IntEnz

EC 2.6.1.44 - Alanine—glyoxylate transaminase

IntEnz Enzyme Nomenclature
EC 2.6.1.44

Names

Reaction

• 24248 [IUBMB]
  glyoxylate

  glyoxylate

  Name origin: UniProt - CHECKED (C)

  CHEBI:36655

  Formula: C2HO3
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  L-alanine

  L-alanine

  Name origin: UniProt - CHECKED (C)

  CHEBI:57972

  Formula: C3H7NO2
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  =

  glycine

  glycine

  Name origin: UniProt - CHECKED (C)

  CHEBI:57305

  Formula: C2H5NO2
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  +

  pyruvate

  pyruvate

  Name origin: UniProt - CHECKED (C)

  CHEBI:15361

  Formula: C3H3O3
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

Cofactor

• pyridoxal 5'-phosphate

Comments:

A pyridoxal-phosphate protein. With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate. A second component also catalyses the reaction of EC 2.6.1.51 serine-pyruvate transaminase.

Links to other databases

References

1. Noguchi, T., Okuno, E., Takada, Y., Minatogawa, Y., Okai, K. and Kido, R.
   Characteristics of hepatic alanine-glyoxylate aminotransferase in different mammalian species.
   Biochem. J. 169 : 113-122 (1978). [PMID: 629740]
2. Okuno, E., Minatogawa, Y. and Kido, R.
   Co-purification of alanine-glyoxylate aminotransferase with 2-aminobutyrate aminotransferase in rat kidney.
   Biochim. Biophys. Acta 715 : 97-104 (1982). [PMID: 6803844]
3. Thompson, J.S. and Richardson, K.E.
   Isolation and characterization of an L-alanine: glyoxylate aminotransferase from human liver. J.
   Biol. Chem. 242 : 3614-3619 (1967). [PMID: 6038488]

[EC 2.6.1.44 created 1972, modified 1982]