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

BRENDA support

Literature summary extracted from

  • Sopitthummakhun, K.; Maenpuen, S.; Yuthavong, Y.; Leartsakulpanich, U.; Chaiyen, P.
    Serine hydroxymethyltransferase from Plasmodium vivax is different in substrate specificity from its homologues (2009), FEBS J., 276, 4023-4036.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.2.1 expressed in Escherichia coli BL21(DE3) cells Plasmodium vivax

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.2.1 0.14
-
 tetrahydrofolate in 50 mM HEPES buffer (pH 7.0), at 25°C Plasmodium vivax
2.1.2.1 0.18
-
 L-serine in 50 mM HEPES buffer (pH 7.0), at 25°C Plasmodium vivax
2.1.2.1 47
-
 D-serine apparent value, in 50 mM HEPES buffer (pH 7.0), at 25°C Plasmodium vivax

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.2.1 49000
-
 2 * 49000, SDS-PAGE Plasmodium vivax
2.1.2.1 72400
-
 gel filtration Plasmodium vivax

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.1 Plasmodium vivax
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.2.1 DEAE-Sepharose column chromatography, SP-Sepharose column chromatography, and Sephadex G-25 gel filtration Plasmodium vivax

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.2.1 0.16
-
 crude extract, in 50 mM HEPES (pH 7.0), 1 mM dithiothreitol and 0.5 mM EDTA at 25°C Plasmodium vivax
2.1.2.1 1.86
-
 after 3.8fold purification, in 50 mM HEPES (pH 7.0), 1 mM dithiothreitol and 0.5 mM EDTA at 25°C Plasmodium vivax

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.1 D-serine + tetrahydrofolate the binding affinity for D-serine is 150fold lower than that of L-serine Plasmodium vivax glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?
2.1.2.1 L-serine + tetrahydrofolate L-serine is the physiological substrate Plasmodium vivax glycine + 5,10-methylenetetrahydrofolate + H2O
-
 ?
2.1.2.1 additional information SHMT also catalyzes the tetrahydrofolate-independent retro-aldol cleavage of 3-hydroxy amino acids Plasmodium vivax ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.2.1 homodimer 2 * 49000, SDS-PAGE Plasmodium vivax

Synonyms

EC Number Synonyms Comment Organism
2.1.2.1 serine hydroxymethyltransferase
-
 Plasmodium vivax
2.1.2.1 SHMT
-
 Plasmodium vivax

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.1.2.1 5 30 the catalytic activity increases upon temperature increment Plasmodium vivax

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.2.1 0.26
-
 D-serine in 50 mM HEPES buffer (pH 7.0), at 25°C Plasmodium vivax
2.1.2.1 0.98
-
 L-serine in 50 mM HEPES buffer (pH 7.0), at 25°C Plasmodium vivax
2.1.2.1 0.98
-
 tetrahydrofolate in 50 mM HEPES buffer (pH 7.0), at 25°C Plasmodium vivax

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.2.1 8
-
 in 50 mM HEPES Plasmodium vivax

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.1.2.1 6.5 10
-
 Plasmodium vivax

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.1 pyridoxal 5'-phosphate the Kd for binding of the enzyme and pyridoxal 5'-phosphate is 0.00014 mM Plasmodium vivax