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Literature summary for 2.3.1.46 extracted from

  • Coe, D.M.; Viola, R.E.
    Assessing the roles of essential functional groups in the mechanism of homoserine succinyltransferase (2007), Arch. Biochem. Biophys., 461, 211-218.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
metA, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Escherichia coli

Protein Variants

Protein Variants Comment Organism
C142A site-directed mutagenesis, the mutant is inactive Escherichia coli
C142S site-directed mutagenesis, the mutant is almost inactive Escherichia coli
E237A site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Escherichia coli
E237D site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli
E246A site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Escherichia coli
E246D site-directed mutagenesis, the mutant shows reduced catalytic efficiency with L-homoserine, but increased with succinyl-CoA compared to the wild-type enzyme Escherichia coli
H235N site-directed mutagenesis, the mutant is almost inactive Escherichia coli
K156L site-directed mutagenesis, the mutant is inactive Escherichia coli
K45A/K46A site-directed mutagenesis, the mutant is inactive Escherichia coli
K45L site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli
K46L site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Escherichia coli
R193A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli
R193A/E246A site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency with L-homoserine and reduced activity with succinyl-CoA compared to the wild-type enzyme Escherichia coli
R193K site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli
R249A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli
R249K site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli
Y238F site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli
Y238F/E246A site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency with L-homoserine, but increased with succinyl-CoA compared to the wild-type enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetics and thermodynamics of wild-type and mutant enzymes, overview Escherichia coli
0.043
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant E246D Escherichia coli
0.044
-
L-homoserine pH 7.5, 25°C, recombinant mutant K45L Escherichia coli
0.05
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant Y238F/E246A Escherichia coli
0.094
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant E246A Escherichia coli
0.15
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant E237A Escherichia coli
0.2
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant R193A/E246A Escherichia coli
0.23
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant R249A Escherichia coli
0.24
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant E237D Escherichia coli
0.28
-
succinyl-CoA pH 7.5, 25°C, recombinant wild-type enzyme Escherichia coli
0.31
-
L-homoserine pH 7.5, 25°C, recombinant mutant R193K Escherichia coli
0.31
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant R249K Escherichia coli
0.35
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant Y238F Escherichia coli
0.36
-
L-homoserine pH 7.5, 25°C, recombinant mutant E237D Escherichia coli
0.38
-
L-homoserine pH 7.5, 25°C, recombinant wild-type enzyme Escherichia coli
0.4
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant R193K Escherichia coli
0.43
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant R193A Escherichia coli
1.1
-
L-homoserine pH 7.5, 25°C, recombinant mutant E237A Escherichia coli
1.1
-
L-homoserine pH 7.5, 25°C, recombinant mutant R193A Escherichia coli
1.15
-
L-homoserine pH 7.5, 25°C, recombinant mutant R249A Escherichia coli
1.51
-
L-homoserine pH 7.5, 25°C, recombinant mutant R249K Escherichia coli
1.78
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant K46L Escherichia coli
2
-
L-homoserine pH 7.5, 25°C, recombinant mutant Y238F Escherichia coli
2.26
-
L-homoserine pH 7.5, 25°C, recombinant mutant K46L Escherichia coli
2.9
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant K45L Escherichia coli
9.1
-
L-homoserine pH 7.5, 25°C, recombinant mutant E246D Escherichia coli
59.1
-
L-homoserine pH 7.5, 25°C, recombinant mutant E246A Escherichia coli
93.8
-
L-homoserine pH 7.5, 25°C, recombinant mutant R193A/E246A Escherichia coli
95.5
-
L-homoserine pH 7.5, 25°C, recombinant mutant Y238F/E246A Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
succinyl-CoA + L-homoserine Escherichia coli
-
CoA + O-succinyl-L-homoserine
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by 2 different steps of anion exchange chromatography Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine ping pong catalytic reaction mechanism, roles of essential functional groups, the catalytic triad is formed by the nucleophile Cys142, the essential base His235, and Glu237, required for proper orientation of His235, Lys46 is required for interaction with succinyl-CoA, and Arg193 is involved in binding of L-Homoserine Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
recombinant wild-type and mutant enzymes Escherichia coli

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
homoserine succinyltransferase
-
Escherichia coli
HST
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.8
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant E237A Escherichia coli
1.2
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant R193A/E246A Escherichia coli
1.26
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant K46L Escherichia coli
2 3.7 succinyl-CoA pH 7.5, 25°C, recombinant mutant R249K Escherichia coli
3.3
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant R193A Escherichia coli
3.4
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant R193K Escherichia coli
6.7
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant E237D Escherichia coli
6.9
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant E246A Escherichia coli
8.9
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant Y238F/E246A Escherichia coli
10
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant R249A Escherichia coli
13
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant Y238F Escherichia coli
15
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant E246D Escherichia coli
25.7
-
succinyl-CoA pH 7.5, 25°C, recombinant wild-type enzyme Escherichia coli
40.1
-
succinyl-CoA pH 7.5, 25°C, recombinant mutant K45L Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Escherichia coli