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Literature summary for 2.3.1.30 extracted from

  • Pye, V.E.; Tingey, A.P.; Robson, R.L.; Moody, P.C.
    The structure and mechanism of serine acetyltransferase from Escherichia coli (2004), J. Biol. Chem., 279, 40729-40736.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
recombinant enzyme, crystals grew from 0.1 M MES, pH 6.6, 1ß% 2-methyl-2,3-pentanediol, 0.5 M sodium thiocyanate, 5.5 mM cysteine, and SeMet SAT (10 mg/ml) sitting drops, at 20°C within 7 days. 2.2 A crystal structure of the enzyme, which is s dimer of trimers in complex with cysteine Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
cysteine competitive, binds at the serine substrate site, negatively regulates its own synthesis Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9D4
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Escherichia coli

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
SAT
-
Escherichia coli