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Literature summary for 2.3.1.30 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
Search for more literature for 2.3.1.30

Cloned(Commentary)

Cloned (Comment) Organism
overexpression Escherichia coli

Inhibitors

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 CysE gene
-

Purification (Commentary)

Purification (Comment) Organism
recombinant from E. coli Escherichia coli

Reaction

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
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)

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

Synonyms

Synonyms Comment Organism
SAT
-
 Escherichia coli

Turnover Number [1/s]

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