Carbohydrate, Lipids,

Protein
D R . Q A R I N A H A S YA L A P U T R I , M . B I O M E D

B I O C H E M I S T R Y D E PA R T M E N T

FA C U LT Y O F M E D I C I N E – U N I V E R S I TA S M U H A M M A D I YA H S U M AT E R A U TA R A
Classification of Carbohydrate,
Lipids and Nitrogen Containing
Compound
Carbohydrate
 Carbohydrates are widely distributed in plants and animals
Glucose: the most important carbohydrate
Absorbed into the bloodstream as glucose, other sugars are
converted into glucose

Biomedical Major metabolic fuel of mammals and a universal fuel of the

fetus
Importance Precursor for synthesis of all the other carbohydrates in the
body
Diseases associated: diabetes mellitus, galactosemia,
glycogen storage diseases, and lactose intolerance.
 Aldehyde or
ketone derivatives
(CH2O)n Classification:
of polyhydric
alcohols

Monosaccharides Disaccharides Oligosaccharides Polysaccharides

 Cannot be hydrolyzed into simpler
carbohydrates

Trioses
Classification based Tetroses
Monosaccharides on the number of Pentoses
Hexoses
carbon atoms: Heptoses

Classification based Aldoses

on contained group: Ketoses

Trioses
Tetroses
Pentoses
Hexoses
Heptoses
DISAKARIDA
-laktosa : hidrolisis  galaktosa & glukosa

-Maltosa: hidrolisis  2 mol glukosa

-Sukrosa: hidrolisis  fruktosa & glukosa

-Trehalosa: hidrolisis  2 mol glukosa

Maltosa: Gula pereduksi karena mempunyai
gugus karbonil yang bebas dan dapat dioksidasi

Mengandung residu 2 mol D-glukosa

Enzim amilase liur  menghidrolisis pati 

maltosa

Enzim maltase (usus)  maltosa  2 mol. D-

glukosa

Disakarida Selobiosa  2 D-glukosa, tapi

dihubungkan oleh ikatan Beta (1-4)
LAKTOSA
Lactosa, atau gula susu, terdiri dari galaktosa &
glukosa, dengan ikatan b(14)

Laktosa  hidrolisis menjadi glukosa dan

galaktosa

Galaktosa tidak dapat langsung digunakan,

tapi harus dikonversi menjadi glukosa
GALAKTOSA
 Adalah penyakit defisiensi genetik
Pada lintasan metabolisme D-galaktosa  D-glukosa
Galaktosa-1PO4 UDP-D-galaktosa 
UDP-glukosa glukosa 1-PO4 (enzim: UDP-glukosa 1-fosfat
uridintransformase)
GALAKTOSEMIA Enzim mengalami kerusakan (genetik)
Galaktosa  gagal diubah menjadi glukosa
Terakumulasi di dalam darah dan jaringan
Hati dan organ lain membesar, katarak, retradasi mental
Defisiensi genetik ini muncul pada bayi
Dapat diatasi dengan mencegah minum susu dan
produk2nya
 Laktosa + laktase (usus)  D-galaktosa+D-glukosa

Bayi dan anak mampu mencerna laktosa

Sebagian besar orang dewasa di dunia kurang enzim

laktase  tidak tahan thd. Susu
INTOLERANSI Minum susu  laktosa menumpuk di lumen usus halus
LAKTOSA
Tanda-tanda klinis:

Kembung, Mual, Kejang perut,Nyeri dan diare

Prevalensi: Denmark (3%), Thailand (97%)

 CADANGAN ENERGI

Polimer heksosa:

• Glikogen (hewan)  glukosa

• - Amilum (tumbuhan)  glukosa
• - Inulin (tumbuhan)  fruktosa
POLISAKARIDA
Polimer pentosa:

• -hemiselulosa: Arabinosa

STRUKTURAL

• - Sellulosa (tumbuhan)
• - khitin
Fig 9-14

1.0 m 0.10 m
Polisakarida
Tumbuhan menyimpan glukosa sebagai amylosa
atau amilopektin, polimer glukosa disebut
sebagai amilum. Glukosa disimpan dalam bentuk
polimer sehingga mengurangi efek osmotik.
Amilosa adalah polimer glukosa dengan ikatan
a(14). Terdapat dalam bentuk konformasi helix.
Bagian akhir dari polisakarida dimana suatu
anomerik C1 tidak terdapat dalam ikatan
glikosidik disebut “reducing end”.
 CH2OH CH2OH
H O H H O H amylopectin
H H
OH H OH H 1
O
OH
O
H OH H OH

CH2OH CH2OH 6 CH2 CH2OH CH2OH

H O H H O H H 5 O H H O H H O H
H H H H H
OH H OH H OH H 1 4 OH H OH H
4 O O
O O OH
OH
3 2
H OH H OH H OH H OH H OH

Amilopektin merupakan polimer glukosa yang terutama terdidi dari ikatan a(14),
tetapi juga mempunyai cabang yang dibentukoleh ikatan (16). Cabang-cabang itu bisa
panjang sekali.
Cabang itu menghasilkan suatu bentuk struktur yang kompak dan menyediakan banyak
ujung akhir dimana enzim pemecah (cleavage enzymes) dapat memutusnya.
 CH2OH CH2OH
H O O
glycogen
H H H
H H
OH H OH H 1
O
OH
O
H OH H OH

CH2OH CH2OH 6 CH2 CH2OH CH2OH

H O H H O H H 5 O H H O H H O H
H H H H H
OH H OH H OH H 1 4 OH H OH H
4 O O
O O OH
OH
3 2
H OH H OH H OH H OH H OH

Glikogen, polimer glukosa untuk penyimpanan glukosa pada

binatang, mempunyai struktur polimer menyerupai polimer pada
tumbuhan amilopektin, tetapi glikogen mempunyai lebih banyak
ikatan cabang a(16).
Bentuk dengan cabang banyak ini menyebabkan pembebasan yang
lebih cepat dari glukosa pada glikogen, mis : pada otot sewaktu
berlatih. Hal ini sangat penting untuk binatang.
Lipid
Lipids are the group of biological macromolecules that have a major hydrocarbon component
and are mostly nonpolar and hydrophobic
Functionally, lipids are important in cell membrane structure and in energy production
There are three main families of lipids:
◦ Fats
◦ Steroids
◦ Phospholipids/ Lipid- complex

Introduction
 SIMPLE LIPIDS:

Ester of fatty acids with various alcohol

CLASSIFICATION
OF LIPID
a. FATS: Esters of fatty acids with glycerol.

• Oils is are fats in the liquid state.

b. Waxes: Esters of fatty acids with higher

molecular weight monohydric alcohols.
 fatty acid

Glycerol fatty acid

carbohydrate

Glycolipid
fatty acid Sphingosine

carbohydrate

Glycosphingolipid
 2. COMPLEX LIPIDS
Ester of fatty acids containing groups in addition to an
alcohol and a fatty acids
CLASSIFICATION a. PHOSPHOLIPIDS
OF LIPID Lipids containing: a phosphoric acid residue, nitogen
containing bases, & other substituents, eg.in
GLYCEROPHOSPHOLIPIDS (the alcohol is glycerol) &
SPINGOPHOSPHOLIPIDS (the alcohol is sphingosine)
 fatty acid

Glycerol Unsaturated fatty acid

Phosphric acid recidues nitrogen bases

Glycerophospholipid

fatty acid sphingosine Phosphric acid recidues nitrogen bases

Sphingophospholipid
 b. GLYCOLIPIDS (GLYCOSPHINGOLIPIDS)
Lipids containing: a fatty acids, sphingosine, &
carbohydrate
CLASSIFICATION c. OTHER COMPLEX LIpid: sulfolipids , aminolipids, &
lipoproteins.
OF LIPID
d. PRECURSOR & DERIVED LIPIDS: fatty acids, glycerol,
steroids, other alcohols, fatty aldehydes, ketone
bodies, hydrocarbons, lipid-soluble vitamins, &
hormones.
Phospholipids

Sumber: Medical Physiology , Updated Second Edition Copyright c 2012 by

Saunders, an imprint of Elsevier Inc.
Structures of some
common membrane
lipids
Sumber: Medical Physiology , Updated
Second Edition Copyright c 2012 by
Saunders, an imprint of Elsevier Inc.
Sumber: Medical Physiology , Updated
Second Edition Copyright c 2012 by
Saunders, an imprint of Elsevier Inc.
Fats and Fatty Acids
A fat, also known as a triacylglycerol or triglyceride, is a
glycerol linked to three fatty acids.
Condensation reactions between glycerol hydroxyl groups and
fatty acid carboxyl groups form ester linkages joining the two
subunits.
Fatty acids can be either saturated or unsaturated.

45
 STRUCTURE
•Triglyceride - three fatty acids attached to a
TRIGLYCERIDES glycerol backbone
•Diglyceride – two fatty acids +glycerol
•Monoglyceride – one fatty acid +glycerol
Fatty Acids Triglyceride
 •Major lipid in the body and diet
•Stored fat provides about 60% of the body’s resting energy
FUNCTIONS OF needs – compactly!

TRIGLYCERIDES •Insulation and protection

•Carrier of fat-soluble compounds
•Sensory qualities – flavor and texture
 CHAIN LENGTH
•Short chain = less than 6 carbons

FATTY ACIDS •Medium chain = 6-10 carbons

•Long chain = 12 or more carbons
•The shorter the carbon chain, the more liquid
FATTY ACIDS
FATTY ACIDS
SATURATION
•SATURATED FATTY ACID = If all the carbon atoms in
the chain are joined with single bonds, and the
remaining bonds are attached to hydrogen
•UNSATURATED FATTY ACID = If adjoining carbons are
joined by double bonds
UNSATURATED FATTY ACIDS

UNSATURATED

One double bond = monounsaturated fatty acid

Two or more double bonds = polyunsaturated fatty acid

TWO TYPES OF •CIS - hydrogens on the carbons joined by a double bond are
BOND on the same side = the carbon chain is bent

FORMATION •TRANS – hydrogens on the carbons joined by a double bond

are on the opposite side = the carbon chain is straighter
•Long-chain saturated fatty acids stack tightly and form solids at room
temperature
•Monounsaturated and polyunsaturated fatty acids don’t stack compactly and
are liquid at room temperature
•Short-chain saturated fatty acids are also liquid at room temperature

FATTY ACIDS
FATTY ACIDS
•Nonessential Fatty Acids – our body can make certain fatty
acids so they are not required in the diet
•Essential Fatty Acids – our bodies cannot make C-C double
bonds before the 9th carbon from the methyl end, so we must
get these fatty acids from our diet
•EFAS = omega-6 linoleic acid & omega-3 alpha-linolenic acid
 •Omega-3 Fatty Acid – double bond at carbon 3
ESSENTIAL •Omega-6 Fatty Acid – double bond at carbon 6

FATTY ACIDS •Omega-9 Fatty Acid – double bond at carbon 9

•*count carbons from the methyl (omega) end

Omega 3

Omega 6

Omega 9
 Omega-3: Omega-6:

• Alpha-Linolenic Acid (ALA) • Linoleic Acid

• Eicosapentaenoic Acid • Arachidonic Acid
(EPA)
• Docosahexaenoic Acid
(DHA)

OMEGA-3 & OMEGA-6

•Flaxseed, soybean oil, walnuts, some leafy dark green vegetables
(ALA)
•Fatty fish: salmon, tuna, and mackerel, fish oils (EPA and DHA)

SOURCES OF OMEGA-3
FATTY ACIDS
SOURCES OF •Seeds, nuts, common vegetable oils: corn, safflower,
cottonseed, sunflower seed, peanut (linoleic acid)
OMEGA-6 •Meat (arachidonic acid)
FATTY ACIDS
Nitrogen Containing
Compounds
 The addition of nitrogen into
an organic framework leads to
two families of molecules

Classification:
Amines: compounds containing Amides: compounds that have
a nitrogen atom bonded in a a nitrogen atom bonded to one
hydrocarbon framework side of a carbonyl group
Amines
An organic compound that can be considered to be a
derivative of ammonia (NH3)
Contain carbon-nitrogen bonds

Classified according to the number of carbon atoms

bonded directly to the nitrogen atom
A primary (1°) amine has one alkyl (or aryl) group on the
nitrogen atom
A secondary (2°) amine has two alkyl (or aryl) group on
the nitrogen atom
A tertiary (3°) amine has three alkyl (or aryl) group on
the nitrogen atom
Amides
Derived from carboxylic acids
A carboxylic acid contains the −COOH functional group, and in an amide the −OH part of that
group is replaced by an −NH2 group  −CONH2 group
Classification:
◦ Primary
◦ Secondary
◦ Tertiary
Primary Amides
Named by changing the name of the acid by dropping the -oic acid or -ic acid endings and
adding –amide
The carbonyl carbon is given the #1 location number
It is not necessary to include the location number in the name because it is assumed that the
functional group will be on the end of the parent chain

methanamide or formamide (left), ethanamide or acetamide (center) , benzamide (right)

Secondary Amides
Named by using an uppercase N to designate that the alkyl group is on the
nitrogen atom

Alkyl groups attached to the nitrogen are named as substituents

The letter N is used to indicate they are attached to the nitrogen

N-methylpropanamide
Tertiary Amides
Named in the same way as secondary amides, but with two N’s
Characteristics and
Classification of Protein
and Amino Acids
Protein
Account for more than 50% of the dry mass of most cells

Functions:

• Structural support
• Storage
• Transport
• Cellular communications
• Movement
• Defense against foreign substances
 Linear polymers of aa via amide linkages form peptides
(1-10), polypeptides (11-100) and proteins (>100)

Eg: Aspartame (2), glutathione (3), vasopressin (9),

insulin (51)

Proteins have a amino-end and carboxyl-end

Proteins
In the lab, proteins can be hydrolyzed (to aa) by strong
acid treatment

Physiologic hydrolysis by peptidases and proteases

 Amino acid sequence determines primary structure

Unique for each protein; innumerable possibilities

Primary Gene sequence determines aa sequence

Structure
Each aa is called a residue; numbering (& synthesis)
always from –NH2 end toward –COOH end

Amino acids covalently attached to each other by an

amide linkage called as a peptide bond.
 Peptide Bond
• Peptide bonds are planar (2 a-C and -O=C-N-H- in one plane)
• Partial double bond character due to resonance structures of peptide bond
(bond length is 1.32 Ao instead of 1.49 Ao (single) or 1.27 Ao (double)
• Due to steric hindrance, all peptide bonds in proteins are in trans
configuration
• The 2 bonds around the a-carbon have freedom of rotation making proteins
flexible to bend and fold
 Secondary structure is the initial
folding pattern (periodic repeats)
of the linear polypeptide

Secondary 3 main types of secondary

structure: a- helix, b-sheet and
Structure bend/loop

Secondary structures are stabilized

by hydrogen bonds
 The a-helix
• The a-helix is right-handed or clock-wise (for L- isoforms left-handed
helix is not viable due to steric hindrance)
• Each turn has 3.6 aa residues and is 5.4 Ao high
• The helix is stabilized by H-bonds between –N-H and –C=O groups of
every 4th amino acid
• a-helices can wind around each other to form ‘coiled coils’ that are
extremely stable and found in fibrous structural proteins such as keratin,
myosin (muscle fibers) etc
 -Pleated Sheet
• Extended stretches of 5 or more aa are called - strands
• -strands organized next to each other make -sheets
• If adjacent strands are oriented in the same direction (N-end to C-end), it is
a parallel -sheet, if adjacent strands run opposite to each other, it is an
antiparallel -sheet
• There can also be mixed -sheets
• H-bonding pattern varies depending on type of sheet
• -sheets are usually twisted rather than flat
• Fatty acid binding proteins are made almost entirely of -sheets
 Polypeptide chains can fold upon
themselves forming a bend or a loop.
Usually, 4 aa are required to form the
turn

Bend / Loop H-bond between the 1st and 4th aa in the

turn
Bends are usually on the surface of
globular proteins
Proline residues frequently found in
bends / loops
 Tertiary Structure
3D folding or ‘bundling up’ of the protein

Non-polar residues are buried inside, polar residues are exposed outwards to aqueous environment

Many proteins are organized into multiple ‘domains’

Domains are compact globular units that are connected by a flexible segment of the polypeptide

Each domain is contributes a specific function to the overall protein

Different proteins may share similar domain structures, eg: kinase-, cysteine-rich-, globin-domains
 Tertiary Structure
• 5 kinds of bonds stabilize tertiary structure: H-bonds, van der waals
interactions, hydrophobic interactions, ionic interactions and
disulphide linkages
• In disulphide linkages, the SH groups of two neighboring cysteines
form a –S-S- bond called as a disulphide linkage. It is a covalent
bond, but readily cleaved by reducing agents that supply the
protons to form the SH groups again
• Reducing agents include -mercaptoethanol and DTT
 association of more than one polypeptides

Each unit of this protein is called as a subunit

and the protein is an oligomeric protein

Quaternary Subunits (monomers) can be identical or

Structure different

The protein is homopolymeric or

heteropolymeric

Disulfide bonds usually stabilize the oligomer

A protein consists of one or more polypeptides
Polypeptides are polymers built from the same
set of 20 amino acids
Amino acids are organic molecules with carboxyl
and amino groups
Amino acids differ in their properties due to
differing side chains, called R groups
Hydrophobic / non-polar R group: Glycine,
alanine, valine, leucine, isoleucine, methionine,
proline, phenylalanine, tryptophan
Classification
Polar R group (net charge 0 at pH 7.4): Serine,
of Amino
threonine, cysteine, tyrosine, asparagine,
glutamine, histidine
Acids
Based on
Polarity
Polar R group (Charged ion at pH 7.4):
aspartate, glutamate, lysine, arginine
Aliphatic: gly (G), ala (A) , val (V), leu (L), ile (I)

Aromatic: Trp (W), Phe (F), Tyr (Y), His (H),

Sulphur : Met (M), Cys (C)

Classification
Hydroxyl: Ser (S), Thr (T), Tyr (Y)
of Amino
Cyclic: pro (P)
Acids
Carboxyl: asp (D), glu (E)
Based on R-
Amine: lys (K), arg (R)
group
Amide: asn (N), gln (Q)
Non-polar, hydrophobic aliphatic and aromatic amino acids
often cluster together an are found in the interior of proteins
Polar amino acids contain functional groups in their side chains that can
Hydrogen Bond with other groups.
They are hydrophilic and often found on the surface of proteins
Amino acids with hydroxyl groups in their
sidechains (S, T, Y)
Amino Acids that Carry a Charge in Their
Side Chain at Neutral pH (D, E, K, R, H)
Asparagine (N) is a derivative of Aspartic Acid (D)
Glutamine (Q) is derivative of Glutamic Acid (E)
Aromatic Side Chain (F, W, Y)
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