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Literature summary extracted from

  • Pinthong, C.; Maenpuen, S.; Amornwatcharapong, W.; Yuthavong, Y.; Leartsakulpanich, U.; Chaiyen, P.
    Distinct biochemical properties of human serine hydroxymethyltransferase compared with the Plasmodium enzyme: implications for selective inhibition (2014), FEBS J., 281, 2570-2583.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.1.2.1 drug development the human enzyme is a potential target for cancer treatment Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.2.1 recombinant soluble enzyme overexpression in Escherichia coli strain BL21(DE3) Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.2.1 tetrahydrofolate strong substrate inhibition Homo sapiens
2.1.2.1 Thiosemicarbazide
-
Homo sapiens
2.1.2.1 Thiosemicarbazide
-
Plasmodium falciparum
2.1.2.1 Thiosemicarbazide
-
Plasmodium vivax

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.2.1 additional information
-
additional information steady-state kinetics, overview Homo sapiens
2.1.2.1 0.0052
-
(6S)-tetrahydrofolate pH 7.0, 25°C, recombinant enzyme, with L-serine in HEPES buffer Homo sapiens
2.1.2.1 0.007
-
(6S)-tetrahydrofolate pH 7.0, 25°C, recombinant enzyme, with L-serine in phosphate buffer Homo sapiens
2.1.2.1 0.021
-
(6S)-tetrahydrofolate pH 7.0, 25°C, recombinant enzyme, with D-serine Homo sapiens
2.1.2.1 0.17
-
L-serine pH 7.0, 25°C, recombinant enzyme, in phosphate buffer Homo sapiens
2.1.2.1 0.18
-
L-serine pH 7.0, 25°C, recombinant enzyme, in HEPES buffer Homo sapiens
2.1.2.1 55
-
D-serine pH 7.0, 25°C, recombinant enzyme Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.1.2.1 cytosol cytosolic isoform Homo sapiens 5829
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.2.1 52020
-
4 * 52020, cytosolic isoform, sequence calculation, 4 * 53000, recombinant cytosolic isoform, SDS-PAGE Homo sapiens
2.1.2.1 53000
-
4 * 52020, cytosolic isoform, sequence calculation, 4 * 53000, recombinant cytosolic isoform, SDS-PAGE Homo sapiens
2.1.2.1 195000
-
cytosolic isoform, gel filtration Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.2.1 (6S)-tetrahydrofolate + D-serine Plasmodium falciparum
-
5,10-methylenetetrahydrofolate + glycine + H2O
-
r
2.1.2.1 (6S)-tetrahydrofolate + D-serine Plasmodium vivax
-
5,10-methylenetetrahydrofolate + glycine + H2O
-
r
2.1.2.1 (6S)-tetrahydrofolate + L-serine Plasmodium falciparum
-
5,10-methylenetetrahydrofolate + glycine + H2O
-
r
2.1.2.1 (6S)-tetrahydrofolate + L-serine Plasmodium vivax
-
5,10-methylenetetrahydrofolate + glycine + H2O
-
r
2.1.2.1 (6S)-tetrahydrofolate + L-serine Homo sapiens
-
5,10-methylenetetrahydrofolate + glycine + H2O
-
r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Plasmodium falciparum
-
tetrahydrofolate + L-serine
-
r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Plasmodium vivax
-
tetrahydrofolate + L-serine
-
r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Homo sapiens
-
tetrahydrofolate + L-serine
-
r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Plasmodium falciparum
-
tetrahydrofolate + D-serine
-
r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O Plasmodium vivax
-
tetrahydrofolate + D-serine
-
r
2.1.2.1 additional information Plasmodium falciparum Plasmodium SHMT can use D-serine and L-serine as a substrate ?
-
?
2.1.2.1 additional information Plasmodium vivax Plasmodium SHMT can use D-serine and L-serine as a substrate ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.1 Homo sapiens P34896
-
-
2.1.2.1 Plasmodium falciparum
-
-
-
2.1.2.1 Plasmodium vivax
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.2.1 recombinant enzyme 11.2fold from Escherichia coli strain BL21(DE3) to homogeneity by polyethyleneimine precipitation, anion exchange chromatography, and gel filtration Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.1 (6S)-tetrahydrofolate + D-serine
-
Plasmodium falciparum 5,10-methylenetetrahydrofolate + glycine + H2O
-
r
2.1.2.1 (6S)-tetrahydrofolate + D-serine
-
Plasmodium vivax 5,10-methylenetetrahydrofolate + glycine + H2O
-
r
2.1.2.1 (6S)-tetrahydrofolate + D-serine poor activity Homo sapiens 5,10-methylenetetrahydrofolate + glycine + H2O
-
r
2.1.2.1 (6S)-tetrahydrofolate + L-serine
-
Plasmodium falciparum 5,10-methylenetetrahydrofolate + glycine + H2O
-
r
2.1.2.1 (6S)-tetrahydrofolate + L-serine
-
Plasmodium vivax 5,10-methylenetetrahydrofolate + glycine + H2O
-
r
2.1.2.1 (6S)-tetrahydrofolate + L-serine
-
Homo sapiens 5,10-methylenetetrahydrofolate + glycine + H2O
-
r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
Plasmodium falciparum tetrahydrofolate + L-serine
-
r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
Plasmodium vivax tetrahydrofolate + L-serine
-
r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
Homo sapiens tetrahydrofolate + L-serine
-
r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
Plasmodium falciparum tetrahydrofolate + D-serine
-
r
2.1.2.1 5,10-methylenetetrahydrofolate + glycine + H2O
-
Plasmodium vivax tetrahydrofolate + D-serine
-
r
2.1.2.1 additional information Plasmodium SHMT can use D-serine and L-serine as a substrate Plasmodium falciparum ?
-
?
2.1.2.1 additional information Plasmodium SHMT can use D-serine and L-serine as a substrate Plasmodium vivax ?
-
?

Subunits

EC Number Subunits Comment Organism
2.1.2.1 homotetramer 4 * 52020, cytosolic isoform, sequence calculation, 4 * 53000, recombinant cytosolic isoform, SDS-PAGE Homo sapiens

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.2.1 25
-
assay at Plasmodium falciparum
2.1.2.1 25
-
assay at Plasmodium vivax
2.1.2.1 25
-
assay at Homo sapiens

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.1.2.1 additional information
-
unlike Plasmodium enzymes in which the activity is almost abolished at lower temperatures, the activity of hcSHMT still remains active below the temperature breakpoint Homo sapiens
2.1.2.1 additional information
-
unlike Plasmodium enzymes in which the activity is almost abolished at lower temperatures, the activity of human cytosolic SHMT still remains active below the temperature breakpoint Plasmodium falciparum
2.1.2.1 additional information
-
unlike Plasmodium enzymes in which the activity is almost abolished at lower temperatures, the activity of human cytosolic SHMT still remains active below the temperature breakpoint Plasmodium vivax
2.1.2.1 3 43 activity range Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.2.1 2 8 L-serine pH 7.0, 25°C, recombinant enzyme, in HEPES buffer Homo sapiens
2.1.2.1 15
-
L-serine pH 7.0, 25°C, recombinant enzyme, in phosphate buffer Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.2.1 7.8
-
recombinant enzyme Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.2.1 5,10-methylenetetrahydrofolate
-
Plasmodium falciparum
2.1.2.1 5,10-methylenetetrahydrofolate
-
Plasmodium vivax
2.1.2.1 5,10-methylenetetrahydrofolate
-
Homo sapiens
2.1.2.1 pyridoxal 5'-phosphate dependent on. The binding environment of PLP in human and Plasmodium enzymes is significantly different Plasmodium falciparum
2.1.2.1 pyridoxal 5'-phosphate dependent on. The binding environment of PLP in human and Plasmodium enzymes is significantly different Plasmodium vivax
2.1.2.1 pyridoxal 5'-phosphate dependent on. The binding environment of PLP in human and Plasmodium enzymes is significantly different Homo sapiens
2.1.2.1 tetrahydrofolate
-
Plasmodium falciparum
2.1.2.1 tetrahydrofolate
-
Plasmodium vivax
2.1.2.1 tetrahydrofolate
-
Homo sapiens

General Information

EC Number General Information Comment Organism
2.1.2.1 evolution the enzyme belongs to the alpha class of PLP-dependent enzymes. The ligand binding environment of enzymes SHMT from human and Plasmodium are different, overview Plasmodium falciparum
2.1.2.1 evolution the enzyme belongs to the alpha class of PLP-dependent enzymes. The ligand binding environment of enzymes SHMT from human and Plasmodium are different, overview Plasmodium vivax
2.1.2.1 evolution the enzyme belongs to the alpha class of PLP-dependent enzymes. The ligand binding environment of enzymes SHMT from human and Plasmodium are different, overview Homo sapiens
2.1.2.1 physiological function the enzyme is essential for parasite viability Plasmodium falciparum
2.1.2.1 physiological function the enzyme is essential for parasite viability Plasmodium vivax

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.1.2.1 0.172
-
D-serine pH 7.0, 25°C, recombinant enzyme Homo sapiens
2.1.2.1 88
-
L-serine pH 7.0, 25°C, recombinant enzyme, in phosphate buffer Homo sapiens
2.1.2.1 155.5
-
L-serine pH 7.0, 25°C, recombinant enzyme, in HEPES buffer Homo sapiens