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Literature summary for 2.1.2.1 extracted from

  • Florio, R.; Chiaraluce, R.; Consalvi, V.; Paiardini, A.; Catacchio, B.; Bossa, F.; Contestabile, R.
    The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia coli serine hydroxymethyltransferase (2009), FEBS J., 276, 132-143.
    View publication on PubMed
Search for more literature for 2.1.2.1

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain GS1993 recA- Escherichia coli

Protein Variants

Protein Variants Comment Organism
L276A the mutant is in the monomeric state and shows reduced activity Escherichia coli
L85A the apo-L85A mutant enzyme is approximately 75% dimeric and shows reduced activity Escherichia coli
L85A/L276A the mutant is in the monomeric state and shows reduced activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00435
-
 tetrahydrofolate apparent value, mutant enzyme L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA Escherichia coli
0.00703
-
 tetrahydrofolate apparent value, wild type enzyme, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA Escherichia coli
0.00716
-
 tetrahydrofolate apparent value, mutant enzyme L85A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA Escherichia coli
0.0112
-
 tetrahydrofolate apparent value, mutant enzyme L85A/L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA Escherichia coli
0.14
-
 L-serine apparent value, wild type enzyme, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA Escherichia coli
0.15
-
 L-serine apparent value, mutant enzyme L85A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA Escherichia coli
0.2
-
 L-serine apparent value, mutant enzyme L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA Escherichia coli
0.2
-
 L-serine apparent value, mutant enzyme L85A/L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
91000
-
 wild type SHMT exists as a dimer in both apo- and holo-forms, ultracentrifugation Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A825
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine + tetrahydrofolate
-
 Escherichia coli glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?

Subunits

Subunits Comment Organism
dimer in the 0.0025-0.025 mM subunit concentration range, the wild type SHMT is a dimer, either in the presence or absence of cofactor. The apo-L85A mutant enzyme is approximately 75% dimeric Escherichia coli
monomer the apo-L276A and the apo-L85A mutants are in the monomeric state Escherichia coli

Synonyms

Synonyms Comment Organism
serine hydroxymethyltransferase
-
 Escherichia coli
SHMT
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.7
-
 L-serine mutant enzyme L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA Escherichia coli
6.7
-
 L-serine mutant enzyme L85A/L276A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA Escherichia coli
10.8
-
 L-serine mutant enzyme L85A, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA Escherichia coli
11.4
-
 L-serine wild type enzyme, at 20°C in 50 mM Na-HEPES (pH 7.2), containing 0.2 mM dithiothreitol and 0.1 mM EDTA Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Escherichia coli