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Literature summary 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

Protein Variants

EC Number Protein Variants Comment Organism
2.1.2.1 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
2.1.2.1 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
2.1.2.1 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
2.1.2.1 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
2.1.2.1 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
2.1.2.1 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
2.1.2.1 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
2.1.2.1 P258G inactive mutant enzyme Escherichia coli
2.1.2.1 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
2.1.2.1 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.2.1 0.015
-
 tetrahydrofolate wild-type enzyme Escherichia coli
2.1.2.1 0.017
-
 tetrahydrofolate mutant enzyme P218G Escherichia coli
2.1.2.1 0.017
-
 tetrahydrofolate mutant enzyme P264A Escherichia coli
2.1.2.1 0.019
-
 tetrahydrofolate mutant enzyme P218A Escherichia coli
2.1.2.1 0.02
-
 tetrahydrofolate mutant enzyme P214A Escherichia coli
2.1.2.1 0.02
-
 tetrahydrofolate mutant enzyme P214G Escherichia coli
2.1.2.1 0.02
-
 tetrahydrofolate mutant enzyme P216A Escherichia coli
2.1.2.1 0.085
-
 tetrahydrofolate mutant enzyme P216G Escherichia coli
2.1.2.1 0.13
-
 L-Ser mutant enzyme P218A Escherichia coli
2.1.2.1 0.13
-
 L-Ser mutant enzyme P218G Escherichia coli
2.1.2.1 0.14
-
 L-Ser mutant enzyme P214A Escherichia coli
2.1.2.1 0.24
-
 L-Ser mutant enzyme P214G Escherichia coli
2.1.2.1 0.25
-
 L-Ser mutant enzyme P216A Escherichia coli
2.1.2.1 0.3
-
 L-Ser wild-type enzyme Escherichia coli
2.1.2.1 0.33
-
 L-Ser mutant enzyme P264A Escherichia coli
2.1.2.1 0.58
-
 L-Ser mutant enzyme P216G Escherichia coli
2.1.2.1 1.33
-
 L-Ser mutant enzyme P264G Escherichia coli
2.1.2.1 8
-
 L-Ser mutant enzyme P258A Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.1 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.2.1
-
 Escherichia coli

Substrates and Products (Substrate)

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.2.1 additional information
-
 thermal denaturation is irreversible Escherichia coli
2.1.2.1 67
-
 Tm-value for wild-type enzyme in absence of Ser Escherichia coli
2.1.2.1 73
-
 Tm-value for wild-type enzyme in presence of Ser Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.2.1 0.12
-
 tetrahydrofolate mutant enzyme P264G Escherichia coli
2.1.2.1 0.12
-
 L-Ser mutant enzyme P264G Escherichia coli
2.1.2.1 0.6
-
 tetrahydrofolate mutant enzyme P216G Escherichia coli
2.1.2.1 0.6
-
 L-Ser mutant enzyme P216G Escherichia coli
2.1.2.1 1.6
-
 tetrahydrofolate mutant enzyme P264A Escherichia coli
2.1.2.1 1.6
-
 L-Ser mutant enzyme P264A Escherichia coli
2.1.2.1 3.3
-
 tetrahydrofolate mutant enzyme P214A Escherichia coli
2.1.2.1 3.3
-
 L-Ser mutant enzyme P214A Escherichia coli
2.1.2.1 3.3
-
 tetrahydrofolate mutant enzyme P214G Escherichia coli
2.1.2.1 3.3
-
 L-Ser mutant enzyme P214G Escherichia coli
2.1.2.1 3.3
-
 tetrahydrofolate mutant enzyme P216A Escherichia coli
2.1.2.1 3.3
-
 L-Ser mutant enzyme P216A Escherichia coli
2.1.2.1 3.3
-
 tetrahydrofolate mutant enzyme P218G Escherichia coli
2.1.2.1 3.3
-
 L-Ser mutant enzyme P218G Escherichia coli
2.1.2.1 4.5
-
 tetrahydrofolate mutant enzyme P218A Escherichia coli
2.1.2.1 4.5
-
 L-Ser mutant enzyme P218A Escherichia coli
2.1.2.1 5
-
 tetrahydrofolate wild-type enzyme Escherichia coli
2.1.2.1 5
-
 L-Ser wild-type enzyme Escherichia coli