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common reactions:
– Transamination
– Deamination
– Decarboxylation
• All transaminases require pyridoxal
phosphate, a coenzyme derived from Vitamin
B6.
• No free NH3 , only the transfer of amino group
occurs.
• Transamination is reversible.
• Glutamate is the only amino acid that
undergoes oxidative deamination to a
significant extent to liberate free NH3 for urea
synthesis.
Transamination
In transamination
• Amino acids are degraded in the liver.
• An amino group is transferred from an
amino acid to an -keto acid, usually -
ketoglutarate.
• The reaction is catalyzed by a
transaminase or aminotransferase.
• A new amino acid, usually glutamate, and a
new -keto acid are formed.
3
Transamination reactions
Enzymatic Transamination
• Typically, -ketoglutarate
accepts amino groups
• L-Glutamine acts as a
temporary storage of nitrogen
• L-Glutamine can donate the
amino group when needed for
amino acid biosynthesis
• All aminotransferases rely on
the pyridoxal phosphate
cofactor
Amino Group Transfer - Aminotransferase
CH2 CH2
HC N H 3+ + C O C O + HC N H 3+
a la n in e -k e to g lu ta ra te p y r u v a te g lu ta m a t e
A m in o t r a n s f e r a s e ( T r a n s a m in a s e )
HC N H 3+ + C O C O + HC N H 3+
a s p a r ta t e -k e to g lu t a r a te o x a lo a c e ta te g l u t a m a te
A m in o tr a n s f e r a s e ( T r a n s a m in a s e )
13
Oxidative Deamination
• Glutamate formed by transamination reactions
is deaminated to -ketoglutarate
• Glutamate dehydrogenase - NAD+ or NADP+ is
coenzyme
Transaminase Glutamate
Dehydrogenase
Summarized above:
The role of transaminases in funneling amino N
to glutamate, which is deaminated via Glutamate
Dehydrogenase, producing NH4+.
Excretory
Forms of
Nitrogen
Fate of Individual Amino Acids
• Seven to acetyl-CoA
– Leu, Ile, Thr, Lys, Phe, Tyr, Trp
• Six to pyruvate
– Ala, Cys, Gly, Ser, Thr, Trp
• Five to -ketoglutarate
– Arg, Glu, Gln, His, Pro
• Four to succinyl-CoA
– Ile, Met, Thr, Val
• Two to fumarate
– Phe, Tyr
• Two to oxaloacetate
– Asp, Asn
Summary
of Amino
Acid
Catabolis
m