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TRANSAMINATION
• TRANSFER OF AN AMINO(-NH2) GROUP FROM AN
AMINO ACID TO A KETO ACID
DEAMINATION
• THE REMOVAL OF AMINO GROUP FROM AMINO ACID
AS NH3
AMINE
• IT IS THE COMPOUNDS AND FUNCTIONAL GROUPS
THAT CONTAIN BASIC NITROGEN GROUP WITH A
LONE PAIR
EXAMPLE: NH2,NH3…,
NITROGEN
• SYMBOL : N
• ATOMIC NUMBER : 7
• DISCOVERED AND
ISOLATED :DANIEL RUTERFORD
• OTHER NAME :AZOTE
• NITROGEN COMPOUNDS
KNOWN AS :HYDRAZINE,AZIDE,AMINE
• CHARACTER :COLOURLESS
ROLE:
IT OCCURS IN ALL ORGANISMS PRIMARILY IN
AMINO ACIDS,IT IS THE BASIC CONSITUENTS OF DNA
AND RNA,IT OCCURS IN ENERGY TRANSFER
MOLECULES LIKE ADENOSINE TRIPHOSPHATE.
HUMAN BODY IS MADE UP OF 3% NITROGEN
TRANSAMINATION
The transfer of an amino group from an amino
acid to a keto acid is known as transamination.
This process involves the interconversion of amino
acids and a pair of keto acids, catalysed by a
group of enzymes called transaminase
It is a reversible reaction
Transamination takes place in cytoplasam of all
the cells
Most aminoacids (not lys, Thr, Pro, His, Trp, Arg,
Met)
ROLE OF
TRANSAMINATION
• THE AMINO GROUP OF AMINO ACID IS UTILIZED
FOR THE FORMATION OF UREA WHICH IS AN
EXCRETORY END PRODUCT OF PROTEINS
• THE CARBON SKELETON OF AMINO ACID IS
CONVERTED INTO KETO ACIDS.
• THESE KETO ACIDS UNDERGO FOLLOWING
FUNCTIONS
UTILIZED TO GENERATE
USED FOR THE SYNTHESIS OF PYRIMIDINES
DIVERTED FOR THE FORMATION OF FAT OR
KETO BODIES
INVOLVED FOR THE FORMATION OF
UNWANTED AMINO ACIDS
DEAMINATION
• DEAMINATION IS THE REMOVAL OF AN AMINE GROUP
FROM A MOLECULE.
• ENZYMES WHICH CATALYSE THIS REACTION ARE
CALLED DEAMINASES
• IN THE HUMAN BODY, DEAMINATION TAKE PLACE IN
LIVER, HOWEVER GLUTAMATE IS ALSO DEAMINATED
IN THE KIDNEYS
• IT IS THE PROCESS BY WHICH AMINO ACIDS ARE
BROKEN DOWN IF THERE IS AN EXCESS OF
PROTEIN INTAKE
• THE AMINO GROUP IS REMOVED FROM THE AMINO
ACID AND CONVERTED TO AMMONIAElimination of amino group with
ammonia formation
TYPES OF DEAMINATION
• THERE ARE FOUR TYPES OF
DEAMINATION
OXIDATIVE DEAMINATION
REDUCTION DEAMINATION
HYDROLYTIC DEAMINATION
INTRAMOLECULAR
DEAMINATION
OXIDATIVE DEAMINATION
• AN AMINO ACID IS CONVERTED INTO
THE CORRESPONDING KETO ACID BY
REMOVAL OF THE AMINE FUNCTIONAL
GROUP AS AMMONIA
• IT OCCURS PRIMARILY OCCUR ON
HIGHER ANIMALS
• IT OCCURS MOSTLY ON GLUTAMIC
ACID
• GLUTAMATE DEHYDROGENASE IS THE
ENZYME USED
ROLE OF DEAMINATION
• IT PROVIDE AMMONIA FOR UREA
SYNTHESIS
• DEAMINATION IS THE PROCESS OF
BREAKDOWN OF AMINO ACIDS FOR
ENERGY
• IT PLAYS MAJOR ROLE IN THE
FORMATION OF GLUCOSE
• IT HELPS IN THE PRODUCTION OF
KETONE BODIES
• IT ALSO PRODUCE ACETYL CoA
Transamination & deamination

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Transamination & deamination

  • 1.
  • 2. TRANSAMINATION • TRANSFER OF AN AMINO(-NH2) GROUP FROM AN AMINO ACID TO A KETO ACID DEAMINATION • THE REMOVAL OF AMINO GROUP FROM AMINO ACID AS NH3
  • 3. AMINE • IT IS THE COMPOUNDS AND FUNCTIONAL GROUPS THAT CONTAIN BASIC NITROGEN GROUP WITH A LONE PAIR EXAMPLE: NH2,NH3…,
  • 4. NITROGEN • SYMBOL : N • ATOMIC NUMBER : 7 • DISCOVERED AND ISOLATED :DANIEL RUTERFORD • OTHER NAME :AZOTE • NITROGEN COMPOUNDS KNOWN AS :HYDRAZINE,AZIDE,AMINE • CHARACTER :COLOURLESS ROLE: IT OCCURS IN ALL ORGANISMS PRIMARILY IN AMINO ACIDS,IT IS THE BASIC CONSITUENTS OF DNA AND RNA,IT OCCURS IN ENERGY TRANSFER MOLECULES LIKE ADENOSINE TRIPHOSPHATE. HUMAN BODY IS MADE UP OF 3% NITROGEN
  • 5. TRANSAMINATION The transfer of an amino group from an amino acid to a keto acid is known as transamination. This process involves the interconversion of amino acids and a pair of keto acids, catalysed by a group of enzymes called transaminase It is a reversible reaction Transamination takes place in cytoplasam of all the cells Most aminoacids (not lys, Thr, Pro, His, Trp, Arg, Met)
  • 6.
  • 7. ROLE OF TRANSAMINATION • THE AMINO GROUP OF AMINO ACID IS UTILIZED FOR THE FORMATION OF UREA WHICH IS AN EXCRETORY END PRODUCT OF PROTEINS • THE CARBON SKELETON OF AMINO ACID IS CONVERTED INTO KETO ACIDS. • THESE KETO ACIDS UNDERGO FOLLOWING FUNCTIONS UTILIZED TO GENERATE USED FOR THE SYNTHESIS OF PYRIMIDINES DIVERTED FOR THE FORMATION OF FAT OR KETO BODIES INVOLVED FOR THE FORMATION OF UNWANTED AMINO ACIDS
  • 8. DEAMINATION • DEAMINATION IS THE REMOVAL OF AN AMINE GROUP FROM A MOLECULE. • ENZYMES WHICH CATALYSE THIS REACTION ARE CALLED DEAMINASES • IN THE HUMAN BODY, DEAMINATION TAKE PLACE IN LIVER, HOWEVER GLUTAMATE IS ALSO DEAMINATED IN THE KIDNEYS • IT IS THE PROCESS BY WHICH AMINO ACIDS ARE BROKEN DOWN IF THERE IS AN EXCESS OF PROTEIN INTAKE • THE AMINO GROUP IS REMOVED FROM THE AMINO ACID AND CONVERTED TO AMMONIAElimination of amino group with ammonia formation
  • 9. TYPES OF DEAMINATION • THERE ARE FOUR TYPES OF DEAMINATION OXIDATIVE DEAMINATION REDUCTION DEAMINATION HYDROLYTIC DEAMINATION INTRAMOLECULAR DEAMINATION
  • 10. OXIDATIVE DEAMINATION • AN AMINO ACID IS CONVERTED INTO THE CORRESPONDING KETO ACID BY REMOVAL OF THE AMINE FUNCTIONAL GROUP AS AMMONIA • IT OCCURS PRIMARILY OCCUR ON HIGHER ANIMALS • IT OCCURS MOSTLY ON GLUTAMIC ACID • GLUTAMATE DEHYDROGENASE IS THE ENZYME USED
  • 11.
  • 12.
  • 13. ROLE OF DEAMINATION • IT PROVIDE AMMONIA FOR UREA SYNTHESIS • DEAMINATION IS THE PROCESS OF BREAKDOWN OF AMINO ACIDS FOR ENERGY • IT PLAYS MAJOR ROLE IN THE FORMATION OF GLUCOSE • IT HELPS IN THE PRODUCTION OF KETONE BODIES • IT ALSO PRODUCE ACETYL CoA