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DEAMINATION
OF
AMINO ACID
Name – sayali Jagtap
Roll no - 40
DEAMINATION
OXIDATIVE
DEAMINATI
ON
NON-
OXIDATIVE
DEAMINATION
OXIDATIVE DEAMINATION
• The liberation of free ammonia from
amino group of amino acids,when
coupled with oxidation known as
oxidative deamination.
• Site- mostly in liver and
kidney
OXIDATIVE DEAMINATION BY
GLUTAMATE DEHYDROGENASE
• The alpha amino group of most amino acid are ultimately transferred
to alpha ketoglutarate by transamination forming L-glutamate.
• The L-glutamate undergoes oxidative deamination by the action
of L –glutamate dehydrogenase to liberate ammonia.
• It also requires NAD or NADP as an oxidizing agent.
• Thus,net removal of alpha amino groups to ammonia requires the
combined action of glutamate transaminase and glutamate
dehydrogenase.
Metabolic significance
• It is a reversible reaction .
• Catabolically ,it channels nitrogen from glutamate to
ammonia .
• Anabolically it catalyzes animation of alpha ketoglutarate
by free ammonia to form glutamate.
• Regulation of glutamate dehydrogenase activity.
OXIDATIVE DEAMINATION
BY AMINOACID OXIDASES
• Oxidative deamination occur by both L-and D-amino acid OXIDASES.
• Site – occur in kidney and liver.
• Amino acid oxidases uses FMN or FAD as coenzyme
• This coenzyme oxidize amino acids to an alpha imino acid .alpha imino acid
is an unstable compound which decomposes to the corresponding alpha
keto acid with release of ammonium ion .
• In this reaction oxygen is reduced to hydrogen peroxide ,
which is later decomposed by catalase .
METABOLIC SIGNIFICANCE
• L-amino acid oxidase plays minor
role in amino acid catabolism.
• Activity of D-amino acid oxidase is than that
of L- amino acid oxidase
• D-amino acid present in diet are metabolized by D – amino
acid oxidase in liver.
NON-OXIDATIVE DEAMINATION
BY AMINOACID DEHYDRATASE
• The alpha amino groups of serine and threonine can be
directly deaminated into ammonium ion,this are hydroxy
amino acid .
• Direct deamination,without oxidation
• These direct deamination is catalyzed by serine
dehydratase and threonine dehydratase in which
pyridoxal phosphate (PLP) is the coenzyme .
deamination - sayali jagtap.pdf
deamination - sayali jagtap.pdf

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deamination - sayali jagtap.pdf

  • 1. DEAMINATION OF AMINO ACID Name – sayali Jagtap Roll no - 40
  • 3. OXIDATIVE DEAMINATION • The liberation of free ammonia from amino group of amino acids,when coupled with oxidation known as oxidative deamination. • Site- mostly in liver and kidney
  • 4. OXIDATIVE DEAMINATION BY GLUTAMATE DEHYDROGENASE • The alpha amino group of most amino acid are ultimately transferred to alpha ketoglutarate by transamination forming L-glutamate. • The L-glutamate undergoes oxidative deamination by the action of L –glutamate dehydrogenase to liberate ammonia. • It also requires NAD or NADP as an oxidizing agent. • Thus,net removal of alpha amino groups to ammonia requires the combined action of glutamate transaminase and glutamate dehydrogenase.
  • 5.
  • 6. Metabolic significance • It is a reversible reaction . • Catabolically ,it channels nitrogen from glutamate to ammonia . • Anabolically it catalyzes animation of alpha ketoglutarate by free ammonia to form glutamate. • Regulation of glutamate dehydrogenase activity.
  • 7. OXIDATIVE DEAMINATION BY AMINOACID OXIDASES • Oxidative deamination occur by both L-and D-amino acid OXIDASES. • Site – occur in kidney and liver. • Amino acid oxidases uses FMN or FAD as coenzyme • This coenzyme oxidize amino acids to an alpha imino acid .alpha imino acid is an unstable compound which decomposes to the corresponding alpha keto acid with release of ammonium ion . • In this reaction oxygen is reduced to hydrogen peroxide , which is later decomposed by catalase .
  • 8.
  • 9. METABOLIC SIGNIFICANCE • L-amino acid oxidase plays minor role in amino acid catabolism. • Activity of D-amino acid oxidase is than that of L- amino acid oxidase • D-amino acid present in diet are metabolized by D – amino acid oxidase in liver.
  • 10. NON-OXIDATIVE DEAMINATION BY AMINOACID DEHYDRATASE • The alpha amino groups of serine and threonine can be directly deaminated into ammonium ion,this are hydroxy amino acid . • Direct deamination,without oxidation • These direct deamination is catalyzed by serine dehydratase and threonine dehydratase in which pyridoxal phosphate (PLP) is the coenzyme .