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Literature summary for 2.3.1.30 extracted from

  • Wigley, D.B.; Derrick, J.P.; Shaw, W.V.
    The serine acetyltransferase from Escherichia coli. Over-expression, purification and preliminary crystallographic analysis (1990), FEBS Lett., 277, 267-271.
    View publication on PubMed
Search for more literature for 2.3.1.30

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli, construction of an expression vector which increases the expression to 17% of the soluble cell protein Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapour diffusion method, 8-16% polyethylene glycol 1000, 10 mM Tris-HCl, pH 7.5, 2-4 weeks, room temperature, structure analysis Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
L-cysteine
-
 Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29261
-
 4 * 29261, ultracentrifugation, gel filtration, crystallographic data Escherichia coli
125000
-
 ultracentrifugation experiments Escherichia coli
160000
-
 gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 B
-
Escherichia coli B / ATCC 11303
-
 B
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
71.6
-
-
 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
-
 ?
acetyl-CoA + L-serine
-
 Escherichia coli B / ATCC 11303 CoA + O-acetyl-L-serine
-
 ?

Subunits

Subunits Comment Organism
tetramer 4 * 29261, ultracentrifugation, gel filtration, crystallographic data Escherichia coli