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Literature summary for 2.6.1.52 extracted from

  • Singh, R.K.; Mazumder, M.; Sharma, B.; Gourinath, S.
    Structural investigation and inhibitory response of halide on phosphoserine aminotransferase from Trichomonas vaginalis (2016), Biochim. Biophys. Acta, 1860, 1508-1518.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
to 2.15 A resolution. The active site is in a closed conformation, and pyridoxal 5'-phosphate forms an internal aldimine linkage to Lys 202. Residue Val 340 near the active site might be responsible in closing the active site Trichomonas vaginalis

Inhibitors

Inhibitors Comment Organism Structure
Iodide
-
Trichomonas vaginalis
additional information not inhibitory: chloride, fluoride and bromide up to 200 mM Trichomonas vaginalis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0544
-
O-phospho-L-serine pH 8.5, 22°C Trichomonas vaginalis
0.2028
-
2-oxoglutarate pH 8.5, 22°C Trichomonas vaginalis

Organism

Organism UniProt Comment Textmining
Trichomonas vaginalis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O-phospho-L-serine + 2-oxoglutarate
-
Trichomonas vaginalis 3-phosphonooxypyruvate + L-glutamate
-
r

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
200
-
pH 8.5, 22°C Trichomonas vaginalis Iodide