Transaminase

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(Redirected from
Aminotransferase
)
Aminotransferase
E. coli with Pyridoxal 5' Phosphate cofactor
Identifiers
SymbolAminotransferase
PfamPF00155
InterProIPR004839
Membranome273
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Transaminases or aminotransferases are

catalyze a transamination reaction between an amino acid and an α-keto acid. They are important in the synthesis of amino acids
, which form proteins.

Function and mechanism

An amino acid contains an

amino (NH2) group. A keto acid contains a keto (=O) group. In transamination, the NH2 group on one molecule is exchanged with the =O group on the other molecule. The amino acid becomes a keto acid, and the keto acid becomes an amino acid.[citation needed
]

Transaminases require the coenzyme

alpha-ketoglutarate, giving alanine, aspartic acid, or glutamic acid, respectively. Many transamination reactions occur in tissues, catalysed by transaminases specific for a particular amino/keto acid pair. The reactions are readily reversible, the direction being determined by which of the reactants are in excess. This reversibility can be exploited for synthetic chemistry applications to achieve the synthesis of valuable chiral amines. The specific enzymes are named from one of the reactant pairs, for example; the reaction between glutamic acid and pyruvic acid to make alpha ketoglutaric acid and alanine is called alanine transaminase and was originally called glutamic-pyruvic transaminase or GPT for short.[1]

Tissue transaminase activities can be investigated by incubating a

alpha-keto acid
. The amino (NH2) group and the keto (=O) group are exchanged.

Amino acid metabolism in animals

Animals must metabolize

anaerobic metabolism by muscles.[citation needed
]

Diagnostic uses

The transaminase enzymes are important in the production of various amino acids, and measuring the concentrations of various transaminases in the blood is important in the diagnosing and tracking many diseases.[citation needed] For example, the presence of elevated transaminases can be an indicator of liver and cardiac damage. Two important transaminase enzymes are aspartate transaminase (AST), also known as serum glutamic oxaloacetic transaminase (SGOT); and alanine transaminase (ALT), also called alanine aminotransferase (ALAT) or serum glutamate-pyruvate transaminase (SGPT). These transaminases were discovered in 1954[1][3][4] and their clinical importance was described in 1955.[5][6][7][8]

See also

  • GABA transaminase
    inhibitor

References

  1. ^
    PMID 13221663
    .
  2. ISSN 1476-4687
    .
  3. PMID 13221664
    .
  4. PMID 13195683
    .
  5. ^ "Biblioteca Nazionale di Napoli. News: Serata in onore di Mario Coltorti e Giuseppe Giusti". vecchiosito.bnnonline.it. Retrieved 2017-09-10.
  6. ^ "E' morto il prof. Coltorti: scoprì le transaminasi". notizie-segreteria-liver-pool.blogspot.it. Retrieved 2017-09-10.
  7. ^ "Campania su Coltorti". www.istitutobioetica.org. Retrieved 2017-09-10.
  8. ^ MonrifNet (3 January 2009). "Il Resto Del Carlino - Macerata - E' morto Mario Coltorti: scoprì la transaminasi". www.ilrestodelcarlino.it (in Italian). Retrieved 2017-09-10.

Further reading

  • Ghany M, Hoofnagle JH (2005). "Approach to the Patient With Liver Disease". In Kasper DL, Fauci AS, Longo DL, Braunwald E, Hauser SL, Jameson JL (eds.). Harrison's Principles of Internal Medicine (16th ed.). New York: McGraw-Hill. pp. 1814–5.
  • Nelson DL, Cox MM (2000). Lehninger Principles of Biochemistry (3rd ed.). New York: Worth Publishers. pp. 628–31, 634, 828–30.

External links

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