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Literature summary for 2.1.2.1 extracted from

  • Fu, T.F.; Boja, E.S.; Safo, M.K.; Schirch, V.
    Role of proline residues in the folding of serine hydroxymethyltransferase (2003), J. Biol. Chem., 278, 31088-31094.
    View publication on PubMed
Search for more literature for 2.1.2.1

Protein Variants

Protein Variants Comment Organism
P214A the turnover-number is 1.5fold lower than the wild-type value, the Km-value for Ser is 2.1fold lower than the wild-type value, The Km-value for tetrahydropteroylglutamate is 1.3fold higher than the wild-type value, Tm-value in absence of Ser is 3.5°C lower than the wild-type Tm-value. The Tm-value in presence of Ser is 4°C higher than the wild-type value Escherichia coli
P214G the turnover-number is 1.5fold lower than the wild-type value, the Km-value for Ser is 1.3fold lower than the wild-type value, The Km-value for tetrahydropteroylglutamate is 1.3fold higher than the wild-type value Escherichia coli
P216A the turnover-number is 1.5fold lower than the wild-type value, the Km-value for Ser is 1.2fold lower than the wild-type value. The Km-value for tetrahydropteroylglutamate is 1.3fold higher than the wild-type value, Tm-value in absence of Ser is 3.5°C higher than the wild-type Tm-value, The Tm-value in presence of Ser is 0.5°C higher than the wild-type value Escherichia coli
P216G the turnover-number is 8.3fold lower than the wild-type value, the Km-value for Ser is 1.9fold higher than the wild-type value. The Km-value for tetrahydropteroylglutamate is 5.7fold higher than the wild-type value Escherichia coli
P218A the turnover-number is 1.1fold lower than the wild-type value, the Km-value for Ser is 2.3fold lower than the wild-type value. The Km-value for tetrahydropteroylglutamate is 1.3fold higher than the wild-type value, double thermal transition that is considerably lower than wild-type enzyme, no increase in thermal stability upon binding serine Escherichia coli
P218G the turnover-number is 1.5fold lower than the wild-type value, the Km-value for Ser is 2.3fold lower than the wild-type value. The Km-value for tetrahydropteroylglutamate is 1.1fold higher than the wild-type value Escherichia coli
P258A the turnover-number is below 0.5 per min, the KM-value for Ser is 26.7fold higher than the wild-type value Escherichia coli
P258G inactive mutant enzyme Escherichia coli
P264A the turnover-number is 3fold lower than the wild-type value, the Km-value for Ser is 1.1fold higher than the wild-type value, The Km-value for tetrahydropteroylglutamate is 1.1fold higher than the wild-type value, Tm-value in absence of Ser is 9°C lower than the wild-type Tm-value. The Tm-value in presence of Ser is 11.5°C lower than the wild-type value Escherichia coli
P264G the turnover-number is 42.9fold lower than the wild-type value, the Km-value for Ser is 4.4fold higher than the wild-type value Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.015
-
 tetrahydrofolate wild-type enzyme Escherichia coli
0.017
-
 tetrahydrofolate mutant enzyme P218G Escherichia coli
0.017
-
 tetrahydrofolate mutant enzyme P264A Escherichia coli
0.019
-
 tetrahydrofolate mutant enzyme P218A Escherichia coli
0.02
-
 tetrahydrofolate mutant enzyme P214A Escherichia coli
0.02
-
 tetrahydrofolate mutant enzyme P214G Escherichia coli
0.02
-
 tetrahydrofolate mutant enzyme P216A Escherichia coli
0.085
-
 tetrahydrofolate mutant enzyme P216G Escherichia coli
0.13
-
 L-Ser mutant enzyme P218A Escherichia coli
0.13
-
 L-Ser mutant enzyme P218G Escherichia coli
0.14
-
 L-Ser mutant enzyme P214A Escherichia coli
0.24
-
 L-Ser mutant enzyme P214G Escherichia coli
0.25
-
 L-Ser mutant enzyme P216A Escherichia coli
0.3
-
 L-Ser wild-type enzyme Escherichia coli
0.33
-
 L-Ser mutant enzyme P264A Escherichia coli
0.58
-
 L-Ser mutant enzyme P216G Escherichia coli
1.33
-
 L-Ser mutant enzyme P264G Escherichia coli
8
-
 L-Ser mutant enzyme P258A Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
tetrahydrofolate + L-Ser
-
 Escherichia coli ? + glycine + H2O
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 thermal denaturation is irreversible Escherichia coli
67
-
 Tm-value for wild-type enzyme in absence of Ser Escherichia coli
73
-
 Tm-value for wild-type enzyme in presence of Ser Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.12
-
 tetrahydrofolate mutant enzyme P264G Escherichia coli
0.12
-
 L-Ser mutant enzyme P264G Escherichia coli
0.6
-
 tetrahydrofolate mutant enzyme P216G Escherichia coli
0.6
-
 L-Ser mutant enzyme P216G Escherichia coli
1.6
-
 tetrahydrofolate mutant enzyme P264A Escherichia coli
1.6
-
 L-Ser mutant enzyme P264A Escherichia coli
3.3
-
 tetrahydrofolate mutant enzyme P214A Escherichia coli
3.3
-
 L-Ser mutant enzyme P214A Escherichia coli
3.3
-
 tetrahydrofolate mutant enzyme P214G Escherichia coli
3.3
-
 L-Ser mutant enzyme P214G Escherichia coli
3.3
-
 tetrahydrofolate mutant enzyme P216A Escherichia coli
3.3
-
 L-Ser mutant enzyme P216A Escherichia coli
3.3
-
 tetrahydrofolate mutant enzyme P218G Escherichia coli
3.3
-
 L-Ser mutant enzyme P218G Escherichia coli
4.5
-
 tetrahydrofolate mutant enzyme P218A Escherichia coli
4.5
-
 L-Ser mutant enzyme P218A Escherichia coli
5
-
 tetrahydrofolate wild-type enzyme Escherichia coli
5
-
 L-Ser wild-type enzyme Escherichia coli