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Literature summary extracted from

  • Wu, D.; Li, Y.; Song, G.; Cheng, C.; Zhang, R.; Joachimiak, A.; Shaw, N.; Liu, Z.J.
    Structural basis for the inhibition of human 5,10-methenyltetrahydrofolate synthetase by N10-substituted folate analogues (2009), Cancer Res., 69, 7294-7301.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.3.2 cloning from brain cDNA library, expression of the His-tagged enzyme in Escherichia coli strain BL21 Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.3.2 purified recombinant wild-type MTHFS in a binary complex with ADP, with the N5-iminium phosphate reaction intermediate, or as an enzyme-product complex, hanging drop method at 16°C, 600 nl protein solution, with or without 5 mM 5-formyltetrahydrofolate and 5 mM ATP, are equilibrated against 0.05 ml of reservoir solution containing 100 mM HEPES, pH 6.6, 20 mM MgCl2, 20 mM NiCl2, and 20% w/v PEG 3350, 2 days, X-ray diffraction structure determination and analysis Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
6.3.3.2 D154A site-directed mutagenesis, the mutant shows 0.9% of the wild-type catalytic activity Homo sapiens
6.3.3.2 E61A site-directed mutagenesis, the mutant shows 8.6% of the wild-type catalytic activity Homo sapiens
6.3.3.2 F55A site-directed mutagenesis, the mutant shows 53.6% of the wild-type catalytic activity Homo sapiens
6.3.3.2 F85A site-directed mutagenesis, the mutant shows 72.3% of the wild-type catalytic activity Homo sapiens
6.3.3.2 K10A site-directed mutagenesis, the mutant shows 7.5% of the wild-type catalytic activity Homo sapiens
6.3.3.2 K150A site-directed mutagenesis, the mutant shows wild-type catalytic activity Homo sapiens
6.3.3.2 M58A site-directed mutagenesis, the mutant shows 121.6% of the wild-type catalytic activity Homo sapiens
6.3.3.2 M90A site-directed mutagenesis, the mutant shows 49.2% of the wild-type catalytic activity Homo sapiens
6.3.3.2 R145A site-directed mutagenesis, the mutant shows 2.3% of the wild-type catalytic activity Homo sapiens
6.3.3.2 R148A site-directed mutagenesis, the mutant shows 30.7% of the wild-type catalytic activity Homo sapiens
6.3.3.2 R14A site-directed mutagenesis, the mutant shows 12.9% of the wild-type catalytic activity Homo sapiens
6.3.3.2 W109A site-directed mutagenesis, the mutant shows 39.7% of the wild-type catalytic activity Homo sapiens
6.3.3.2 Y152A site-directed mutagenesis, the mutant shows 24.9% of the wild-type catalytic activity Homo sapiens
6.3.3.2 Y153A site-directed mutagenesis, the mutant shows 3.2% of the wild-type catalytic activity Homo sapiens
6.3.3.2 Y83A site-directed mutagenesis, the mutant shows wild-type catalytic activity Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.3.2 ATP + 5-formyltetrahydrofolate Homo sapiens
-
 ADP + phosphate + 5,10-methenyltetrahydrofolate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.3.2 Homo sapiens P49914
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.3.2 recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.3.3.2 MCF-7 cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.3.2 ATP + 5-formyltetrahydrofolate
-
 Homo sapiens ADP + phosphate + 5,10-methenyltetrahydrofolate
-
 ?
6.3.3.2 ATP + 5-formyltetrahydrofolate folate binds in a spherical pocket, substrate binding and active site structure, structure-function analysis, detailed overview Homo sapiens ADP + phosphate + 5,10-methenyltetrahydrofolate
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.3.2 additional information structure modelling, overview Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
6.3.3.2 5,10-Methenyltetrahydrofolate synthetase
-
 Homo sapiens
6.3.3.2 MTHFS
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.3.2 ATP
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
6.3.3.2 malfunction inhibition of MTHFS in human MCF-7 breast cancer cells arrests the growth of cells Homo sapiens
6.3.3.2 physiological function MTHFS regulates the flow of carbon through the one-carbon metabolic network, which supplies essential components for the growth and proliferation of cells Homo sapiens