PROTEIN

METABOLISM
 2023 - 2024

Chapter Outline
Protein Digestion Amino Acid
26.1 26.6
and Absorption Biosynthesis

Amino Acid Hemoglobin

26.2 26.7
Utilization Catabolism

Transamination and Interrelationships

Oxidative 26.3 Among Metabolic 26.8
Deamination Pathways

B Vitamins and
The Urea Cycle 26.4 26.9
Protein Metabolism

Amino Acid Carbon

26.5
Skeletons
26.1 Protein Digestion and
Absorption
Protein Digestion
–DIETARY PROTEIN PRESENT IN THE STOMACH STIMULATES THE RELEASE OF
GASTRIN
26.1 Protein Digestion and
Absorption
Protein Digestive Enzymes in the
Intestine
•PROTEOLYTIC ENZYMES

•PROTEOLYTIC ENZYMES
26.1 Protein Digestion and
Absorption
 26.1 Protein Digestion and
Absorption
PROTEIN DIGESTION BEGINS IN THE _____ AND IS COMPLETED IN THE _____, RESULTING IN
THE RELEASE OF AMINO ACIDS.
A. MOUTH; STOMACH
B. MOUTH; SMALL INTESTINE
C. STOMACH; SMALL INTESTINE
D. SMALL INTESTINE; LIVER
 26.1 Protein Digestion and
Absorption
PROTEIN DIGESTION BEGINS IN THE _____ AND IS COMPLETED IN THE _____, RESULTING IN
THE RELEASE OF AMINO ACIDS.
A. MOUTH; STOMACH
B. MOUTH; SMALL INTESTINE
C. STOMACH; SMALL INTESTINE
D. SMALL INTESTINE; LIVER
26.2 Amino Acid Utilization
Amino Acids
PRODUCED FROM THE DIGESTION OF PROTEINS ENTER THE AMINO ACID
POOL OF THE BODY.

THE AMINO ACID POOL IS THE TOTAL SUPPLY OF FREE AMINO ACIDS
AVAILABLE FOR USE IN THE HUMAN BODY

–PROTEIN TURNOVER: THE REPETITIVE PROCESS IN WHICH PROTEINS ARE

DEGRADED AND RESYNTHESIZED
26.2 Amino Acid Utilization
Nitrogen Balance
•THE STATE THAT RESULTS WHEN THE AMOUNT OF NITROGEN TAKEN INTO
THE HUMAN BODY AS PROTEIN EQUALS THE AMOUNT OF NITROGEN
EXCRETED FROM THE BODY IN WASTE MATERIALS

2 TYPES OF NITROGEN BALANCE

NEGATIVE NITROGEN IMBALANCE

POSITIVE NITROGEN IMBALANCE

26.2 Amino Acid Utilization

Uses of Amino Acids in the Human

Body
‒USES APPROXIMATELY 75% OF FREE AMINO ACIDS
•SYNTHESIS OF NONESSENTIAL AMINO ACIDS
•PRODUCTION OF ENERGY
26.2 Amino Acid Utilization

Degradation Pathways
•THE AMINO NITROGEN ATOM IS REMOVED AND EXCRETED FROM THE
BODY AS UREA
26.2 Amino Acid Utilization

AMINO ACIDS PRODUCED DURING PROTEIN DIGESTION ENTER THE _____

OF THE BODY.
A.ENERGY PRODUCTION POOL
B.AMINO ACID POOL
C.PROTEIN SYNTHESIS POOL
D.NITROGEN BALANCE POOL
26.2 Amino Acid Utilization

AMINO ACIDS PRODUCED DURING PROTEIN DIGESTION ENTER THE _____

OF THE BODY.
A.ENERGY PRODUCTION POOL
B.AMINO ACID POOL
C.PROTEIN SYNTHESIS POOL
D.NITROGEN BALANCE POOL
26.3 Transamination and
Oxidative Deamination
TRANSAMINATION REACTION
-IS A BIOCHEMICAL REACTION
THAT INVOLVES THE
INTERCHANGE
OF THE AMINO GROUP OF AN A-
AMINO ACID WITH THE KETO
GROUP OF AN A-KETO ACID.
26.3 Transamination
GLUTAMATE PRODUCTION VIA
TRANSAMINATION

- GLUTAMATE IS PRODUCED THROUGH

TRANSAMINATION WHEN Α-KETOGLUTARATE
IS THE AMINO GROUP ACCEPTOR
 26.3 Transamination
ASPARTATE PRODUCTION VIA
TRANSAMINATION

- TRANSAMINATION IN WHICH GLUTAMATE IS THE

REACTING AMINO ACID AND OXALOACETATE IS
THE REACTING KETO ACID PRODUCES ASPARTATE
AS THE NEW AMINO ACID.
26.3 Oxidative Deamination
OXIDATITVE DEAMINATION - IS A FORM OF DEAMINATION THAT GENERATES Α-KETO ACIDS
AND OTHER OXIDIZED PRODUCTS FROM AMINE-CONTAINING COMPOUNDS, AND
OCCURS PRIMARILY IN THE LIVER.
26.4 The Urea Cycle

WHAT IS UREA?
26.4 The Urea Cycle

WHAT IS UREA?
UREA IS A CHEMICAL COMPOUND, CHEMICALLY KNOWN AS
CARBAMIDE, IT IS COMPOSED OF NITROGEN AND CARBON,
WITH THE FORMULA (NH2)2CO.
IT IS PRODUCED IN THE LIVER
26.4 The Urea Cycle

WHAT IS UREA?
UREA IS AN ODORLESS WHITE SOLID WITH A SALTY TASTE,
HAS A MELTING POINT OF 133 DEGREE CELSIUS, AND IS
SOLUBLE IN WATER.
26.4 The Urea Cycle

CARBAMOYL PHOSPHATE
CARBAMOYL PHOSPHATE IS FORMED THROUGH THE
CATALYTIC REACTION OF CARBAMOYL PHOSPHATE
SYNTHETASE, CONVERTING CARBON DIOXIDE AND
AMMONIA INTO CARBAMOYL PHOSPHATE.
26.4 The Urea Cycle

CARBAMOYL PHOSPHATE
IT IS FORMED IN THE MITOCHONDRIAL MATRIX.
IT CONTAINS A HIGH-ENERGY PHOSPHATE BOND.
26.4 The Urea Cycle
STEPS OF THE UREA CYCLE?

1. STAGE 1 - CARBAMOYL GROUP TRANSFER

2. STAGE 2 - CITRULLINE–ASPARTATE
CONDENSATION
3. STAGE 3 - ARGININOSUCCINATE CLEAVAGE
4. STAGE 4 - UREA FROM ARGININE HYDROLYSIS
26.4 The Urea Cycle

STAGE 1 - CARBAMOYL GROUP TRANSFER

THE CARBAMOYL GROUP OF CARBAMOYL PHOSPHATE

IS TRANSFERRED TO ORNITHINE TO FORM CITRULLINE.
26.4 The Urea Cycle

STAGE 2 - CITRULLINE–ASPARTATE CONDENSATION

CITRULLINE IS TRANSPORTED INTO THE CYTOSOL AND

REACTS WITH ASPARTATE TO PRODUCE
ARGININOSUCCINATE SYNTHETASE, UTILIZING ATP.
26.4 The Urea Cycle

STAGE 3 - ARGININOSUCCINATE CLEAVAGE

ARGININOSUCCINATE IS CLEAVED TO ARGININE AND

FUMARATE BY THE ENZYME ARGININOSUCCINATE
LYASE.
26.4 The Urea Cycle

STAGE 4 - UREA FROM ARGININE HYDROLYSIS

HYDROLYSIS OF ARGININE PRODUCES UREA AND REGENERATES
ORNITHINE UNDER THE INFLUENCE OF ARGINASE.
THE OXYGEN ATOM PRESENT IN UREA COMES FROM WATER.
ORNITHINE IS TRANSPORTED BACK TO MITOCHONDRIA TO BE
USED IN THE UREA CYCLE.
26.5 Amino Acid Carbon
Skeletons
TRANSAMINATION/OXIDATIVE DEAMINATION REMOVES THE AMINO GROUP
FROM AN AMINO ACID
- AN Α-KETO ACID THAT CONTAINS THE SKELETON OF THE AMINO ACID IS
PRODUCED

EACH OF THE 20 AMINO ACIDS UNDERGO A DIFFERENT DEGRADATION

PROCESS
- PRODUCTS FORMED ARE AMONG A GROUP OF SEVEN INTERMEDIATES
FOUR PRODUCTS ARE INTERMEDIATES IN THE CITRIC ACID CYCLE: A-
KETOGLUTARATE, SUCCINYL COA, FUMARATE, AND OXALOACETATE
THREE PRODUCTS ARE PYRUVATE, ACETYL COA, AND ACETOACETYL
COA
26.5 Amino Acid Carbon
Skeletons
THE AMINO ACIDS THAT ARE DEGRADED TO CITRIC ACID CYCLE
INTERMEDIATES CAN SERVE AS GLUCOSE PRECURSORS AND ARE CALLED
GLUCOGENIC.
GLUCOGENIC AMINO ACID: AN AMINO ACID THAT HAS A CARBON-
CONTAINING DEGRADATION PRODUCT THAT CAN BE USED TO PRODUCE
GLUCOSE VIA GLUCONEOGENESIS

THE AMINO ACIDS CONVERTED TO ACETYL COA OR ACETOACETYL COA CAN

CONTRIBUTE TO THE FORMATION OF FATTY ACIDS OR KETONE BODIES AND
ARE CALLED KETOGENIC.
KETOGENIC AMINO ACID: AN AMINO ACID THAT HAS A CARBON-
CONTAINING DEGRADATION PRODUCT THAT CAN BE USED TO PRODUCE
KETONE BODIES
Fates of Carbon Skeletons of Amino Acids
26.6 Amino Acid Biosynthesis
NONESSENTIAL AMINO ACIDS ARE SYNTHESIZED IN FEWER
STEPS THAN ESSENTIAL AMINO ACIDS.

MOST BACTERIA AND PLANTS SYNTHESIZE ALL AMINO

ACIDS VIA PATHWAYS THAT ARE NOT PRESENT IN HUMANS.

PLANTS ARE THE MAJOR SOURCE OF THE ESSENTIAL AMINO

ACIDS IN HUMANS AND ANIMALS.
Summary of the Starting Materials for the
Biosynthesis of the 11 Nonessential Amino Acids
26.7 Hemoglobin Catabolism
RED BLOOD CELLS ARE HIGHLY SPECIALIZED
CELLS WHOSE PRIMARY FUNCTION IS TO
DELIVER OXYGEN TO, AND REMOVE CARBON
DIOXIDE FROM, BODY TISSUES. MATURE RED
BLOOD CELLS HAVE NO NUCLEUS OR DNA.
INSTEAD, THEY ARE FILLED WITH THE RED
PIGMENT HEMOGLOBIN.

RED BLOOD CELL FORMATION OCCURS IN THE

BONE MARROW, AND ABOUT 200 BILLION NEW
RED BLOOD CELLS ARE FORMED DAILY. THE
LIFE SPAN OF A RED BLOOD CELL IS ABOUT
FOUR MONTHS.
HEMOGLOBIN IS A CONJUGATED
PROTEIN:
GLOBIN - THE PROTEIN PORTION
HEME - THE PROSTHETIC GROUP

HEME CONTAINS FOUR PYRROLE GROUPS

JOINED TOGETHER WITH AN IRON ATOM
IN THE CENTER. IT IS THE IRON ATOM IN
HEME THAT INTERACTS WITH O2,
FORMING A REVERSIBLE COMPLEX WITH
IT.
OLD RED BLOOD CELLS ARE BROKEN DOWN IN THE:
SPLEEN (PRIMARY SITE) AND
LIVER (SECONDARY SITE)

PART OF THIS PROCESS IS THE DEGRADATION OF HEMOGLOBIN. THE GLOBIN

PROTEIN IS HYDROLYZED TO AMINO ACIDS, WHICH BECOME PART OF THE
AMINO ACID POOL.

THE IRON ATOM OF HEME BECOMES PART OF FERRITIN.

FERRITIN: AN IRON-STORAGE PROTEIN, THAT SAVES THE IRON FOR USE IN THE
BIOSYNTHESIS OF NEW HEMOGLOBIN MOLECULES.

THE TETRAPYRROLE CARBON ARRANGEMENT OF HEME IS DEGRADED TO BILE

PIGMENTS THAT ARE ELIMINATED IN FECES AND TO A LESSER EXTENT IN
URINE
1st step:
DEGRADATION OF HEME BEGINS WITH A
RING-OPENING REACTION IN WHICH A
SINGLE CARBON ATOM IS REMOVED.
THE PRODUCT IS CALLED BILIVERDIN.

THIS REACTION HAS SEVERAL

IMPORTANT CHARACTERISTICS:
MOLECULAR OXYGEN, O2, IS
REQUIRED AS A REACTANT.
RING OPENING RELEASES THE IRON
ATOM TO BE INCORPORATED INTO
FERRITIN.
THE PRODUCT CONTAINING THE
EXCISED CARBON ATOM IS CARBON
MONOXIDE (A SUBSTANCE TOXIC TO
THE HUMAN BODY).
2nd step:
IN THE SECOND STEP OF HEME
DEGRADATION, BILIVERDIN IS CONVERTED
TO BILIRUBIN. THIS CHANGE INVOLVES
REDUCTION OF THE CENTRAL METHYLENE
BRIDGE OF BILIVERDIN.

THE CHANGE FROM HEME TO BILIVERDIN

TO BILIRUBIN USUALLY OCCURS IN THE
SPLEEN. THE BILIRUBIN IS THEN
TRANSPORTED BY SERUM ALBUMIN TO
THE LIVER, WHERE IT IS RENDERED MORE
WATER-SOLUBLE BY THE ATTACHMENT OF
SUGAR RESIDUES TO ITS PROPIONATE
SIDE CHAINS (P SIDE CHAINS). THE
SOLUBILIZING SUGAR IS GLUCURONATE.
Final step:
THE SOLUBILIZED BILIRUBIN IS EXCRETED FROM THE LIVER IN BILE, WHICH FLOWS
INTO THE SMALL INTESTINE. HERE THE BILIRUBIN DIGLUCURONIDE IS CHANGED, IN
A MULTISTEP PROCESS, TO EITHER STERCOBILIN FOR EXCRETION IN FECES OR
UROBILIN FOR EXCRETION IN URINE. BOTH STERCOBILIN AND UROBILIN STILL HAVE
TETRAPYRROLE STRUCTURES.
Bile Pigments
THE TETRAPYRROLE DEGRADATION PRODUCTS OBTAINED FROM HEME ARE KNOWN
AS BILE PIGMENTS BECAUSE THEY ARE SECRETED WITH THE BILE AND MOST OF
THEM ARE HIGHLY COLORED.

BILE PIGMENT: IS A COLORED TETRAPYRROLE DEGRADATION PRODUCT PRESENT IN

BILE
BILIVERDIN AND BILIRUBIN: GREEN AND REDDISH-ORANGE
STERCOBILIN: BROWNISH
UROBILIN: YELLOW

DAILY NORMAL EXCRETION OF BILE PIGMENTS:

1–2 MG IN URINE
250–350 MG IN FECES
Bile Pigments
JAUNDICE - IS THE CONDITION THAT
OCCURS WHEN BILIRUBIN CONCENTRATIONS
IN THE BLOOD BECOME HIGHER THAN
NORMAL. THE SKIN AND THE WHITE OF THE
EYES ACQUIRE A YELLOWISH TINT BECAUSE
OF THE EXCESS BILIRUBIN IN THE BLOOD.

JAUNDICE CAN OCCUR AS A RESULT OF LIVER DISEASES, SUCH AS INFECTIOUS

HEPATITIS AND CIRRHOSIS, THAT DECREASE THE LIVER’S ABILITY TO PROCESS
BILIRUBIN;

SPLEEN MALFUNCTION: IN WHICH HEME IS DEGRADED MORE RAPIDLY THAN IT

CAN BE ABSORBED BY THE LIVER;
GALLBLADDER MALFUNCTION: USUALLY FROM AN OBSTRUCTION OF THE BILE
DUCT.
 26.8 Interrelationships Among
Metabolic Pathways
•The metabolic pathways of carbohydrates, lipids, and proteins are integrally linked
to one another
−A change in one pathway can affect many other pathways
•Examples
−Feasting - Over-eating
−Causes the body to store a limited amount as glycogen and the rest as fat
−Fasting - Food is not ingested
−The body uses its stored glycogen and fat for energy
−Starvation - Prolonged fasting
−Body protein is broken down to amino acids to synthesize glucose
Thank You
Prepare 1/4 sheet of paper for the quiz.
1-10
Quiz
Write Capital letter of your choice, small letter would signify as Wrong.

1. What is the primary function of proteins in the body?

a) Energy storage
b) Structural support
c) Nucleic acid synthesis
d) Vitamin absorption

2. Which of the following is the building block of proteins?

a) Glucose
b) Amino acids
c) Fatty acids
d) Nucleotides
3. Where does protein digestion primarily occur in the human body?
a) Stomach
b) Small intestine
c) Large intestine
d) Liver

4. What enzyme is responsible for breaking down proteins in the stomach?

a) Amylase
b) Pepsin
c) Lipase
d) Trypsin

5. After digestion, where are amino acids absorbed into the bloodstream?
a) Stomach
b) Liver
c) Small intestine
d) Large intestine
6.Which organ plays a key role in regulating blood amino acid levels and synthesizing
plasma proteins?
a) Kidneys
b) Liver
c) Pancreas
d) Spleen

7. Peptide bonds are hydrolyzed under the action of what pepsin?

8. Individual amino acids are produced in?
9. The enzyme carboxypeptidase is active in?
10. The enzyme aminopeptidase is active in?
 2023 - 2024

ANSWER KEY
1B
2B
3B
4B
5C
6B
7 Stomach
8 Small intestine
9 Small intestine
10 Small intestine