Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.2.1 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)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

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

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus Q7SIB6
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits Comment Organism
dimer x-ray crystallography Geobacillus stearothermophilus

Synonyms

Synonyms Comment Organism
serine hydroxymethyltransferase
-
Geobacillus stearothermophilus
SHMT
-
Geobacillus stearothermophilus

Temperature Stability [°C]

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

Turnover Number [1/s]

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

Cofactor

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