Metabohtes 2O metabolites Nucleic acids Nitrogenous

Zwitter ion / dipolar ion

BIOMOLECULES • ionic form when diss slued
which are etherutilized in
metabolic functions/
synthesised in cellular
Pigments
Carotenoids and
anthocyanins
Morphine and
• Polymers of nucleotides
• Adenine (A) & Guanine (G) - Purines,
base
Phosphate
group

in water Alkaloids
codeine Cytosine(c), thymine (T) and Uracil (U)
Pentose

• Act as proton doner or machinery

Monoterpenes & - pyrimidines
Class of nitrogenous compounds proton acceptor Imetaboliles Terpenoids
diterpenes Nucleic Acids :- (i) DNA (Deoxyri-

PROTEINS +
NH 3 CH COOH
+
NH 3
R

CH COO
- H 2N
R

CH COO
-
sugars, amino acids, fatty
acids nucleosides & nucleoles
Essential oils Lemongrass oil
bonuclease acids, (ii) RNA
(Ribonucleic acids) Nucleosides
large molecules
R Toxins Abrin & ricin Type of DNA are Nitrogenous base
Zwitter ion
• BDNA – common form +
Polymers of amino acids having one or more long chain of DNA pentose
Lectins Concanavalin A
R
side of amino acids Peptide Bond DNA – helical ladder
chain Nucleotide - Nucleoside
+
Drugs Vinblastine & like Apairs with
H 3N CH COOH Carboxyl + phosphate
amino
α carbon
group curcumin T (A = T), G pairs
group
Basic - lysmi Two or more amino acids Polymeric Rubber, guns & with C (G = C)
all linked by peptide subs cellulose • ZDNA,
• ADNA,
Acidic amino acid - Glutamic acid Neutral - value
Organic molecule • CDNA
Aromatic amino acid - jyrosine, products by living
phenylalanine and Tryhophan
Living tissues are DNA (Deoxyribonuclease Glucos
organisms Statch (mono) Glycoger

Nucleic acids
treated with acid)
Fructose
Non – essential R trichloro acetic (mmo)
Essential Amino Homopotymers
acids amin acids NH3 CH C OH + NH CH COO- acid and grind it inulin
O to form slurry chitin cellulose
• Synthesized in the H H H (N- acetyl – Glucose
• Can not be synthesised
body H glucosamine)
in the body N C C N C COOH
Gylanic, Alanis, serine, Composed of RNA (Ribonucleic acids)
Isoleucine, Levine H
aspartic acid, R O R H,O,N,P,S.
methionine, Phenylalanine, Asparagine, Vmax
Threonine, Tryptophane, Peptide

Rate of reaction
cysteine, Glutaric acid,
lysine, valvule, Arginine Glutamine protein, Bond
Histidine Tyrosine Polysaccharides ½Vmax No inhibitor

Competitive inhibitor

•
Analysis of chemical o Starch, cellulose, glycogen
Structure of Portion composition of o Carbohydrates with a long chain Km
of polymers Substrate concentration [S]
organic Compounds. Proteins nucleic o Homopolymers (Consist of single
mono- saccharide Units)
• Primary structure - sequence of Amino acids, acids carboh- Heteropolymers (made of different
which are joined by peptide bonds (Add linage)
• Secondary structure - Luige level of portion
Holoenzyme ydrates and lipids monosa charades Units)
organization. eg:- Keratin Inorganic chemical are common
α helix:- polypeptide chain twisted into
helical form
composition biomolecules No inhibitor

β- pleated:- 2 or more polypeptide

Apoenzyme Cofactors Non-competitive inhibitor

R a te o f r e a c ti o n
Vmax
chain lime up side by side
• Tertiary structure - Helical polypeptide Protein palt non protein Sample of tissue
chain is folded into a Vmax
woolen wall, ex:- myoglobin part should be treent
• Quaternary structures:- Composed of Catalytic Prosthetic to obtaisi ash.
two or more polypepted Glycosidic bonds link
chains – held together by hydrophobia
activity of group monosaccharides Transition state Km

issler actions, illetrostalic the enzyme Enzymes Substrate concentration [S]

interactions & H – bonds , Ex:- Hemoglobin • Tightly bond Activation energy

without enzyme
Triglycerides

Potential Energy
Non-competitive inhibition
to enzyme Activation
energy with enzyme

LIPIDS Coenzyme Substrate (s)

fats (high except Ribozymes Mostly Biological

oil (low meting
• Organic point) meting points)
(nucleic acid) proteinaceous catalyst Product (P)
Progress of reaction
• Water insoluble compounds O

• Saturaled fatly acids- No double bonds Oxidoreductase Activation Base

not bound • minimous energy • High or low
• Unsaturated fatly acids double bonds Lecithin transferases
tightly to Hydrolases
amount of temperature 3‘
are present inactivates the O O
• Fatly acid - has a COOH group apoenzyme lyases energy
enzyme actively P
Phosphodiester
• required to bond
attached to an group present in cell membrane isomerases activate subs- O O
• Plastic acid – 16 carbons ligases trate to a
5‘
CH2
Phosphate
• Arachidonic acid – 20 carbons condition in • pH, & substrali
• Esterified through ester bond Glycerol – Simple amino acids Phospholiprid
which they conch - affect O
forming mono, di and triglycerides (Trihydroxy propane) enzyme can undergo enzyme actively Base
Phosphorus + phosphorylated chemical each
classification
organic Compound.

anand_mani16 DR. Anand Mani https://www.anandmani.com/ https://discord.io/anandmani t.me/anandmani001