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Literature summary for 2.6.1.52 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
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KM Value [mM]

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

Organism

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

Purification (Commentary)

Purification (Comment) Organism
-
 Tetradesmus obliquus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate + 4,5-dioxopentanoate
-
 Tetradesmus obliquus 5-aminolevulinate + 2-oxoglutarate
-
 ?
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 ?
-
 ?
O-phospho-L-serine + 2-oxoglutarate
-
 Tetradesmus obliquus 3-phosphonooxypyruvate + L-glutamate
-
 r

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
5 9.5
-
 Tetradesmus obliquus