,
the pancreas releases sodium bicarbonate to neutralize the HCl. This helps to protect the
lining of the intestine.
The small intestine also releases digestive hormones, including secretin and CCK, which
stimulate digestive processes to break down the proteins further.
Secretin also stimulates the pancreas to release sodium bicarbonate. The pancreas
releases most of the digestive enzymes, including the proteases trypsin, chymotrypsin,
carboxypeptidase, and elastase, which aid protein digestion.
Together, all of these enzymes break complex proteins into smaller individual amino acids
which are then transported across the intestinal mucosa to be used to create new
proteins, or to be converted into fats or acetyl CoA and used in the Krebs cycle.
Amino acids can also be used as a source of energy,
especially in times of starvation. Because the
processing of amino acids results in the creation of
metabolic intermediates, including pyruvate, acetyl
CoA, acetoacyl CoA, oxaloacetate, and α-
ketoglutarate, amino acids can serve as a source of
energy production through the Krebs cycle.