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Samrat Prithviraj Chauhan Govt. College Ajmer
Department Of Chemistry
2021-2022
Submitted By: Teena Sharma
M.Sc.(Chemistry) Semester 4
Coenzyme Chemistry
CONTENT
Introduction
• Coenzyme A
• NAD+
• NADP+
• FMN
• FAD
Coenzyme
Vitamin B12
Reference
Introduction
• Fritz Albert Lipmann received the 1953
Nobel Prize in medicine or physiology “for
his discovery of coenzyme A (an important
catalytic substance in the cellular
conversion of food into energy) and its
importance for intermediary metabolism.
• Lipmann is credited with formulating the
general rules for the biotechnology of
energy transmission and was major
participant in deciphering the cellular,
catalytic, and energetic mechanisms
needed to understand how the body
builds and renews itself.
Fritz Albert Lipmann
(June 12,1899-July 24,1986)
Co-factor
A cofactor is a non protein chemical
compound that is required for the
protein ’s biological activity. These
proteins are commonly enzymes, and
cofactors can be considered “helper
molecules” that assist in biochemical
transformations.
Cofactors can be divided into two
broad groups: organic cofactors, such
as flavin or heme, and inorganic
cofactors, such as the metal ions
Mg2+ , Cu+,Mn2+, or iron-sulfur
clusters.
CO-ENZYMES
• Enzymes are conjugated proteins
• Enzymes (conjugated proteins) = Apo-enzyme
(inactive)
• The non protein part = Co-enzyme
• Apo-enzyme + Coenzyme = Holoenzyme
(active)
Apo-Enzyme and Co-Enzyme
• Coenzymes are a type of cofactor and they are bound
to enzyme’s active sites to aid with their proper
functioning.
• Coenzymes which are directly involved and altered in
the course of chemical reactions are considered to be
a type of secondary substrate.
• The non-protein part is called Co-enzyme.
• When tightly bound the Co-enzyme is called
Prosthetic-Group
Function of coenzyme
• The coenzyme is essential for the biological activity of
the enzyme.
• A coenzyme is a low molecular weight organic
substance, without which the enzyme cannot exhibit
any reaction.
• One molecule of the coenzyme is able to convert a
large number of substrate molecules with the help of
enzyme.
Some important coenzymes
Transfer of group
other than H+
oPyridoxal Phosphate
oCo-enzyme A
oCobamide co-enzyme
B12
oLipoic Acid
Transfer of H+ group
oNAD+ , NADP+
oFMN , FAD
oLipoic Acid
Coenzyme A
• Coenzyme A is a prominent coenzyme of living organism which
transfers the acyl group of carboxylic acid.
• It plays an important role in the metabolism of
proteins,carbohydrates and fats which are important reactions that
allow the energy from food to be released. For example coenzyme
A is required for the oxidation of pyruvate in the citric acid cycle.
• Coenzyme A is also important in the synthesis of cholesterol and
steroid hormones, and is required for the detoxification of a range
of harmful drugs that can accumulate in the liver.
Nicotinamide Adenine Dinucleotide
(𝑵𝑨𝑫+
)
• NAD+ is composed of two nucleotide, adenine and
nicotinamide
• The nucleotides are held together by a pair of
phosphate groups which acts as bridge and are also
bonded to a ribose sugar each.
• The function of NAD+ is to carry electrons from one
enzyme controlled reaction to another.
• NAD+is involved with redox reaction because
substrates are either oxidized , in which they lose
electrons or are reduced in which they gain electrons.
Nicotinamide Adenine Dinucleotide
Phosphate(NADP+)
• It is also known as
Coenzyme 2 or
phosphocoenzyme or TPN
(triphosphopyridine
nucleotide) or
codehydrogenase 2.
• It has one additional
phosphate group than DPN
molecule in position 2’ of
ribose molecule of
adenosine.
• It also helps in
Dehydrogenation.
Flavin Mono Nucleotide(FMN)
• It is also known as Riboflavin
phosphate.
• Riboflavin is a component of
this coenzyme. Another
name of this coenzyme is
riboflavin-5’-phosphate & it
combines with various
specific proteins
(apoenzymes) to form
enzymes e.g., L-amino acid
oxidase & cytochrome-C
reductase.
Flavin Adenine Dinucleotide (FAD)
• FAD is composed of an
adenine nucleotide, a
ribose sugar and two
phosphate groups.
• FAD can also exist as a
monophosphate and is
called flavin adenine
monophosphate (FMN).
• FAD is involved with redox
reactions.
• Like NAD, FAD can exist in
two redox states FAD and
FADH.
Vitamin B12 (cobalamin)
• Cobalamin contains Co(III)
coordinated to a corrin ring
• It is synthesized by only a
few microorganism and
Humans obtain cobalamin
from foods of animal
origin(deficiency leads to
pernicious anemia)
• Involved in synthesis of
DNA, amino acids, fatty
acids, one-C
metabolism(methylations).
Vitamin B12
Reference
Principle of Biochemistry, A.L. Lehninger,
Worth Publishers
Outlines of Biochemistry By Eric E. Conn
and P. K. Stumpf (Third Edition)
Principles of Bioinorganic Chemistry by
S.J. Lippard and J.M. Berg
Thankyou

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Teena_sem_4_Coenzyme_.pptx

  • 1. Samrat Prithviraj Chauhan Govt. College Ajmer Department Of Chemistry 2021-2022 Submitted By: Teena Sharma M.Sc.(Chemistry) Semester 4 Coenzyme Chemistry
  • 2. CONTENT Introduction • Coenzyme A • NAD+ • NADP+ • FMN • FAD Coenzyme Vitamin B12 Reference
  • 3. Introduction • Fritz Albert Lipmann received the 1953 Nobel Prize in medicine or physiology “for his discovery of coenzyme A (an important catalytic substance in the cellular conversion of food into energy) and its importance for intermediary metabolism. • Lipmann is credited with formulating the general rules for the biotechnology of energy transmission and was major participant in deciphering the cellular, catalytic, and energetic mechanisms needed to understand how the body builds and renews itself. Fritz Albert Lipmann (June 12,1899-July 24,1986)
  • 4. Co-factor A cofactor is a non protein chemical compound that is required for the protein ’s biological activity. These proteins are commonly enzymes, and cofactors can be considered “helper molecules” that assist in biochemical transformations. Cofactors can be divided into two broad groups: organic cofactors, such as flavin or heme, and inorganic cofactors, such as the metal ions Mg2+ , Cu+,Mn2+, or iron-sulfur clusters.
  • 5. CO-ENZYMES • Enzymes are conjugated proteins • Enzymes (conjugated proteins) = Apo-enzyme (inactive) • The non protein part = Co-enzyme • Apo-enzyme + Coenzyme = Holoenzyme (active)
  • 6. Apo-Enzyme and Co-Enzyme • Coenzymes are a type of cofactor and they are bound to enzyme’s active sites to aid with their proper functioning. • Coenzymes which are directly involved and altered in the course of chemical reactions are considered to be a type of secondary substrate. • The non-protein part is called Co-enzyme. • When tightly bound the Co-enzyme is called Prosthetic-Group
  • 7. Function of coenzyme • The coenzyme is essential for the biological activity of the enzyme. • A coenzyme is a low molecular weight organic substance, without which the enzyme cannot exhibit any reaction. • One molecule of the coenzyme is able to convert a large number of substrate molecules with the help of enzyme.
  • 8.
  • 9. Some important coenzymes Transfer of group other than H+ oPyridoxal Phosphate oCo-enzyme A oCobamide co-enzyme B12 oLipoic Acid Transfer of H+ group oNAD+ , NADP+ oFMN , FAD oLipoic Acid
  • 10. Coenzyme A • Coenzyme A is a prominent coenzyme of living organism which transfers the acyl group of carboxylic acid. • It plays an important role in the metabolism of proteins,carbohydrates and fats which are important reactions that allow the energy from food to be released. For example coenzyme A is required for the oxidation of pyruvate in the citric acid cycle. • Coenzyme A is also important in the synthesis of cholesterol and steroid hormones, and is required for the detoxification of a range of harmful drugs that can accumulate in the liver.
  • 11. Nicotinamide Adenine Dinucleotide (𝑵𝑨𝑫+ ) • NAD+ is composed of two nucleotide, adenine and nicotinamide • The nucleotides are held together by a pair of phosphate groups which acts as bridge and are also bonded to a ribose sugar each. • The function of NAD+ is to carry electrons from one enzyme controlled reaction to another. • NAD+is involved with redox reaction because substrates are either oxidized , in which they lose electrons or are reduced in which they gain electrons.
  • 12.
  • 13. Nicotinamide Adenine Dinucleotide Phosphate(NADP+) • It is also known as Coenzyme 2 or phosphocoenzyme or TPN (triphosphopyridine nucleotide) or codehydrogenase 2. • It has one additional phosphate group than DPN molecule in position 2’ of ribose molecule of adenosine. • It also helps in Dehydrogenation.
  • 14. Flavin Mono Nucleotide(FMN) • It is also known as Riboflavin phosphate. • Riboflavin is a component of this coenzyme. Another name of this coenzyme is riboflavin-5’-phosphate & it combines with various specific proteins (apoenzymes) to form enzymes e.g., L-amino acid oxidase & cytochrome-C reductase.
  • 15. Flavin Adenine Dinucleotide (FAD) • FAD is composed of an adenine nucleotide, a ribose sugar and two phosphate groups. • FAD can also exist as a monophosphate and is called flavin adenine monophosphate (FMN). • FAD is involved with redox reactions. • Like NAD, FAD can exist in two redox states FAD and FADH.
  • 16. Vitamin B12 (cobalamin) • Cobalamin contains Co(III) coordinated to a corrin ring • It is synthesized by only a few microorganism and Humans obtain cobalamin from foods of animal origin(deficiency leads to pernicious anemia) • Involved in synthesis of DNA, amino acids, fatty acids, one-C metabolism(methylations). Vitamin B12
  • 17. Reference Principle of Biochemistry, A.L. Lehninger, Worth Publishers Outlines of Biochemistry By Eric E. Conn and P. K. Stumpf (Third Edition) Principles of Bioinorganic Chemistry by S.J. Lippard and J.M. Berg