6.3.4.3: formate-tetrahydrofolate ligase
This is an abbreviated version!
For detailed information about formate-tetrahydrofolate ligase, go to the full flat file.
Word Map on EC 6.3.4.3
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6.3.4.3
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trifunctional
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one-carbon
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5,10-methylenetetrahydrofolate
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acetogens
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mthfr
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5,10-methenyltetrahydrofolate
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homoacetogens
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folate-dependent
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acetogenesis
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cylindrosporum
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thermoaceticum
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folate-mediated
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1.5.1.5
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dehydrogenase-cyclohydrolase
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5,10-methenyl-thf
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5,10-methylene-thf
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biogas
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acetobacterium
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acidi-urici
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syntrophic
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pharmacology
- 6.3.4.3
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trifunctional
-
one-carbon
- 5,10-methylenetetrahydrofolate
-
acetogens
- mthfr
- 5,10-methenyltetrahydrofolate
-
homoacetogens
-
folate-dependent
-
acetogenesis
- cylindrosporum
- thermoaceticum
-
folate-mediated
-
1.5.1.5
-
dehydrogenase-cyclohydrolase
-
5,10-methenyl-thf
-
5,10-methylene-thf
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biogas
- acetobacterium
- acidi-urici
-
syntrophic
- pharmacology
Reaction
Synonyms
10-CHO-THF synthase, 10-formyl-THF synthetase, 10-Formyltetrahydrofolate synthetase, 10-formylTHF synthetase, ADE3, C(1)-tetrahydrofolate synthase, C1 synthase, C1-tetrahydrofolate synthase, C1-tetrahydrofolate synthetase, C1-THF synthase, C1-THFS, CpeFhs, DCS, dehydrogenasse-cyclohydrolase-synthetase, FHS, formate-tetrahydrofolate ligase, formate:tetrahydrofolate ligase (ADP-forming), formyl tetrahydrofolate synthetase, Formyl-THF synthetase, Formyltetrahydrofolate synthetase, ftfL, FTHFS, FTL, methylenetetrahydrofolate dehydrogenase 1-like, methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase, methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase enzyme, MIS1, MTHFD, MTHFD1, MTHFD1L, MTHFDIL, N10-formyltetrahydrofolate synthetase, NAD-dependent methylenetetrahydrofolate dehydrogenase, Synthetase, formyl tetrahydrofolate, Tetrahydrofolate formylase, Tetrahydrofolic formylase, THF synthase, THFS
ECTree
6.3.4.3 formate-tetrahydrofolate ligaseAdvanced search results
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Engineering on EC 6.3.4.3 - formate-tetrahydrofolate ligase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H125S
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site-directed mutant enzymes H125S, H131S, and H268S do not fold properly and/or do not associate to the active tetramer and, as a consequence are susceptible to intracellular proteolytic digestion
H131S
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site-directed mutant enzymes H125S, H131S, and H268S do not fold properly and/or do not associate to the active tetramer and, as a consequence are susceptible to intracellular proteolytic digestion
H268S
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site-directed mutant enzymes H125S, H131S, and H268S do not fold properly and/or do not associate to the active tetramer and, as a consequence are susceptible to intracellular proteolytic digestion
R653Q
E98Q
93% of wild-type activity, slight increase in thermal stability in the absence of monovalent cation
additional information
R653Q
amino position 653 is located within the 10-formyltetrahydrofolate synthetase domain of the MTHFD1 protein affecting the supply of 10-formyltetrahydrofolate required for purine synthesis
R653Q
mutant enzyme has normal substrate affinity but a 36% reduction in half-life at 42°C, the mutation reduces the metabolic activity of MTHFD1 within cells: formate incorporation into DNA in murine Mthfd1 knockout cells transfected with Arg653Gln is reduced by 26%, compared to cells transfected with wild-type protein, the mutant may increase the risk for neural tube defects, under ideal storage and standard assay conditions, the synthetase activity of MTHFD1 is unaffected by the R653Q mutation
additional information
in Escherichia coli DELTAfolD mutants, the essential function of folD can be replaced by Clostridium perfringens fhs when it is provided on a medium-copy-number plasmid or integrated as a single-copy gene in the chromosome. The fhs-supported folD deletion (DELTAfolD) strain grows well in a complex medium. The DELTAfolD strain, harboring heterologous fhs on the chromosome, shows a high NADP+ -to-NADPH ratio and hypersensitivity to trimethoprim. The presence of fhs in Escherichia coli is disadvantageous for its aerobic growth. but under hypoxia, Escherichia coli strains harboring fhs outcompete those lacking it
additional information
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in Escherichia coli DELTAfolD mutants, the essential function of folD can be replaced by Clostridium perfringens fhs when it is provided on a medium-copy-number plasmid or integrated as a single-copy gene in the chromosome. The fhs-supported folD deletion (DELTAfolD) strain grows well in a complex medium. The DELTAfolD strain, harboring heterologous fhs on the chromosome, shows a high NADP+ -to-NADPH ratio and hypersensitivity to trimethoprim. The presence of fhs in Escherichia coli is disadvantageous for its aerobic growth. but under hypoxia, Escherichia coli strains harboring fhs outcompete those lacking it
additional information
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in Escherichia coli DELTAfolD mutants, the essential function of folD can be replaced by Clostridium perfringens gene fhs. Simultaneous presence of Clostridium perfringens 5,10-methenyltetrahydrofolate dehydrogenase and 5,10-methenyltetrahydrofolate cyclohydrolase, CpeFolD and CpeFchA, supports the growth of the DELTAfolD/pCpeFhs strain in M9 minimal medium, and rescues it for its requirements for formate and glycine
additional information
in Escherichia coli DELTAfolD mutants, the essential function of folD can be replaced by Clostridium perfringens gene fhs. Simultaneous presence of Clostridium perfringens 5,10-methenyltetrahydrofolate dehydrogenase and 5,10-methenyltetrahydrofolate cyclohydrolase, CpeFolD and CpeFchA, supports the growth of the DELTAfolD/pCpeFhs strain in M9 minimal medium, and rescues it for its requirements for formate and glycine
additional information
-
in Escherichia coli DELTAfolD mutants, the essential function of folD can be replaced by Clostridium perfringens fhs when it is provided on a medium-copy-number plasmid or integrated as a single-copy gene in the chromosome. The fhs-supported folD deletion (DELTAfolD) strain grows well in a complex medium. The DELTAfolD strain, harboring heterologous fhs on the chromosome, shows a high NADP+ -to-NADPH ratio and hypersensitivity to trimethoprim. The presence of fhs in Escherichia coli is disadvantageous for its aerobic growth. but under hypoxia, Escherichia coli strains harboring fhs outcompete those lacking it
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additional information
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in Escherichia coli DELTAfolD mutants, the essential function of folD can be replaced by Clostridium perfringens gene fhs. Simultaneous presence of Clostridium perfringens 5,10-methenyltetrahydrofolate dehydrogenase and 5,10-methenyltetrahydrofolate cyclohydrolase, CpeFolD and CpeFchA, supports the growth of the DELTAfolD/pCpeFhs strain in M9 minimal medium, and rescues it for its requirements for formate and glycine
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additional information
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the recombinant protein product (short isoform) of the alternatively spliced short transcript of the mitochondrial isozyme is not enzymatically active
additional information
MTHFD1L-knockdown in cells is established by shRNA. Knockdown of MTHFD1L causes cell cycle delay
additional information
short hairpin RNA (shRNA)-induced MTHFD1L silencing, analysis of the effcets on the biological behavior of OSCC cells are assessed in vitro and in vivo, overview. Knockdown of MTHFD1L suppresses cell proliferation, colony formation, and tumorigenesis, while it induces apoptosis in oral squamous cell carcinoma (OSCC). Mechanistically, a microarray analysis shows that MTHFD1L suppresses c-MYC and activates p53 signaling by regulating the protein expression of TP53, GADD45A, FAS and JUN
additional information
construction of a DCS disruption knockout mutant fibroblast SF6 cell line lacking the cytoplasmic isozyme but expressing active mitochondrial isozyme from a disruption mutant embryonic stem cell line
additional information
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the recombinant protein product (short isoform) of the alternatively spliced short transcript of the mitochondrial isozyme is not enzymatically active
