Protein Metabolism 1st Semester | Soyabean

- Damaged tissues
- Recycling enzymes and hormones
● Nitrogen Balance
● Protein supply only small portion of our body’s
- States that results the amount of
needs
nitrogen taken to the human body as
● CHO and fats supply 90% of the body
protein equals the amount of Nitrogen
● CHON is 10%
excreted from the body in waste
- For the proteins to be metabolized by
materials
the body it need the help of
● 2 types of nitrogen imbalance
HYDROCHLORIC ACID
➔ Negative nitrogen imbalance
● 3 major functions of hydrochloric acid
- Degradation exceeds synthesis
● Antiseptic properties kills most of the
- Amount of nitrogen in the urine
bacteria
exceeds the amount of nitrogen
● Denaturing action that unwinds the
ingested
globular proteins,
Negative nitrogen imbalance happens:
- makes the peptide bonds
- Tissue wasting (protein catabolism)
accessible to digestive
- Protein poor diets
enzyme
- Starvation
- Peptide Bonds- Provide
- Wasting illnesses
stability to the proteins
➔ Positive Nitrogen Imbalance
● Its acidity leads to the activation of
- Nitrogen intakes exceed nitrogen
pepsinogen
outputs
- Pepsinogen- inactive form of
This happens:
digestive enzyme pepsin,
- When protein protein anabolism exceeds
needed for total digestion of
protein catabolism(mas maraming pumapasok
our diet
kesa nabuburn na proteins))
● Protein breakdown begins in the
- Growth
stomach,unlike carbohydrates
- Pregnancy
● No protein hydrolyzing enzymes are found in
- Convalescence (pag galing) from an
saliva
emaciating illness
● Hydrolysis - breaking of the peptide bonds
Uses of Amino acids
occurs via denaturation
● Protein synthesis
- Denaturation by pepsin enzyme and
● Synthesis of nonprotein nitrogen-containing
HCI acid produce short chain
compounds
polypeptides in the stomach
- Purines,hemoglobins,neurotransmitter
● Trypsin, chymotrypsin,carboxypeptidase,and
s, pyrimidines,hormones
aminopeptidase ( pancreatic juices) from cells
● Synthesis of nonessential amino acids
in the small intestine creates”free amino acids”
● Production of energy
● Acidic protein contents coming from the
stomach going to the small intestine stimulates
production of the hormone secretin
● Secretin stimulate pancreatic production of
bicarbonate ion,HCO3 , which is needed for
the neutralization of gastric acid
● So , THE FREE AMINO ACIDS are absorbed
in intestinal wall ; via active transport, it will
enter the bloodstream and brought to the cells
● Amino Acid Pool- total supply of free amino
acids
3 sources of free amino acids:
- Dietary protein breakdown
- Biosynthesis of amino acids in the liver
- Protein turnover
● Protein turnover- breakdown and resynthesis
of body protein
- From old tissues
 Protein Metabolism
2 steps in The degradation of amino acids in our diet:
● Removal of alpha amino group
● Breakdown and process carbon skeleton
2 steps Release of amino groups:
● Transamination
● Oxidative deamination
Amino Acids:
● Glutamate -(most important , metabolically)
● Aspartate
● Alanine
● glutamine
- Present in concentrations in mammalian cells
Transaminase enzyme are used for diagnosing
disorders
● Alanine aminotransferase
- Escapes in large amounts from dead
or dying liver tissue
- Alanine
- Oxoglutarate
- Pyruvate
- Glutamate
➔ Glutamate:pyruvate transaminase
(GPT) (other name for alanine
aminotransferase)
- Alanine is the principal amino acid
released from muscle tissue during
starvation
- Important substrate for hepatic
gluconeogenesis
- Alanine transamination is required for
the proper maintenance of fasting
blood glucose concentrations
● Aspartate aminotransferase
- Active enzyme inside heart cells
- Measured in blood for myocardial
infarction
- Aspartate,oxoglutarate,
oxaloacetate,glutamate
➔ Glutamate:oxaloacetate
transaminase(GOT)
● For our body to be able to eliminate exces
amino acids, amino acids should undergo a
process called trans-deamination, the enzymes
here are called transaminases.
● Transaminases share a common substrate
product (oxoglutarate and glutamate) with the
enzyme GLUTAMATE DEHYDROGENASE
● Glutamate- has central role in the overall
control of nitrogen metabolism
● The glutamate produce from the
transamination step is then deaminated by
oxidative deamination using the enzyme
glutamate dehydrogenase
1st Semester | Soyabean
● Ammonia
- Simplest nitrogen containing
compound
- It has to be converted to urea to be
eliminated
-
● urea
- Derivative of ammonia
- More water soluble
● Urea cycle
- Ammonium salts are toxic compounds
causing vomiting, convulsion,coma
and, death when the blood
concentration exceeds 0.25mm
- The inputs to the urea cycle are
NH3(ammonia), CO2(carbon dioxide)
aspartic acid ,and ATP
- Outputs are Urea,ADP, and fumaric
cycle
- The carbonyl group of urea is derived
from CO2 ammonia contributes one of
the amine groups on urea
● Fumarate from the urea cycle enters the krebs
cycle (krebs cycle are also known as citric acid
cycle or tricarboxylic acid cycle)
● Krebs cycle- series of chemical reactions that
occurs in most aerobic organisms and part of
the aerobic cell metabolism.
● Aspartate produce from oxaloacetate of the
krebs cycle enters the urea cycle
● Oxaloacetate has 4 potential fates
- Transamination
- Conversion to glucose
- Formation Of citrate
- Conversion to pyruvate
Summary
● Transamination takes off amine group from
amino acids and forms glutamate (ionized
glutamic acid)
● Amine group form ammonia when remove in
deamination
● This combines with CO2 and aspartate. Forms
Urea,arginine and fumarate
● Uric Acids- very insoluble purine compound,
forms supersaturated solution
- In humans uric acid deposits crystal
and causes gout
 Protein Metabolism 1st Semester | Soyabean

THE HUMAN BODY'S RESPONSE TO FASTING

11 NON ESSENTIAL AMINO ACIDS

THE HUMAN BODY'S RESPONSE TO

STARVATION

● Phenylketonuria (PKU)
- Defective phenylalanine hydroxylase
- Phenylalanine accumulates in body..
Phenylalanine is transaminated to
phenylpyruvate.
- Accumulation of phenylpyruvate leads
to severe mental retardation to infants

THE HUMAN BODY'S RESPONSE TO FEASTING