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Literature summary extracted from

  • Karsten, W.E.; Ohshiro, T.; Izumi, Y.; Cook, P.F.
    Reaction of serine-glyoxylate aminotransferase with the alternative substrate ketomalonate indicates rate-limiting protonation of a quinonoid intermediate (2005), Biochemistry, 44, 15930-15936.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.45 expressed in Escherichia coli strain HB101 Hyphomicrobium methylovorum

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.45 Hyphomicrobium methylovorum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.45 Ni-NTA column chromatography Hyphomicrobium methylovorum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.45 L-serine + 2-oxomalonate
-
 Hyphomicrobium methylovorum 3-hydroxypyruvate + 2-aminomalonate
-
 ?
2.6.1.45 L-serine + glyoxylate
-
 Hyphomicrobium methylovorum 3-hydroxypyruvate + glycine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.6.1.45 serine-glyoxylate aminotransferase
-
 Hyphomicrobium methylovorum
2.6.1.45 SGAT
-
 Hyphomicrobium methylovorum

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.45 pyridoxal 5'-phosphate
-
 Hyphomicrobium methylovorum