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Literature summary for 2.3.1.30 extracted from

  • Kumar, S.; Raj, I.; Nagpal, I.; Subbarao, N.; Gourinath, S.
    Structural and biochemical studies of serine acetyltransferase reveal why the parasite Entamoeba histolytica cannot form a cysteine synthase complex (2011), J. Biol. Chem., 286, 12533-12541.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of serine acetyltransferase (SAT) isoform 1 at 1.77 A, in complex with its substrate serine at 1.59 A and inhibitor Cys at 1.78 A resolution is reported Entamoeba histolytica

Protein Variants

Protein Variants Comment Organism
additional information a mutant with a C terminus of EhSAT1 mutated to DWSI (4 amino acids changed) inhibits EhOASS efficiently Entamoeba histolytica

Inhibitors

Inhibitors Comment Organism Structure
cysteine competitive inhibitor of Ser Entamoeba histolytica

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Entamoeba histolytica Q9U8X2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + L-serine
-
Entamoeba histolytica CoA + O-acetyl-L-serine
-
?

Subunits

Subunits Comment Organism
trimer
-
Entamoeba histolytica

Synonyms

Synonyms Comment Organism
EhSAT1
-
Entamoeba histolytica
SAT isoform 1
-
Entamoeba histolytica
serine acetyltransferase
-
Entamoeba histolytica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Entamoeba histolytica