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Literature summary extracted from

  • Pai, V.R.; Rajaram, V.; Bisht, S.; Bhavani, B.S.; Rao, N.A.; Murthy, M.R.; Savithri, H.S.
    Structural and functional studies of Bacillus stearothermophilus serine hydroxymethyltransferase: the role of Asn(341), Tyr(60) and Phe(351) in tetrahydrofolate binding (2009), Biochem. J., 418, 635-642.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.2.1 expressed in Escherichia coli BL21(DE3) cells Geobacillus stearothermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.2.1 mutant proteins are crystallized by the hanging drop vapor diffusion method, using 50% 2-methyl 2,4-pentanediol as the precipitant with 0.2 mM EDTA, 5 mM beta-mercaptoethanol in 100 mM HEPES (pH 7.5) Geobacillus stearothermophilus

Protein Variants

EC Number Protein Variants Comment Organism
2.1.2.1 F351G the mutation has no effect on tetrahydrofolate-independent and tetrahydrofolate-dependent activities Geobacillus stearothermophilus
2.1.2.1 N341A the mutant is inactive for the tetrahydrofolate-dependent activity, while the mutation has no effect on tetrahydrofolate-independent activity Geobacillus stearothermophilus
2.1.2.1 Y60A the mutant is inactive for the tetrahydrofolate-dependent activity, while the mutation has no effect on tetrahydrofolate-independent activity Geobacillus stearothermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.2.1 0.9
-
 L-serine wild type enzyme, at 37°C Geobacillus stearothermophilus
2.1.2.1 1
-
 L-serine mutant enzyme F315G, at 37°C Geobacillus stearothermophilus

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.1 Geobacillus stearothermophilus Q7SIB6
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.2.1 ammonium sulfate precipitation, DEAE-cellulose column chromatography, gel filtration Geobacillus stearothermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.1 L-serine + tetrahydrofolate
-
 Geobacillus stearothermophilus glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?
2.1.2.1 additional information SHMT also catalyses several tetrahydrofolate-independent side reactions such as cleavage of beta-hydroxy amino acids, transamination, racemization and decarboxylation Geobacillus stearothermophilus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.2.1 dimer x-ray crystallography Geobacillus stearothermophilus

Synonyms

EC Number Synonyms Comment Organism
2.1.2.1 serine hydroxymethyltransferase
-
 Geobacillus stearothermophilus
2.1.2.1 SHMT
-
 Geobacillus stearothermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.1.2.1 65
-
 the melting temperature of the wild type enzyme is at 65°C Geobacillus stearothermophilus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.2.1 3.9
-
 L-serine wild type enzyme, at 37°C Geobacillus stearothermophilus
2.1.2.1 3.9
-
 L-serine mutant enzyme F315G, at 37°C Geobacillus stearothermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.1 pyridoxal 5'-phosphate dependent on Geobacillus stearothermophilus