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Transamination - Wikipedia PDF

Transamination is a chemical reaction that transfers an amino group from one amino acid to an alpha-keto acid, catalyzed by transaminase enzymes, forming new amino acids. This reaction allows for the interconversion of amino acids and is one of the major pathways for degrading or biosynthesizing amino acids. The reaction involves transferring the amino group between the amino acid and alpha-keto acid, using pyridoxal phosphate as a cofactor to carry the amino group between intermediate forms. This occurs through a ping pong bi bi mechanism involving three steps of transimination, tautomerization, and hydrolysis.

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636 views12 pages

Transamination - Wikipedia PDF

Transamination is a chemical reaction that transfers an amino group from one amino acid to an alpha-keto acid, catalyzed by transaminase enzymes, forming new amino acids. This reaction allows for the interconversion of amino acids and is one of the major pathways for degrading or biosynthesizing amino acids. The reaction involves transferring the amino group between the amino acid and alpha-keto acid, using pyridoxal phosphate as a cofactor to carry the amino group between intermediate forms. This occurs through a ping pong bi bi mechanism involving three steps of transimination, tautomerization, and hydrolysis.

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Transamination

Aminotransfer reaction between an amino acid and an


alpha-keto acid

Transamination, a chemical reaction that


transfers an amino group to a ketoacid to
form new amino acids. This pathway is
responsible for the deamination of most
amino acids. This is one of the major
degradation pathways which convert
essential amino acids to non-essential
amino acids (amino acids that can be
synthesized de novo by the organism).

Transamination in biochemistry is
accomplished by enzymes called
transaminases or aminotransferases. α-
ketoglutarate acts as the predominant
amino-group acceptor and produces
glutamate as the new amino acid.

Aminoacid + α-ketoglutarate ↔ α-keto


acid + Glutamate
Glutamate's amino group, in turn, is
transferred to oxaloacetate in a second
transamination reaction yielding
aspartate.

Glutamate + oxaloacetate ↔ α-
ketoglutarate + aspartate

Mechanism of Action
Transamination catalyzed by
aminotransferase occurs in two stages. In
the first step, the α amino group of an
amino acid is transferred to the enzyme,
producing the corresponding α-keto acid
and the aminated enzyme. During the
second stage, the amino group is
transferred to the keto acid acceptor,
forming the amino acid product while
regenerating the enzyme. The chirality of
an amino acid is determined during
transamination. For the reaction to
complete, aminotransferases require
participation of aldehyde containing
coenzyme, pyridoxal-5'-phosphate (PLP),
a derivative of Pyridoxine (Vitamin B6).
The amino group is accommodated by
conversion of this coenzyme to
pyridoxamine-5'-phosphate (PMP). PLP is
covalently attached to the enzyme via a
Schiff Base linkage formed by the
condensation of its aldehyde group with
the ε-amino group of an enzymatic Lys
residue. The Schiff base, which is
conjugated to the enzymes pyridinium ring
is the focus of the coenzyme activity.
Ping Pong Bi Bi mechanism of PLP dependent
enzyme catalyzed transamination.
Aminotransferase reaction occurs in two stages
consisting of three steps: Transimination,
Tautomerisation and Hydolysis. In the first stage,
alpha amino group of the aminoacid is transferred
to PLP yielding an alpha ketoacid and PMP. In the
second stage of the reaction, in which the amino
group of PMP is transferred to a different alpha
Ketoacid to yield a new alpha amino acid and PLP.

The product of transamination reactions


depend on the availability of α-keto
acids. The products usually are either
alanine, aspartate or glutamate, since
their corresponding alpha-keto acids are
produced through metabolism of fuels.
Being a major degradative aminoacid
pathway, lysine, proline and threonine
are the only three amino acids that do
not always undergo transamination and
rather use respective dehydrogenase.
Alternative Mechanism
A second type of transamination
reaction can be described as a
nucleophilic substitution of one amine
or amide anion on an amine or
ammonium salt.[1] For example, the
attack of a primary amine by a primary
amide anion can be used to prepare
secondary amines:
RNH2 + R'NH− → RR'NH + NH2−
Symmetric secondary amines can be
prepared using Raney nickel (2RNH2 →
R2NH + NH3). And finally, quaternary
ammonium salts can be dealkylated
using ethanolamine:
R4N+ + NH2CH2CH2OH → R3N +
RN+H2CH2CH2OH
Aminonaphthalenes also undergo
transaminations.[2]

Types of aminotransferase
Transamination is mediated by several
different aminotransferase enzymes.
These may be specific for individual amino
acids, or they may be able to process a
group of chemically similar ones. The
latter applies to the group of the branched-
chain amino acids, which comprises
leucine, isoleucine, and valine. The two
common types of aminotransferases are
Alanine aminotransferase (ALT) and
Aspartate aminotransferase (AST).

References
1. Booth, Gerald (2000-01-01).
"Naphthalene Derivatives". Ullmann's
Encyclopedia of Industrial Chemistry.
Wiley-VCH Verlag GmbH & Co. KGaA.
doi:10.1002/14356007.a17_009 .
ISBN 9783527306732.

• Smith, M. B. and March, J. Advanced


Organic Chemistry: Reactions,
Mechanisms, and Structure, 5th ed. Wiley,
2001, p. 503. ISBN 0-471-58589-0 • Gerald
Booth "Naphthalene Derivatives" in
Ullmann's Encyclopedia of Industrial
Chemistry, 2005, Wiley-VCH, Weinheim.
doi:10.1002/14356007.a17_009

Voet & Voet. "Biochemistry" Fourth edition

External links
Amino Acid Biosynthesis
The chemical logic behind aminoacid
degradation and the urea cycle

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