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Literature summary for 2.6.1.45 extracted from

  • Karsten, W.E.; Ohshiro, T.; Izumi, Y.; Cook, P.F.
    Initial velocity, spectral, and pH studies of the serine-glyoxylate aminotransferase from Hyphomicrobiuim methylovorum (2001), Arch. Biochem. Biophys., 388, 267-275.
    View publication on PubMed
Search for more literature for 2.6.1.45

Inhibitors

Inhibitors Comment Organism Structure
beta-chloroalanine competitive vs. L-alanine, uncompetitive vs. 2-oxomalonate Hyphomicrobium methylovorum
oxalate competitive vs. 2-oxomalonate, uncompetitive vs. L-serine Hyphomicrobium methylovorum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.28
-
 L-serine pH 8.0 Hyphomicrobium methylovorum
1.13
-
 2-Oxomalonate pH 8.0 Hyphomicrobium methylovorum

Organism

Organism UniProt Comment Textmining
Hyphomicrobium methylovorum
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-serine + glyoxylate = 3-hydroxypyruvate + glycine ping-pong reaction mechanism Hyphomicrobium methylovorum
a

Substrates and Products (Substrate)

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

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0036
-
 beta-chloroalanine pH 8.0 Hyphomicrobium methylovorum
0.27
-
 oxalate pH 8.0 Hyphomicrobium methylovorum