Chapter 4 Carbohydrates Metabolism The biochemistry and molecular biology department of CMU.
INTRODUCTION TO BIOCHEMISTRY AND CARBOHYDRATES BY DR. MARYJANE.
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Transcript of INTRODUCTION TO BIOCHEMISTRY AND CARBOHYDRATES BY DR. MARYJANE.
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INTRODUCTION TO BIOCHEMISTRY
ANDCARBOHYDRATES
BYDR. MARYJANE
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Biochemistry is the study of the chemical processes and
transformations in living organisms
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Biochemistry is the study of the structure and function of cellular components, such as proteins, carbohydrates, lipids, nucleic acids, and other biomolecules
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AMINO ACIDS
BYDR. MARYJANE
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INTRODUCTION
• There are about 300 amino acids that occur in nature but only 20 of them are found in proteins.
• Each amino acids has the following four groups or atoms attached to the alpha (α) carbon:
• 1. amino group (NH₂)• 2. carboxyl group (COOH)• 3. hydrogen atom (H)• 4. distinctive side chain or radical group (R)
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STUCTURE OF AMINO ACIDS
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Showing you how the R group varies
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• All amino acids can either be:• 1. D- amino acids, i.e., the amino group is
attached to the right of the α-carbon. This is found in some antibiotics and bacteria cell walls• 2. L-amino acid, i.e., the amino group is
attached to the left of the α-carbon. This is found in proteins.• These two forms are called stereoisomers
or enantiomers
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Classification according to charge and polarity Amino acids with Nonpolar side chains or
R-groups Amino acids with Polar side chains: a. uncharged polar side chains b. acidic side chains c. basic side chains
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Nonpolar side chains
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CLASSIFICATION OF AMINO ACIDS• A. Amino acids with nonpolar side R- Groups.• Glycine (Gly)• Alanine (Ala)• Valine (Val)• Leucine(Leu)• Isoleucine (Ile)• Phenylalanine (Phe)• Tryptophan (Trp)• Methionine (Met)• Proline (Pro)
• Proline differs from the other amino acids in that it the α-amino N form a rigid, five membered ring structure and also contains a secondary amino group rather than a primary amino group. Therefore it is frequently referred to as an imino acid
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Imino acid proline
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AMINO ACIDS WITH POLAR R-GROUPS
• Amino acids with uncharged polar R-Groups:• Serine• Threonine• Tyrosine• Asparagine• Glutamine• cysteine
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Disulfide bond• The side chain of cysteine
contains a sulfhydryl group (-SH). The –SH group of two cysteines can become oxidized to form cystine which contains a covalent cross link called disulfide bond (-S-S-).
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• C. Amino acids with acidic R- Groups: are proton donors & negatively charged at physiologic pH
• Aspartic acid (Asp) • Glutamic acid (Glu)
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• D. amino acids with basic R- Groups: are proton acceptors & positively charged at physiologic pH
• Histidine (His)• Lysine (Lys)• Arginine (Arg)• Histidine and arginine are needed in growing
children
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CLASSIFICATION ACCORDING TO THE AMINO ACID STRUCTURE.
• Can either be aromatic or aliphatic• A. aromatic amino acids• B. aliphatic amino acids
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Aromatic amino acids
Phenylalanine: contains a benzene ring Tyrosine: contains a phenol group Tryptophan: contains a heterocyclic
structure, indole
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Amino Acids Abbreviations
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Nutritional classification of amino acids Essential amino acids Non essential amino acids
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Essential amino acids
Arginine Histidine Isoleucine Leucine Threonine Lysine Methionine Phenyalanine Tryptophan Valine Histidine and arginine are essential only for
periods when cell growth exceeds production such as during childhood
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Non essential amino acids
Tyrosine Glycine Alanine Cysteine Serine Aspartate Asparagine Glutamate Gutamine proline
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METABOLIC CLASSIFICATION• Are classified according to their metabolic fate in the body
into
• Glucogenic amino acid• Ketogenic amino acid• Both glucogenic and ketogenic amino
acid
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• ketogenic amino acids: these gives ketone bodies. Leucine and Lysine are the only ketogenic amino acid.
• glucogenic and ketogenic amino acids: these gives both ketone bodies and glucose. They are: phenylalanine, tyrosine, tryptophan and isoleucine.
• glucogenic amino acids: it gives glucose. They include the rest of amino acids not included in the 1st and 2nd groups, they are: alanine, valine, proline, methionine, glycine, serine, threonine, cysteine, asparagine, glutamine, aspartate, glutamic acid, arginine and histidine.
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FUNCTIONS OF AMINO ACIDS.• A. structural functions: these are amino acids found in the
structure of:• 1. body peptides and proteins: e.g., plasma proteins, tissue
proteins, enzymes etc.• 2. hormones; some hormones are amino acid derivatives
e.g., thyroxine and catecholamines.• 3. amines; some amino acids give corresponding amines by
decarboxylation e.g. histidine gives histamine.• B. Neurotransmitters: some amino acids, glutamate acts as
neurotransmitters.• C. Detoxification: some amino acids are used in
detoxification reactions e.g., glycine• D. Health and growth: essential amino acids support growth
in infants and maintain health in adults.
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TyrosineTyrosine is involved in the synthesis of:
DopamineCatecholamines-Epinephrine,nor epinephrine,dopamineChemical messengers-Transmit impulses across the neurons in the brain and onward to the musclesControl muscle movement
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TyrosineNor Epinephrine
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TyrosineMelaninTyrosinase-Deficiency-Albinism
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Phenylalanine
Epinephrine
Phenylalanine
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TryptophanTryptophan is involved in the synthesis of:
Melatonin
Serotonin
Niacin