Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.30 extracted from

  • Kai, Y.; Kashiwagi, T.; Ishikawa, K.; Ziyatdinov, M.K.; Redkina, E.I.; Kiriukhin, M.Y.; Gusyatiner, M.M.; Kobayashi, S.; Takagi, H.; Suzuki, E.
    Engineering of Escherichia coli L-serine O-acetyltransferase on the basis of crystal structure: desensitization to feedback inhibition by L-cysteine (2006), Protein Eng. Des. Sel., 19, 163-167.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of mutant enzymes in Escherichia coli Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of the enzyme with its inhibitor L-cysteine Escherichia coli

Protein Variants

Protein Variants Comment Organism
A94T activity is 160.2% of wild-type value, Ki for L-Cys is 5.7fold higher than wild-type value Escherichia coli
M256I Ki for L-Cys is 24fold higher than wild-type value Escherichia coli
R89H/T90V/P93A/A94T activity is 113.1% of wild-type value, Ki for L-Cys is 658fold higher than wild-type value Escherichia coli
R89P activity is 95.2% of wild-type value, Ki for L-Cys is 700fold higher than wild-type value Escherichia coli
R89S/T90L activity is 72.6% of wild-type value, Ki for L-Cys is 25fold higher than wild-type value Escherichia coli
R99T/T90R activity is 65.5% of wild-type value, Ki for L-Cys is 7.5fold higher than wild-type value Escherichia coli
V95G/D96G activity is 85.7% of wild-type value, Ki for L-Cys is 190fold higher than wild-type value Escherichia coli
V95L/D96P activity is 87.5% of wild-type value, Ki for L-Cys is 850fold higher than wild-type value Escherichia coli
V95R/D96P activity is 42.5% of wild-type value, Ki for L-Cys is 1583fold higher than wild-type value Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
L-Cys
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + L-serine Escherichia coli first step of L-cysteine synthesis CoA + O-acetyl-L-serine
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A9D4
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.715
-
25°C, pH 7.5, mutant enzyme V95R/D96P Escherichia coli
1.067
-
25°C, pH 7.5, mutant enzyme M256I Escherichia coli
1.1
-
25°C, pH 7.5, mutant enzyme R99T/T90R Escherichia coli
1.22
-
25°C, pH 7.5, mutant enzyme R89S/T90L Escherichia coli
1.44
-
25°C, pH 7.5, mutant enzyme V95G/D96G Escherichia coli
1.47
-
25°C, pH 7.5, mutant enzyme V95L/D96P Escherichia coli
1.6
-
25°C, pH 7.5, mutant enzyme R89P Escherichia coli
1.68
-
25°C, pH 7.5, wild-type enzyme Escherichia coli
1.9
-
25°C, pH 7.5, mutant enzyme R89H/T90V/P93A/A94T Escherichia coli
2.69
-
25°C, pH 7.5, mutant enzyme A94T Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + L-serine first step of L-cysteine synthesis Escherichia coli CoA + O-acetyl-L-serine
-
?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0006
-
L-Cys 25°C, pH 7.5, wild-type enzyme Escherichia coli
0.0034
-
L-Cys 25°C, pH 7.5, mutant enzyme A94T Escherichia coli
0.0045
-
L-Cys 25°C, pH 7.5, mutant enzyme R99T/T90R Escherichia coli
0.0145
-
L-Cys 25°C, pH 7.5, mutant enzyme M256I Escherichia coli
0.015
-
L-Cys 25°C, pH 7.5, mutant enzyme R89S/T90L Escherichia coli
0.114
-
L-Cys 25°C, pH 7.5, mutant enzyme V95G/D96G Escherichia coli
0.395
-
L-Cys 25°C, pH 7.5, mutant enzyme R89H/T90V/P93A/A94T Escherichia coli
0.42
-
L-Cys 25°C, pH 7.5, mutant enzyme R89P Escherichia coli
0.51
-
L-Cys 25°C, pH 7.5, mutant enzyme V95L/D96P Escherichia coli
0.95
-
L-Cys 25°C, pH 7.5, mutant enzyme V95R/D96P Escherichia coli