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Literature summary extracted from

  • Stolz, M.; Doernemann, D.
    Kinetic characteristics, substrate specificity and catalytic properties of phosphoserine aminotransferase from the green alga Scenedesmus obliquus, mutant C-2A' (1995), Z. Naturforsch. C, 50c, 630-637.
No PubMed abstract available

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.52 0.083
-
 L-phosphoserine pH 8.0, 35°C Tetradesmus obliquus
2.6.1.52 0.18
-
 2-oxoglutarate pH 8.0, 35°C Tetradesmus obliquus
2.6.1.52 0.233
-
 2-oxoglutarate pH 8.0, 35°C Tetradesmus obliquus
2.6.1.52 0.84
-
 4,5-Dioxopentanoate pH 8.0, 35°C Tetradesmus obliquus

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.52 Tetradesmus obliquus
-
 mutant C-2 A'
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.6.1.52
-
 Tetradesmus obliquus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.52 L-glutamate + 4,5-dioxopentanoate
-
 Tetradesmus obliquus 5-aminolevulinate + 2-oxoglutarate
-
 ?
2.6.1.52 additional information 4,5-dioxovalerate with glutamate as amino donor is effective as competitive substrate to phosphohydroxypyruvate in the forward reaction and yields 5-aminolevulinate, 4,5-dioxovalerate and glutamate-1-semialdehyde can both serve as competitive aminoacceptor in the reverse reaction with phosphoserine and as substrate with 2-oxoglutarate as aminoacceptor Tetradesmus obliquus ?
-
 ?
2.6.1.52 O-phospho-L-serine + 2-oxoglutarate
-
 Tetradesmus obliquus 3-phosphonooxypyruvate + L-glutamate
-
 r

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.6.1.52 6.8 8.2
-
 Tetradesmus obliquus
2.6.1.52 7
-
 phosphoserine with 2-oxoglutarate as amino acceptor Tetradesmus obliquus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.6.1.52 5 9.5
-
 Tetradesmus obliquus