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PROTEINS,
ENZYMES AND
VITAMINS
Protein Classification
Based On SHAPE
1. Fibrous Protein – have simple,
regular linear structures.
2.Globular Protein - molecules have
peptide chains that are folded into
spherical or globular shapes.
3. Membrane Protein – a protein that is
found associated with a cell membrane.
Common Fibrous
Proteins
a. Keratin – found in protective
coverings for organisms.
b. Collagen – most abundant
proteins in humans; found in
tendons, bone and other
connective tissue.
Common Fibrous
Proteins
c. Elastin – found in blood
vessel and ligaments
d. Myosin – found in muscular
tissue.
e. Fibrin – found in blood
Common Globular
Proteins
a. Hemoglobin – transports
oxygen from the lungs to
tissue.
b. Myoglobin – oxygen storage
molecule in muscles.
Common Globular
Proteins
c. Insulin – regulatory hormone for
controlling glucose metabolism.
d. Transferrin – involved in iron
transport in the blood.
e. Immunoglobulin – involved in
immune system responses.
Protein Classification
Based on FUNCTIONS
a. Catalytic Protein – as catalysts;
b. Defense Protein – body’s
immune system;
c. Transport Protein – transports
small biomolecules to other
locations in the body;
Protein Classification
Based on FUNCTIONS
d. Messenger Protein – transmits
signals to coordinate biochemical
processes.
e. Contractile Protein – proteins
necessary for all forms of
movement.
Protein Classification
Based on FUNCTIONS
f. Structural Protein – confer
stillness and rigidity.
g. Transmembrane Protein – help
control the movement of small
molecule and ions through the cell
membrane.
Protein Classification
Based on FUNCTIONS
h. Storage Protein – proteins that
binds or store small molecules for
future use.
i. Regulatory Protein – act as sites
at which messenger molecules
can bind and thereby initiate the
effect that the messenger carries.
Other Proteins
a. Glycoproteins – protein that
contains carbohydrates.
b. Lipoprotein – proteins that
contains lipid in addition to amino
acid; help suspend lipids and
transport them through the
bloodstream.
4 Major Classes of
Plasma Lipoproteins
a. Chylomicrons – transport dietary
triacylglycerol from intestine to liver
and to adipose tissue.
b. Very-Low-Density Lipoproteins
(VLDL) – transport triacylglycerols
synthesized in the liver to adipose
tissue.
4 Major Classes of
Plasma Lipoproteins
c. Low-Density Lipoproteins (LDP) –
transport cholesterol synthesized in the
liver to cells throughout the body.
d. High-Density Lipoproteins (HDP) – to
collect excess cholesterol from body
tissues and transport back to the liver
for degradation to bile acids.
Enzymes
•Simple Enzymes –
composed only of amino
acid chains.
Enzymes
• Conjugated Enzymes – an enzyme that
has a non protein part in addition to a
protein part.
a. Apoenzyme – the protein part
b. Cofactor – non protein part
c. Holoenzyme – biochemically active
conjugated enzyme.
Enzymes
•Coenzyme – serves as a cofactor
in a conjugated enzyme.
•Substrate – reactant in an
enzyme-catalyzed reaction.
6 Major Classes of
Enzymes
1. Oxireductase – oxydation-
reduction reaction.
2. Transferase – transfer of a
functional group from one
molecule to another.
6 Major Classes of
Enzymes
3. Hydrolase – hydrolysis
reaction.
4. Lyase – addition of a group to a
double bond or the removal of a
group to from a double bond.
6 Major Classes of
Enzymes
5. Isomerase – isomeration
(rearrangement of atoms) of a
substrate in a reaction.
6. Ligase – bonding together of
two molecules into one with the
participation of ATP.
Enzymes
• Lock-and-Key Model – only a
substrate whose shape and
chemical nature are
complementary to those of the
active site can interact with the
enzyme.
Enzymes
• Induced-Fit Model – enzyme
active site, although not exactly
complementary in shape to that of
the substrate, is flexible enough
that it can adapt to the shape of
the substrate.
Enzyme Inhibition
a. Reversible Competitive
Inhibition – competitive inhibitor
binds to the active site which
prevents the normal substrate from
binding to the site.
Enzyme Inhibition
b. Reversible Noncompetitive
Inhibition – noncompetitive
inhibitor binds to a site other than
active site; enzyme cannot
catalyze the reaction due to the
presence of the inhibitor.
Enzyme Inhibition
c. Irreversible Inhibition – a
molecule that forms a covalent
bond to a part of the active site,
permanently preventing substrate
from occupying it.
Vitamin
Water-soluble
Vitamins
Fat-Soluble
Vitamins
Thiamin Vitamin B12
Riboflavin Biotin
Niacin Vitamin B6
Folate Vitamin C
Pantothenic Acid
Vitamin A
Vitamin D
Vitamin E
Vitamin K
Vitamin C
• Has the simplest structure of 13 Vitamins.
• First vitamin to be discovered and synthesize
in the laboratory.
• Functions as a cosubstrate in the formation
of collagen.
• Also functions as a general antioxidant for
water-soluble substances in the blood and
other body fluids.
Vitamin B
• Thiamin (Vit. B1)
• Riboflavin (Vit. B2)
• Niacin (Nicotinic Acid, Nicotinamide,
Vit. B3)
• Vit. B6 (Pyridoxine, pyridoxal,
pyridoxamine)
Vitamin B
•Folate (Folic Acid)
•Vit. B12 (Cobalamin)
•Pantothenic Acid (Vit. B5)
•Biotin
Vitamin B
•Functions as a components of
conenzymes.
• Have a direct impact on your
energy levels, brain function and
cell metabolism.
Vitamin B
•Functions as a components of
conenzymes.
• Have a direct impact on your
energy levels, brain function and
cell metabolism.
Vitamin A
4 Major Functions:
1. Vision
2. Regulating cell differentiation
3. Maintenance of the health of
Epithelial Tissues
4. Reproduction and Growth
Vitamin D
• Maintains normal blood levels of
calcium ion and phosphate ion so
that bones can absorb these ions.
Vitamin E
• An antioxidant.
• Prevents inflammation.
• Support immune function.
Vitamin K
• Plays a role in blood clotting, bone
metabolism and regulating blood
calcium levels.

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Proteins2CEnzymes2CVitamins.pptx

  • 2. Protein Classification Based On SHAPE 1. Fibrous Protein – have simple, regular linear structures. 2.Globular Protein - molecules have peptide chains that are folded into spherical or globular shapes. 3. Membrane Protein – a protein that is found associated with a cell membrane.
  • 3. Common Fibrous Proteins a. Keratin – found in protective coverings for organisms. b. Collagen – most abundant proteins in humans; found in tendons, bone and other connective tissue.
  • 4. Common Fibrous Proteins c. Elastin – found in blood vessel and ligaments d. Myosin – found in muscular tissue. e. Fibrin – found in blood
  • 5. Common Globular Proteins a. Hemoglobin – transports oxygen from the lungs to tissue. b. Myoglobin – oxygen storage molecule in muscles.
  • 6. Common Globular Proteins c. Insulin – regulatory hormone for controlling glucose metabolism. d. Transferrin – involved in iron transport in the blood. e. Immunoglobulin – involved in immune system responses.
  • 7. Protein Classification Based on FUNCTIONS a. Catalytic Protein – as catalysts; b. Defense Protein – body’s immune system; c. Transport Protein – transports small biomolecules to other locations in the body;
  • 8. Protein Classification Based on FUNCTIONS d. Messenger Protein – transmits signals to coordinate biochemical processes. e. Contractile Protein – proteins necessary for all forms of movement.
  • 9. Protein Classification Based on FUNCTIONS f. Structural Protein – confer stillness and rigidity. g. Transmembrane Protein – help control the movement of small molecule and ions through the cell membrane.
  • 10. Protein Classification Based on FUNCTIONS h. Storage Protein – proteins that binds or store small molecules for future use. i. Regulatory Protein – act as sites at which messenger molecules can bind and thereby initiate the effect that the messenger carries.
  • 11. Other Proteins a. Glycoproteins – protein that contains carbohydrates. b. Lipoprotein – proteins that contains lipid in addition to amino acid; help suspend lipids and transport them through the bloodstream.
  • 12. 4 Major Classes of Plasma Lipoproteins a. Chylomicrons – transport dietary triacylglycerol from intestine to liver and to adipose tissue. b. Very-Low-Density Lipoproteins (VLDL) – transport triacylglycerols synthesized in the liver to adipose tissue.
  • 13. 4 Major Classes of Plasma Lipoproteins c. Low-Density Lipoproteins (LDP) – transport cholesterol synthesized in the liver to cells throughout the body. d. High-Density Lipoproteins (HDP) – to collect excess cholesterol from body tissues and transport back to the liver for degradation to bile acids.
  • 14. Enzymes •Simple Enzymes – composed only of amino acid chains.
  • 15. Enzymes • Conjugated Enzymes – an enzyme that has a non protein part in addition to a protein part. a. Apoenzyme – the protein part b. Cofactor – non protein part c. Holoenzyme – biochemically active conjugated enzyme.
  • 16. Enzymes •Coenzyme – serves as a cofactor in a conjugated enzyme. •Substrate – reactant in an enzyme-catalyzed reaction.
  • 17. 6 Major Classes of Enzymes 1. Oxireductase – oxydation- reduction reaction. 2. Transferase – transfer of a functional group from one molecule to another.
  • 18. 6 Major Classes of Enzymes 3. Hydrolase – hydrolysis reaction. 4. Lyase – addition of a group to a double bond or the removal of a group to from a double bond.
  • 19. 6 Major Classes of Enzymes 5. Isomerase – isomeration (rearrangement of atoms) of a substrate in a reaction. 6. Ligase – bonding together of two molecules into one with the participation of ATP.
  • 20. Enzymes • Lock-and-Key Model – only a substrate whose shape and chemical nature are complementary to those of the active site can interact with the enzyme.
  • 21. Enzymes • Induced-Fit Model – enzyme active site, although not exactly complementary in shape to that of the substrate, is flexible enough that it can adapt to the shape of the substrate.
  • 22. Enzyme Inhibition a. Reversible Competitive Inhibition – competitive inhibitor binds to the active site which prevents the normal substrate from binding to the site.
  • 23. Enzyme Inhibition b. Reversible Noncompetitive Inhibition – noncompetitive inhibitor binds to a site other than active site; enzyme cannot catalyze the reaction due to the presence of the inhibitor.
  • 24. Enzyme Inhibition c. Irreversible Inhibition – a molecule that forms a covalent bond to a part of the active site, permanently preventing substrate from occupying it.
  • 25. Vitamin Water-soluble Vitamins Fat-Soluble Vitamins Thiamin Vitamin B12 Riboflavin Biotin Niacin Vitamin B6 Folate Vitamin C Pantothenic Acid Vitamin A Vitamin D Vitamin E Vitamin K
  • 26. Vitamin C • Has the simplest structure of 13 Vitamins. • First vitamin to be discovered and synthesize in the laboratory. • Functions as a cosubstrate in the formation of collagen. • Also functions as a general antioxidant for water-soluble substances in the blood and other body fluids.
  • 27. Vitamin B • Thiamin (Vit. B1) • Riboflavin (Vit. B2) • Niacin (Nicotinic Acid, Nicotinamide, Vit. B3) • Vit. B6 (Pyridoxine, pyridoxal, pyridoxamine)
  • 28. Vitamin B •Folate (Folic Acid) •Vit. B12 (Cobalamin) •Pantothenic Acid (Vit. B5) •Biotin
  • 29. Vitamin B •Functions as a components of conenzymes. • Have a direct impact on your energy levels, brain function and cell metabolism.
  • 30. Vitamin B •Functions as a components of conenzymes. • Have a direct impact on your energy levels, brain function and cell metabolism.
  • 31. Vitamin A 4 Major Functions: 1. Vision 2. Regulating cell differentiation 3. Maintenance of the health of Epithelial Tissues 4. Reproduction and Growth
  • 32. Vitamin D • Maintains normal blood levels of calcium ion and phosphate ion so that bones can absorb these ions.
  • 33. Vitamin E • An antioxidant. • Prevents inflammation. • Support immune function.
  • 34. Vitamin K • Plays a role in blood clotting, bone metabolism and regulating blood calcium levels.