Asam amino dan

protein
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• Protein differs molecularly from carbohydrates and lipids  by
containing nitrogen

• Primary roles for :

• Structural proteins
• Enzymes
• Hormones
• Transports
• Immunoproteins

• Amino acids  ultimate structure and function of proteins

determined by genetic code stored in cell nucleus as DNA
• Proteins have four levels ofstructure, as indicated here:
• l. Primary structure: Peptide bonds are formed betureen
sequential amino acids according to directions on mRNA. The
completed protein is a linear chain of amino acids.
• 2. Secondary structure: Attractions between R groups of amino
acids create helices and pleated sheet structures.
• 3. Tertiary structure: Helices and pleated sheets are folded into
compact domains. Small proteins have one domain, and large
proteins have multiple domains
• 4. Quaternary structure: Individual polypeptides can serve as
subunits in the formation of larger assemblies, or complexes.
Subunits are bound together by numerous weak, noncovalent
interactions; sometimes they are stabilized by disulfide bonds.
For ex : four Hb monomers are joined to form the tetramer.
Essential amino acids
• Chemically amino acids are carboxylic acids with an an amino group attached to
the α-carbon
• All amino acids have this same general structure; it is the side chain also
attached to the α-carbon (the R group), which dictates the identity and function
of each amino acid.
• Note that the a-carbon is a chiral carbon, and isomers can be formed. It is the L-
isomer that is functional in the human body. Many amino acids can be
synthesized from carbon skeletons produced as intermediates in the major
metabolic pathways by a process called transamination, which adds an amino
group from another amino acid without actually producing a free amino group.
• Transamination is an important process because it allows for the production of
nonessential amino acids from metabolic intermediates while using free amino
groups, so that they are not left to produce toxic ammonia.
• -For example, pyruvate formed during glycolysis is easily converted to the amino
acid alanine by adding an amino group via the enzyme alanaine
aminotransaminase. On the other hand, essential amino acids have carbon
skeletons that humans cannot make (or cannor make enough) and can obtain
only from the diet
• Protein can also be an energy source. proteins contain over 5 kcal/g. However, using protein
for energy necessitates the removal of tlte amino group and the formation and excretion of
urea in a process involving deamination, which has a metabolic cost of over 1 kcal/g.
therefore the resulting carbon skeleton product can be used for energy at the rate of 4
kcal/g.

• These carbon skeletons can also be used to produce glucose; in fact, when the diet is low in
carbohydrate or an individual is starving, protein is the only good source of de novo
synthesis of glucose available. The process of de novo synthesis of glucose is called
gluconeogenesis.

• Oxaloacetate is moved out of the mitochondria and converted to phosphoenolpynwate

(PEP) (see Figure 3-2). From PEP the glycolytic pathway can be reversed because all the
enzymes with the exception of phosphofructokinase and glucokinase are reversible. Both of
these enzymes can be reversed by specific phosphatase enzyme when there is a need for
blood glucose.

• Since glucokinase is found primarily in the liver, it is only reversed there, making the liver
the primary site for de novo synthesis of blood glucose. Amino acids that produce carbon
skeletons that can be converted to glucose are called glucogenic amino acids. Only two of
the 20 amino acids cannot be used to produce at least some glucose. These amino acids are
lysine and threonine. They produce products that are converted to ketones and used for
energy, thus they are known as ketogenic amino acids.