Co-
Factor
Co-Factor
Enzyme
Cofactors are non
protein molecules
that assist enzyme
during that Catalysis
of reactions.
• Enzyme without
its cofactor is
referred to as
an apoenzyme
• The complete,
catalytically
active enzyme is
called
holoenzyme
Prosthetic group
Matel ion
Coenzymes
Cofactor can be subdivided into three
groups
Prosthetic group
• The organic compound which are tightly bind
the cofactors are called prosthetic group
• Loosely bound cofactors serve functions like
those of prosthetic group but bind in a
transient, disposable manner either to the
enzyme or to a substrate
• They are more likely substrate because they
bind to and are released from the enzyme
just as substrate and products are formed
Prosthetic group
• Tightly integrated into the
enzyme structure by covalent or
non covalent force
B) Inorganic
•Metal are the most common
prosthetic group
Metal ions :
Cobalt ,copper,Magnesium,
Manage, Zinc, iron
A) organic
• Flavin mononucleotide
• Flavin adenine
dinucleotide
• Biotin
Continue....
• Enzyme that contain tightly bound metal ion
are termed- metalloenzyme
• enzyme that require metal ion as loosely bound
cofactor are termed as metal activated enzyme
• Metal ion facilitate binding and orientation of
the substrate
• Formation of covalent bond with reaction
intermediates
• Interact with substrate to render them more
electrophilic and nucleophilic
Role of metal ions
• Coenzymes serve as a recyclable shuttles - or
group - transfer agent that transport many
substrates from their point of generation to
their point of utilisation.
• Nicotinamide is a component of the redox
coenzyme NAD and NADP
• Riboflavin is a component of the redox
coenzyme FMN and FAD
• Thiamin participate in decarboxylation of α-
ketogluteric acids and folic acid
Coenzymes
• Hydrogen atom or hydride ions
• Methyl group
• Acyl group
• Oligosaccharide
Continue....
Chemical materials transported by coenzyme include

Co-factor

  • 1.
  • 2.
  • 3.
    Cofactors are non proteinmolecules that assist enzyme during that Catalysis of reactions. • Enzyme without its cofactor is referred to as an apoenzyme • The complete, catalytically active enzyme is called holoenzyme
  • 4.
    Prosthetic group Matel ion Coenzymes Cofactorcan be subdivided into three groups
  • 5.
    Prosthetic group • Theorganic compound which are tightly bind the cofactors are called prosthetic group • Loosely bound cofactors serve functions like those of prosthetic group but bind in a transient, disposable manner either to the enzyme or to a substrate • They are more likely substrate because they bind to and are released from the enzyme just as substrate and products are formed
  • 6.
    Prosthetic group • Tightlyintegrated into the enzyme structure by covalent or non covalent force B) Inorganic •Metal are the most common prosthetic group Metal ions : Cobalt ,copper,Magnesium, Manage, Zinc, iron A) organic • Flavin mononucleotide • Flavin adenine dinucleotide • Biotin Continue....
  • 7.
    • Enzyme thatcontain tightly bound metal ion are termed- metalloenzyme • enzyme that require metal ion as loosely bound cofactor are termed as metal activated enzyme • Metal ion facilitate binding and orientation of the substrate • Formation of covalent bond with reaction intermediates • Interact with substrate to render them more electrophilic and nucleophilic Role of metal ions
  • 8.
    • Coenzymes serveas a recyclable shuttles - or group - transfer agent that transport many substrates from their point of generation to their point of utilisation. • Nicotinamide is a component of the redox coenzyme NAD and NADP • Riboflavin is a component of the redox coenzyme FMN and FAD • Thiamin participate in decarboxylation of α- ketogluteric acids and folic acid Coenzymes
  • 9.
    • Hydrogen atomor hydride ions • Methyl group • Acyl group • Oligosaccharide Continue.... Chemical materials transported by coenzyme include