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Literature summary extracted from

  • Hindson, V.J.; Shaw, W.V.
    Random-order ternary complex reaction mechanism of serine acetyltransferase from Escherichia coli (2003), Biochemistry, 42, 3113-3119.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.30 overexpression Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.30 CoA
-
 Escherichia coli
2.3.1.30 glycine competitive against L-serine, noncompetitive against acetyl-CoA Escherichia coli
2.3.1.30 L-alanine noncompetitive against acetyl-CoA Escherichia coli
2.3.1.30 additional information no inhibition by N-acetylserine Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.30 Escherichia coli
-
 CysE gene
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.30 recombinant from E. coli Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.30 acetyl-CoA + L-serine = CoA + O-acetyl-L-serine steady-state random-order mechanism Escherichia coli
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.30 additional information
-
 at acetyl-CoA concentration 15fold higher than L-serine concentration, a nonproductive ternary complex of enzyme-CoA-L-serine is formed, kinetics Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.30 acetyl-CoA + L-serine
-
 Escherichia coli CoA + O-acetyl-L-serine
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.3.1.30 SAT
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.30 0.068
-
 acetyl-CoA acetyl-CoA hydrolysis Escherichia coli