Information on EC 6.3.4.3 - formate-tetrahydrofolate ligase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
6.3.4.3
-
RECOMMENDED NAME
GeneOntology No.
formate-tetrahydrofolate ligase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
substrate binds to the enzyme in a random fashion, products are not released until all substrates are bound
-
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
stepwise mechanism involving a dissociable intermediate, consistent only with a sequential mechanism
-
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
stepwise reaction mechanism, formyl phosphate is a potential intermediate
-
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
direct formylation at the N-10 position, solvent oxygen is not incorporated into N10-formyltetrahydrofolate
-
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
sequential mechanism, formyl phosphate is an intermediate
-
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
the enzyme is not trifunctional showing only 10-formyl-THS synthetase activity, enzyme evolutionary considerations
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
formylation
-
-
-
-
formylation
-
-
formylation
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
folate polyglutamylation
-
-
folate transformations I
-
-
folate transformations II
-
-
formate reduction to 5,10-methylenetetrahydrofolate
-
-
reductive acetyl coenzyme A pathway
-
-
folate polyglutamylation
-
-
reductive acetyl coenzyme A pathway
-
-
One carbon pool by folate
-
-
Carbon fixation pathways in prokaryotes
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
formate:tetrahydrofolate ligase (ADP-forming)
In eukaryotes occurs as a trifunctional enzyme also having methylenetetrahydrofolate dehydrogenase (NADP+) (EC 1.5.1.5) and methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) activity.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10-formyl-THF synthetase
-
-
10-Formyltetrahydrofolate synthetase
-
-
-
-
10-Formyltetrahydrofolate synthetase
-
-
10-Formyltetrahydrofolate synthetase
-
10-Formyltetrahydrofolate synthetase
-
-
10-Formyltetrahydrofolate synthetase
-
10-formylTHF synthetase
-
C(1)-tetrahydrofolate synthase
-
a monofunctional 10-formyl-tetrahydrofolate synthetase lacking the 5,10-methylene-tetrahydrofolate dehydrogenase and 5,10-methenyl-tetrahydrofolate cyclohydrolase activities typically found in the trifunctional cytoplasmic proteins
C1 synthase
-
C1-tetrahydrofolate synthase
-
-
C1-tetrahydrofolate synthase
-
C1-tetrahydrofolate synthase
-
-
C1-tetrahydrofolate synthetase
-
C1-THF synthase
-
-
dehydrogenasse-cyclohydrolase-synthetase
-
FHS
-
-
-
-
formate-tetrahydrofolate ligase
-
-
-
-
formate-tetrahydrofolate ligase
-
-
formate:tetrahydrofolate ligase (ADP-forming)
-
-
-
-
Formyl-THF synthetase
-
-
-
-
Formyl-THF synthetase
-
-
Formyltetrahydrofolate synthetase
-
-
-
-
Formyltetrahydrofolate synthetase
-
-
Formyltetrahydrofolate synthetase
-
Formyltetrahydrofolate synthetase
-
Formyltetrahydrofolate synthetase
-
-
Formyltetrahydrofolate synthetase
-
Formyltetrahydrofolate synthetase
-
Formyltetrahydrofolate synthetase
-
-
Formyltetrahydrofolate synthetase
-
Formyltetrahydrofolate synthetase
-
Formyltetrahydrofolate synthetase
-
-
Formyltetrahydrofolate synthetase
-
-
Formyltetrahydrofolate synthetase
-
-
Formyltetrahydrofolate synthetase
-
-
Formyltetrahydrofolate synthetase
-
Formyltetrahydrofolate synthetase
-
-
Formyltetrahydrofolate synthetase
-
Formyltetrahydrofolate synthetase
-
-
Formyltetrahydrofolate synthetase
-
Formyltetrahydrofolate synthetase
Mesorhizobium loti, Mesorhizobium sp.
-
-
Formyltetrahydrofolate synthetase
Mesorhizobium sp. BNC1
-
-
-
Formyltetrahydrofolate synthetase
-
Formyltetrahydrofolate synthetase
-
Formyltetrahydrofolate synthetase
-
-
Formyltetrahydrofolate synthetase
-
-
Formyltetrahydrofolate synthetase
-
Formyltetrahydrofolate synthetase
-
-
Formyltetrahydrofolate synthetase
-
Formyltetrahydrofolate synthetase
-
Formyltetrahydrofolate synthetase
-
Formyltetrahydrofolate synthetase
-
-
Formyltetrahydrofolate synthetase
-
Formyltetrahydrofolate synthetase
-
Formyltetrahydrofolate synthetase
-
-
Formyltetrahydrofolate synthetase
-
FTHFS
-
-
-
-
FTHFS
Mesorhizobium loti, Mesorhizobium sp.
-
-
FTHFS
Mesorhizobium sp. BNC1
-
-
-
methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase
-
methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase enzyme
-
MTHFD
-
-
MTHFD1
trifunctional enzyme consisting of methylenetetrahydrofolate-dehydrogenase, methenyltetrahydrofolate-cyclohydrolase, and formyltetrahydrofolate synthetase
MTHFD1
-
-
MTHFD1L
-
-
N10-formyltetrahydrofolate synthetase
-
Synthetase, formyl tetrahydrofolate
-
-
-
-
Tetrahydrofolate formylase
-
-
-
-
Tetrahydrofolic formylase
-
-
-
-
THF synthase
-
MTHFDIL gene product
THFS
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9023-66-9
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
fragment; isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
Bacillus subtilis W168
W168
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
Clostridium acidi-urici
-
-
-
Manually annotated by BRENDA team
Clostridium acidi-urici
9a
-
-
Manually annotated by BRENDA team
Clostridium acidi-urici
monofunctional enzyme
-
-
Manually annotated by BRENDA team
Clostridium acidi-urici 9a
9a
-
-
Manually annotated by BRENDA team
wild-type and site-directed mutant enzymes H125S, H131S, and H268S
-
-
Manually annotated by BRENDA team
fragment; isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
Enterococcus faecalis 19433
19433
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
strain VPI 12708
-
-
Manually annotated by BRENDA team
Eubacterium sp. VPI 12708
strain VPI 12708
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
mutation in MTHFD can act as a risk factor in human neural tube defects, however, it is unlikely that this gene plays a major role in the etiology of neural tube defects
-
-
Manually annotated by BRENDA team
trifunctional enzyme
SwissProt
Manually annotated by BRENDA team
trifunctional enzyme with 10-formyltetrahydrofolate synthetase, EC 6.3.4.3, 5,10-methenyltetrahydrofolate cyclohydrolase, EC 3.5.4.9, and 5,10-methylenetetrahydrofolate dehydrogenase activity, EC 1.5.1.5
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
Mesorhizobium sp.
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
Mesorhizobium sp. BNC1
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
Micrococcus luteus 4698
4698
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
previously referred to as Clostridium thermoaceticum
UniProt
Manually annotated by BRENDA team
25238, weak activity
-
-
Manually annotated by BRENDA team
DCS, complete gene and exon 27; gene mthfd1 encodes the cytosolic isozyme which is a trifunctional methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase enzyme DCS, a mitochondrial monofunctional 10-formyltetrahydrofolate synthetase isozyme is encoded by a different gene
SwissProt
Manually annotated by BRENDA team
trifunctional enzyme with 10-formyltetrahydrofolate synthetase, EC 6.3.4.3, 5,10-methenyltetrahydrofolate cyclohydrolase, EC 3.5.4.9, and 5,10-methylenetetrahydrofolate dehydrogenase activity, EC 1.5.1.5
-
-
Manually annotated by BRENDA team
trifunctional enzyme with 10-formyltetrahydrofolate synthetase, EC 6.3.4.3, 5,10-methenyltetrahydrofolate cyclohydrolase, EC 3.5.4.9, and 5,10-methylenetetrahydrofolate dehydrogenase activity, EC 1.5.1.5
-
-
Manually annotated by BRENDA team
Peptostreptococcus anaerobius 27337
27337
-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
monofunctional enzyme
-
-
Manually annotated by BRENDA team
Proteus mirabilis 25433
25433
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
trifunctional enzyme with 10-formyltetrahydrofolate synthetase, EC 6.3.4.3, 5,10-methenyltetrahydrofolate cyclohydrolase, EC 3.5.4.9, and 5,10-methylenetetrahydrofolate dehydrogenase activity, EC 1.5.1.5
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
fragment; isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
Staphylococcus epidermidis 14990
14990
-
-
Manually annotated by BRENDA team
trifunctional enzyme with 10-formyltetrahydrofolate synthetase, EC 6.3.4.3, 5,10-methenyltetrahydrofolate cyclohydrolase, EC 3.5.4.9, and 5,10-methylenetetrahydrofolate dehydrogenase activity, EC 1.5.1.5
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
-
-
Manually annotated by BRENDA team
isolated from environmental samples collected from different sites in Wux, China, gene fths
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
complete loss of synthetase activity is incompatible with life. Embryos die shortly after 10.5 days gestation, and are developmentally delayed or abnormal. Female synthetase-deficient mice have decreased neutrophil counts during pregnancy and increased incidence of developmental defects in embryos. Synthetase deficiency may lead to pregnancy complications through decreased purine synthesis and reduced cellular proliferation
metabolism
-
FTHFS is a key enzyme of the Wood-Ljungdahl pathway
metabolism
FTHFS is a key enzyme of the Wood-Ljungdahl pathway
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R,S)-tetrahydrofolate + ATP + formate
?
show the reaction diagram
-
-
-
-
r
ADP + carbamoylphosphate + tetrahydrofolate
ATP + ?
show the reaction diagram
-
-
-
?
ADP + phosphate + 10-formyltetrahydrofolate
?
show the reaction diagram
Clostridium cylindrosporum, Clostridium acidi-urici
-
ATP production. The relative concentration of formylated and unformylated folate coenzymes may be a significant regulatory parameter in the purine-fermenting Clostridia
-
-
-
ATP + (6R,S)-tetrahydrofolate pteroylpentaglutamate
ADP + phosphate + 10-formyltetrahydrofolate pteroylpentaglutamate
show the reaction diagram
-
-
-
?
ATP + (6R,S)-tetrahydrofolate pteroyltriglutamate
ADP + phosphate + 10-formyltetrahydrofolate pteroyltriglutamate
show the reaction diagram
-
-
-
?
ATP + formate
ADP + HCOOPO32-
show the reaction diagram
-
formate kinase reaction, sequential random bi bi mechanism
-
-
ATP + formate + (6R,S)-tetrahydrofolate monoglutamate
ADP + phosphate + 10-formyltetrahydrofolate monoglutamate
show the reaction diagram
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
Clostridium acidi-urici
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
Clostridium acidi-urici
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
Clostridium acidi-urici
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
Clostridium acidi-urici
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
Clostridium acidi-urici
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
Clostridium acidi-urici
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
Clostridium acidi-urici
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
r
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
r
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
r
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
r
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
r
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
r
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
trifuntional enzyme having 10-formyl-tetrahydrofolate synthetase, 5,10-methylene-tetrahydrofolate cyclohydrolase and 5,10-methylene-tetrahydrofolate dehydrogenase activity
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
FtfL activity is required for methylotrophic growth
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
flow of one-carbon units through cytoplasmic and mitochondrial folate pathways, overview
-
r
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
Eubacterium sp. VPI 12708, Staphylococcus epidermidis 14990, Clostridium acidi-urici 9a, Proteus mirabilis 25433, Micrococcus luteus 4698, Enterococcus faecalis 19433, Bacillus subtilis W168
-
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
Peptostreptococcus anaerobius 27337
-
-
-
-
ATP + formate + tetrahydrofolate
?
show the reaction diagram
-
enzyme of one-carbon metabolism
-
-
-
ATP + formate + tetrahydrofolate
?
show the reaction diagram
-
two different physiological roles: 1. Functions anabolically in most organisms to activate formate via the forward reaction, and brings it into the one-carbon metabolic pool as N10-formyltetrahydrofolate, 2. In purine-fermenting bacteria the enzyme probably functions catabolically in the terminal step of the purine degradative pathway. This reaction may be responsible for ATP production in these organisms
-
-
-
ATP + formate + tetrahydrofolate
?
show the reaction diagram
-
the trifunctional enzyme is involved in the interconversion of one-carbon adducts of tetrahydrofolate
-
-
-
ATP + formate + tetrahydrofolate
?
show the reaction diagram
Clostridium acidi-urici
-
the enzyme is responsible for the recruitment of single carbon units from the formate pool into a variety of folate-dependent biosynthetic pathways
-
-
-
ATP + formate + tetrahydrofolate
?
show the reaction diagram
-
rate-determining step in the conversion of formate to Ser
-
-
-
ATP + formate + tetrahydropteroyl-(Glu)n
ADP + phosphate + 10-formyltetrahydropteroyl-(Glu)n
show the reaction diagram
-
-
-
-
ATP + formate + tetrahydropteroyl-(Glu)n
ADP + phosphate + 10-formyltetrahydropteroyl-(Glu)n
show the reaction diagram
-
r, n: 3
-
-
ATP + formate + tetrahydropteroyl-(Glu)n
ADP + phosphate + 10-formyltetrahydropteroyl-(Glu)n
show the reaction diagram
-
n: 1-5
-
-
ATP + formate + tetrahydropteroyl-(Glu)n
ADP + phosphate + 10-formyltetrahydropteroyl-(Glu)n
show the reaction diagram
-
n: 1-5
-
-
ATP + formate + tetrahydropteroyl-(Glu)n
ADP + phosphate + 10-formyltetrahydropteroyl-(Glu)n
show the reaction diagram
-
n: 1-5
-
-
ATP + formate + tetrahydropteroyl-(Glu)n
ADP + phosphate + 10-formyltetrahydropteroyl-(Glu)n
show the reaction diagram
-
n: 1-6
-
-
ATP + formate + tetrahydropteroyl-(Glu)n
ADP + phosphate + 10-formyltetrahydropteroyl-(Glu)n
show the reaction diagram
-
r, n: 2,3
-
-
Carbamoyl phosphate + ADP
? + ATP
show the reaction diagram
-
-
-
-
Carbamoyl phosphate + ADP
? + ATP
show the reaction diagram
-
-
-
-
dATP + formate + tetrahydrofolate
dADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
37% of the activity relative to ATP
-
-
tetrahydrofolate + formate + ATP
10-formyltetrahydrofolate + ADP + phosphate
show the reaction diagram
-
monofunctional enzyme
-
?
tetrahydrofolate + formate + ATP
10-formyltetrahydrofolate + ADP + phosphate
show the reaction diagram
-
monofunctional enzyme similar in structure to the cytoplasmatic trifunctional enzyme, dehydrogenase and cyclohydrolase activities are silent due to mutations of critical binding and catalytic residues
mitochondria also use formyltetrahydrofolate to produce formylmethionyl-tRNA to initiate protein synthesis
r
tetrahydrofolate + formate + ATP
10-formyltetrahydrofolate + ADP + phosphate
show the reaction diagram
-
trifunctional enzyme exhibits synthetase, dehydrogenase and cyclohydrogenase activities
-
r
tetrahydrofolate + formate + ATP
10-formyltetrahydrofolate + ADP + phosphate
show the reaction diagram
trifunctional enzyme exhibits synthetase, dehydrogenase and cyclohydrolase activities
-
r
formate + ATP + tetrahydrofolate
10-formyltetrahydrofolate + ADP + phosphate
show the reaction diagram
-
synthetase activity of MTHFD1
-
-
additional information
?
-
-
enzyme is involved in the folate-mediated one-carbon metabolism, overview
-
-
-
additional information
?
-
the enzyme may participate in the progression of colorectal cancer by conferring growth advantage
-
-
-
additional information
?
-
-
(MTHFD1) is a trifunctional enzyme that interconverts tetrahydrofolate derivatives for nucleotide synthesis
-
-
-
additional information
?
-
-
Leishmania possess a second cytoplasmic pathway for 10-formyltetrahydrofolate synthesis through FTL
-
-
-
additional information
?
-
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
-
additional information
?
-
-
MTHFD1 is a cytoplasmic enzyme with 5,10-methylenetetrahydrofolate dehydrogenase, 5,10-methenyltetrahydrofolate cyclohydrolase, and 10-formyltetrahydrofolate synthetase activities
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + 10-formyltetrahydrofolate
?
show the reaction diagram
Clostridium cylindrosporum, Clostridium acidi-urici
-
ATP production. The relative concentration of formylated and unformylated folate coenzymes may be a significant regulatory parameter in the purine-fermenting Clostridia
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
P21164
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
P21164
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
Q6UB35
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
A7BK03, A7BK04, A7BK05, A7BK06, A7BK07, A7BK08, A7BK09, A7BK10, A7BK11, A7BK12, A7BK13, A7BK14, A7BK15, A7BK16, A7BK17
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
D4QDA0
-
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
Q83WS0
FtfL activity is required for methylotrophic growth
-
?
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
Q922D8
flow of one-carbon units through cytoplasmic and mitochondrial folate pathways, overview
-
r
ATP + formate + tetrahydrofolate
?
show the reaction diagram
-
enzyme of one-carbon metabolism
-
-
-
ATP + formate + tetrahydrofolate
?
show the reaction diagram
-
two different physiological roles: 1. Functions anabolically in most organisms to activate formate via the forward reaction, and brings it into the one-carbon metabolic pool as N10-formyltetrahydrofolate, 2. In purine-fermenting bacteria the enzyme probably functions catabolically in the terminal step of the purine degradative pathway. This reaction may be responsible for ATP production in these organisms
-
-
-
ATP + formate + tetrahydrofolate
?
show the reaction diagram
-
the trifunctional enzyme is involved in the interconversion of one-carbon adducts of tetrahydrofolate
-
-
-
ATP + formate + tetrahydrofolate
?
show the reaction diagram
Clostridium acidi-urici
-
the enzyme is responsible for the recruitment of single carbon units from the formate pool into a variety of folate-dependent biosynthetic pathways
-
-
-
ATP + formate + tetrahydrofolate
?
show the reaction diagram
-
rate-determining step in the conversion of formate to Ser
-
-
-
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
D4QDA0
-
-
?
tetrahydrofolate + formate + ATP
10-formyltetrahydrofolate + ADP + phosphate
show the reaction diagram
-
monofunctional enzyme
-
?
tetrahydrofolate + formate + ATP
10-formyltetrahydrofolate + ADP + phosphate
show the reaction diagram
-
monofunctional enzyme similar in structure to the cytoplasmatic trifunctional enzyme, dehydrogenase and cyclohydrolase activities are silent due to mutations of critical binding and catalytic residues
mitochondria also use formyltetrahydrofolate to produce formylmethionyl-tRNA to initiate protein synthesis
r
tetrahydrofolate + formate + ATP
10-formyltetrahydrofolate + ADP + phosphate
show the reaction diagram
-
trifunctional enzyme exhibits synthetase, dehydrogenase and cyclohydrogenase activities
-
r
tetrahydrofolate + formate + ATP
10-formyltetrahydrofolate + ADP + phosphate
show the reaction diagram
P05440, P07245
trifunctional enzyme exhibits synthetase, dehydrogenase and cyclohydrolase activities
-
r
formate + ATP + tetrahydrofolate
10-formyltetrahydrofolate + ADP + phosphate
show the reaction diagram
-
synthetase activity of MTHFD1
-
-
additional information
?
-
-
enzyme is involved in the folate-mediated one-carbon metabolism, overview
-
-
-
additional information
?
-
Q6UB35
the enzyme may participate in the progression of colorectal cancer by conferring growth advantage
-
-
-
additional information
?
-
-
(MTHFD1) is a trifunctional enzyme that interconverts tetrahydrofolate derivatives for nucleotide synthesis
-
-
-
additional information
?
-
-
Leishmania possess a second cytoplasmic pathway for 10-formyltetrahydrofolate synthesis through FTL
-
-
-
additional information
?
-
P05440, P07245
the presence of cytoplasmic and mitochondrial isoforms of a trifunctional dehydrogenase-cyclohydrolase-synthetase support a model wherin the mitochondria can produce fromate which can be used by the cytoplasmic enzymes for the synthesis of purins and for methylation reactions
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
the requirement for a divalent cation is most effectively satisfied by Mg2+. Mn2+ and Ca2+ can substitute for Mg2+
Ca2+
-
Km for CaCl2: 0.21 mM; the requirement for a divalent cation is most effectively satisfied by Mg2+. Mn2+ and Ca2+ can substitute for Mg2+
Cs+
-
specific monovalent cations required for maximal activity, order of effectiveness: NH4+, Tl+, Rb+ ~ K+, Cs+, Na+ ~ Li+
Cs+
-
activity is stimulated by various monovalent cations. The order of effectiveness of 10, 50 or 100 mM salts: Rb+, K+, NH4+, Na+, Cs+
Divalent metal ion
-
the requirement for a divalent cation is most effectively satisfied by Mg2+. Mn2+ and Ca2+ can substitute for Mg2+
Divalent metal ion
-
the requirement for a divalent cation is most effectively satisfied by Mg2+. Mn2+ and Ca2+ can substitute for Mg2+
K+
-
specific monovalent cations required for maximal activity, order of effectiveness: NH4+, Tl+, Rb+ ~ K+, Cs+, Na+ ~ Li+
K+
-
activity is stimulated by various monovalent cations. The order of effectiveness of 10, 50 or 100 mM salts: Rb+, K+, NH4+, Na+, Cs+
K+
-
stimulates formate kinase reaction, Km: 8.7 mM
K+
-
Km: 4 mM; K+ or NH4+ required
K+
-
monovalent cation required for activity
K+
-
activates at 100-200 mM, inhibitory above 200 mM
Li+
-
specific monovalent cations required for maximal activity, order of effectiveness: NH4+, Tl+, Rb+ ~ K+, Cs+, Na+ ~ Li+
Mg2+
-
the requirement for a divalent cation is most effectively satisfied by Mg2+. Mn2+ and Ca2+ can substitute for Mg2+
Mg2+
-
the requirement for a divalent cation is most effectively satisfied by Mg2+. Mn2+ and Ca2+ can substitute for Mg2+
Mg2+
-
Km for MgCl2: 0.44 mM; the requirement for a divalent cation is most effectively satisfied by Mg2+. Mn2+ and Ca2+ can substitute for Mg2+
Mg2+
-
stimulates formate kinase reaction, Km: 0.88 mM
Mg2+
-
stimulates
Mg2+
-
-
Mn2+
-
the requirement for a divalent cation is most effectively satisfied by Mg2+. Mn2+ and Ca2+ can substitute for Mg2+
Mn2+
-
Km for MnCl2: 0.23 mM; the requirement for a divalent cation is most effectively satisfied by Mg2+. Mn2+ and Ca2+ can substitute for Mg2+
Monovalent cations
-
specific monovalent cations required for maximal activity, order of effectiveness: NH4+, Tl+, Rb+ ~ K+, Cs+, Na+ ~ Li+
Monovalent cations
-
-
Monovalent cations
-
activity is stimulated by various monovalent cations. The order of effectiveness of 10, 50 or 100 mM salts: Rb+, K+,NH4+, Na+,Cs+
Na+
-
specific monovalent cations required for maximal activity, order of effectiveness: NH4+, Tl+, Rb+ ~ K+, Cs+, Na+ ~ Li+
Na+
-
activity is stimulated by various monovalent cations. The order of effectiveness of 10, 50 or 100 mM salts: Rb+, K+, NH4+, Na+, Cs+
NH4+
-
specific monovalent cations required for maximal activity, order of effectiveness: NH4+, Tl+, Rb+ ~ K+, Cs+, Na+ ~ Li+
NH4+
-
activates forward and reverse reaction
NH4+
-
activity is stimulated by various monovalent cations. The order of effectiveness of 10, 50 or 100 mM salts: Rb+, K+, NH4+, Na+, Cs+
NH4+
-
Km: 1.8 mM; K+ or NH4+ required
NH4+
-
monovalent cation required for activity
NH4+
-
activates, maximal at 100 mM
Rb+
-
specific monovalent cations required for maximal activity, order of effectiveness: NH4+, Tl+, Rb+ ~ K+, Cs+, Na+ ~ Li+
Rb+
-
activates synthesis of 10-formyltetrahydrofolate
Rb+
-
activity is stimulated by various monovalent cations. The order of effectiveness of 10, 50 or 100 mM salts: Rb+, K+, NH4+, Na+, Cs+
Tl+
-
specific monovalent cations required for maximal activity, order of effectiveness: NH4+, Tl+, Rb+ ~ K+, Cs+, Na+ ~ Li+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S)-2-[[4-[(6aR)-3-amino-1,9-dioxo-5,6,6a,7-tetrahydro-4H-imidazol[3,4-f]pteridin-8-yl]benzoyl]amino]pentanedioate
-
5,10-formyltetrahydrofolate substrate analogue inhibits dehydrogenase activity
2,2'-dipyridyl disulfide
-
-
2,4-diamino-6-(3,4-dichlorophenoxy)-quinazoline
-
-
2,4-diamino-6-benzyl-5-(3-phenylpropyl)-pyrimidine
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
acetyl phosphate
-
inhibits ATP synthesis reaction from carbamoyl phosphate and ADP, and synthesis of 10-formyltetrahydrofolate
Adenylyl imidodiphosphate
-
competitive to ATP
ADP
-
competitive to ATP
alpha,beta-methyleneadenosine 5'-triphosphate
-
competitive to ATP
beta,gamma-methyleneadenosine 5'-triphosphate
-
competitive to ATP
Ca2+
-
in presence of Mg2+
Carbamoyl phosphate
-
-
Fluorescein mercuric acetate
-
-
formate
-
inhibits ATP synthesis reaction from carbamoyl phosphate and ADP
Formyltetrahydrofolate
-
-
methotrexate
-
-
Mn2+
-
in presence of Mg2+
p-hydroxymercuribenzoate
-
-
phosphate
-
inhibits ATP synthesis reaction from carbamoyl phosphate and ADP
Phosphonoacetate
-
inhibits ATP synthesis reaction from carbamoyl phosphate and ADP, and synthesis of 10-formyltetrahydrofolate
pteroylpentaglutamate
-
-
Tetranitromethane
-
-
Zn2+
-
in presence of Mg2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
spermine
-
stimulates activity only in absence of NH4+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.5
(6R,S)-tetrahydrofolate monoglutamate
-
above, recombinant enzyme, 30C
0.0036
(6R,S)-tetrahydrofolate pteroylpentaglutamate
-
recombinant enzyme, 30C
0.016
(6R,S)-tetrahydrofolate pteroyltriglutamate
-
recombinant enzyme, 30C
0.032
ADP
-
ATP synthesis from carbamoylphosphate
0.13
ADP
-
formyltetrahydrofolate synthesis
0.13
ADP
-
tetrahydrofolate, mutant enzyme K71Q
0.012
ATP
-
reaction with tetrahydropteroyl-Glu5
0.021
ATP
30C, pH 8.0
0.0286
ATP
-
mutant R653Q
0.0302
ATP
-
wild type
0.04
ATP
-
recombinant enzyme, 30C, with substrate (6R,S)-tetrahydrofolate pteroyltriglutamate or (6R,S)-tetrahydrofolate pteroylpentaglutamate and formate
0.062
ATP
-
reaction with tetrahydropteroyl-Glu3
0.087
ATP
-
27C, pH 7.0, wild-type FTHFS
0.094
ATP
-
reaction with tetrahydrofolate
0.094
ATP
-
ATP, reaction with tetrahydropteroyl-Glu2; reaction with tetrahydrofolate
0.16
ATP
-
27C, pH 7.0, R97S mutant FTHFS
0.2
ATP
-
above, recombinant enzyme, 30C, with substrate (6R,S)-tetrahydrofolate monoglutamate and formate
11.9
Carbamoyl phosphate
-
-
0.035
formate
-
reaction with tetrahydropteroyl-Glu5
0.0367
formate
-
wild type
0.0371
formate
-
mutant R653Q
0.15
formate
-
recombinant enzyme, 30C, with substrate (6R,S)-tetrahydrofolate pteroylpentaglutamate
0.166
formate
-
-
0.43
formate
-
reaction with tetrahydropteroyl-Glu3
0.44
formate
-
recombinant enzyme, 30C, with substrate (6R,S)-tetrahydrofolate pteroyltriglutamate
0.46
formate
-
27C, pH 7.0, wild-type FTHFS
0.95
formate
-
27C, pH 7.0, R97S mutant FTHFS
0.98
formate
-
reaction with tetrahydropteroyl-Glu2
5.4
formate
-
-
6.7
formate
-
wild-type enzyme
7.6
formate
-
reaction with tetrahydrofolate
8.2
formate
-
mutant enzyme H125S
11.8
formate
-
recombinant enzyme, 30C, with substrate (6R,S)-tetrahydrofolate monoglutamate
12.1
formate
-
mutant enzyme K71Q
16
formate
-
-
20.2
formate
-
mutant enzyme H131S
22
formate
30C, pH 8.0
0.056
MgATP2-
-
-
0.067
MgATP2-
-
-
0.086
MgATP2-
-
-
0.12
MgATP2-
-
N10-formyltetrahydropteroyl-Glu3
0.14
MgATP2-
-
formate, reaction with tetrahydropteroyl-Glu4
0.26
MgATP2-
-
mutant enzyme K71Q
0.4
MgATP2-
-
mutant enzyme H131S
10
N10-formyltetrahydrofolate
-
-
0.015
tetrahydrofolate
-
-
0.032 - 0.077
tetrahydrofolate
-
ATP synthesis
0.04
tetrahydrofolate
-
-
0.23
tetrahydrofolate
-
-
0.23
tetrahydrofolate
-
MgATP2-, wild-type enzyme
0.27
tetrahydrofolate
-
formyltretrahydrofolate synthesis
0.333
tetrahydrofolate
-
mutant R653Q
0.364
tetrahydrofolate
-
wild type
0.46
tetrahydrofolate
-
-
0.69
tetrahydrofolate
-
wild-type enzyme
0.8
tetrahydrofolate
30C, pH 8.0
0.97
tetrahydrofolate
-
mutant enzyme H125S
1.12
tetrahydrofolate
-
mutant enzyme H131S
2.3
tetrahydrofolate
-
-
0.0055
tetrahydropteroyl-Glu2
-
-
0.029
tetrahydropteroyl-Glu2
-
-
0.0003
tetrahydropteroyl-Glu3
-
tetrahydropteroyl-Glu6
0.016
tetrahydropteroyl-Glu3
-
-
0.025
tetrahydropteroyl-Glu3
-
-
0.025
tetrahydropteroyl-Glu3
-
ATP, reaction with tetrahydropteroyl-Glu4
0.0001
tetrahydropteroyl-Glu4
-
tetrahydropteroyl-Glu5
0.003
tetrahydropteroyl-Glu5
-
-
0.59
MgATP2-
-
mutant enzyme H125S
additional information
additional information
-
effect of polyglutamate chain length of tetrahydropteroyl-(Glu)n on the Km values of formate and MgATP2-
-
additional information
additional information
-
monovalent cations decrease the Km for formate
-
additional information
additional information
-
-
-
additional information
additional information
-
Km-values for the forward reaction as a function of temperature in the presence and absence of NH4Cl
-
additional information
additional information
-
steady-state kinetics, recombinant enzyme
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
16
(6R,S)-tetrahydrofolate monoglutamate
Homo sapiens
-
above, recombinant enzyme, 30C
2.6
(6R,S)-tetrahydrofolate pteroylpentaglutamate
Homo sapiens
-
recombinant enzyme, 30C
10
(6R,S)-tetrahydrofolate pteroyltriglutamate
Homo sapiens
-
recombinant enzyme, 30C
0.39
ATP
Moorella thermoacetica
-
27C, pH 7.0, R97S mutant FTHFS
0.99
ATP
Moorella thermoacetica
-
27C, pH 7.0, wild-type FTHFS
6.08
ATP
Moorella thermoacetica
-
27C, pH 7.0, wild-type FTHFS
0.4
formate
Moorella thermoacetica
-
27C, pH 7.0, R97S mutant FTHFS
1.13
formate
Moorella thermoacetica
-
27C, pH 7.0, wild-type FTHFS
6.08
formate
Moorella thermoacetica
-
27C, pH 7.0, wild-type FTHFS
additional information
additional information
Clostridium cylindrosporum
-
-
-
additional information
additional information
Saccharomyces cerevisiae
-
-
-
additional information
additional information
Homo sapiens
-
the Kcat/Km tetrahydrofolate values are 0.03 s/M for the monoglutamate and 0.71 s/M for the pentaglutatmate substrates
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0338
ADP
-
mutant R653Q
0.0364
ADP
-
wild type enzyme
0.0296
pteroylpentaglutamate
-
wild type enzyme
0.0328
pteroylpentaglutamate
-
mutant R653Q
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0033
(2S)-2-[[4-[(6aR)-3-amino-1,9-dioxo-5,6,6a,7-tetrahydro-4H-imidazol[3,4-f]pteridin-8-yl]benzoyl]amino]pentanedioate
Leishmania major
-
dhch1-/pXNG4-FTL mutant, FV1 line
0.0037
(2S)-2-[[4-[(6aR)-3-amino-1,9-dioxo-5,6,6a,7-tetrahydro-4H-imidazol[3,4-f]pteridin-8-yl]benzoyl]amino]pentanedioate
Leishmania major
-
WT/pXNG4-FTL mutant, FV1 line
0.00054
2,4-diamino-6-(3,4-dichlorophenoxy)-quinazoline
Leishmania major
-
dhch1-/pXNG4-FTL mutant, FV1 line
0.00042
2,4-diamino-6-benzyl-5-(3-phenylpropyl)-pyrimidine
Leishmania major
-
dhch1-/pXNG4-FTL mutant, FV1 line
0.00004
methotrexate
Leishmania major
-
dhch1-/pXNG4-FTL mutant, FV1 line
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23
-
synthetase activity of the wild type enzyme
23.8
-
synthetase activity of the mutant R653Q
40
-
-
780
-
recombinant FTHFS
additional information
-
-
additional information
-
-
additional information
mitochondrial isozyme activity in different cell lines, overview
additional information
-
100.2% activity of mutant R653Q after heating at 42C for 90 min, in 7.5% glycerol and 0.35 mM folate pentaglutamate; 102% activity of wild type enzyme after heating at 42C for 90 min, in 7.5% glycerol and 0.35 mM folate pentaglutamate; 57.4% activity of mutant R653Q, without adding of any cofactor, after heating at 42C for 90 min, in 7.5% glycerol; 72.3% activity of wild type enzyme, without adding of any cofactor, after heating at 42C for 90 min, in 7.5% glycerol; 80.5% activity of mutant R653Q after heating at 42C for 90 min, in 7.5% glycerol, 1.2 mM MgCl, 0.6 mM ATP; 88.2% activity of wild type enzyme after heating at 42C for 90 min, in 7.5% glycerol, 1.2 mM MgCl, 0.6 mM ATP; enzyme knock-out cells are transfected with either wild type or R653Q mutant and their ability to synthesize purines is assessed by a 14C-formate incorporation assay, the cells expressing the R653Q variant incorporate only 74% of wild-type levels of formate into DNA, the R653Q protein appears to have a significant impact on cellular nucleotide metabolism
additional information
-
MTHFD1L is upregulated in colon adeno-carcinomas; overexpression of MTHFD1L in HEK-292 cells stimulates colony formation indicating that expression of this gene confers a growth advantage
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27
-
assay at
30
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
high transcript levels
Manually annotated by BRENDA team
higher expression level
Manually annotated by BRENDA team
2fold increased expression of gene DKFZp586G1517 compared to normal colon tissue
Manually annotated by BRENDA team
the MTHFD1L transcript is detected at all stages of mouse embryogenesis examined. MTHFD1L is expressed ubiquitously throughout the embryo but with localized regions of higher expression. The spatial pattern of MTHFD1L expression is virtually indistinguishable from that of MTHFD2 and cytoplasmic C1-THF synthase MTHFD1 in embryonic day 9.5 mouse embryos
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
; SF6 cell, immortalized fibroblast with disrupted gene encoding the trifunctional cytosolic DCS
Manually annotated by BRENDA team
embryonic fibroblast cell line
Manually annotated by BRENDA team
-
low expression
Manually annotated by BRENDA team
Pigeon
-
-
Manually annotated by BRENDA team
low transcript levels
Manually annotated by BRENDA team
higher expression level
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
-
low expression
Manually annotated by BRENDA team
high expression level
Manually annotated by BRENDA team
high transcript levels
Manually annotated by BRENDA team
low transcript levels
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
higher expression level
Manually annotated by BRENDA team
high transcript levels
Manually annotated by BRENDA team
-
low expression
Manually annotated by BRENDA team
additional information
isozyme expression analysis and growth rates of cell lines, overview
Manually annotated by BRENDA team
additional information
-
the cytoplasmatic MTHFD1 is ubiquitously expressed in all mammalian cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
trifunctional cytosolic isozyme
Manually annotated by BRENDA team
-
mitochondrial isozyme
Manually annotated by BRENDA team
mitochondrial isozyme, contains an N-terminal mitochondrial targeting sequence
Manually annotated by BRENDA team
mitochondrial monofunctional isozyme
Manually annotated by BRENDA team
-
mitochondrial C1-THF synthase behaves as a peripheral membrane protein, tightly associated with the matrix side of the mitochondrial inner membrane
Manually annotated by BRENDA team
MTHFD1L enzyme is present in mitochondria from normal embryonic tissues and embryonic fibroblast cell lines, and embryonic mitochondria possess the ability to synthesize formate from glycine. Greater than 75% of 1-C units entering the cytoplasmic methyl cycle are mitochondrially derived
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Moorella thermoacetica (strain ATCC 39073)
Moorella thermoacetica (strain ATCC 39073)
Moorella thermoacetica (strain ATCC 39073)
Moorella thermoacetica (strain ATCC 39073)
Moorella thermoacetica (strain ATCC 39073)
Moorella thermoacetica (strain ATCC 39073)
Moorella thermoacetica (strain ATCC 39073)
Moorella thermoacetica (strain ATCC 39073)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
-
recombinant short isoform, SDS-PAGE
690632
107000
-
recombinant mitochondrial C1-THF synthase without the presequence but with the V5 epitope tag, SDS-PAGE
690632
110000
-
gel filtration
1518
130000
-
gel filtration
1519
143000
-
recombinant mitochondrial isozyme, gel filtration
660817
150000
-
gel filtration
1505
201000
-
gel filtration
1505
226000
-
gel filtration
1505
240000
-
gel filtration, sedimentation analysis
1506
240000
gel filtration
651731
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 67727, SDS-PAGE
?
-
x * 59983, calculation from nucleotide sequence
dimer
-
2 * 67000, SDS-PAGE
dimer
-
2 * 56000, SDS-PAGE
dimer
-
2 * 102000, homodimer, sequence calculation
dimer
-
by gel filtration
tetramer
-
in the presence of specific monovalent cations, K+, Cs+, or NH4+, inactive monomers of formyltetrahydrofolate synthetase associate to a catalytically active tetramer
tetramer
Clostridium acidi-urici, Clostridium cylindrosporum
-
enzymes exist as a catalytically active tetramer in the presence of specific monovalent cations or as an inactive monomer in their absence
tetramer
-
4 * 60000, SDS-PAGE
tetramer
4 * 60000, SDS-PAGE
homotetramer
-
4 * 60000, X-ray crystallography
additional information
-
a tryptic fragment that contains 10-formyltetrahydrofolate synthetase activity is a dimer, MW 66000
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Clostridium acidi-urici
-
crystals of FTHFS complexed with NH4+, K+ or Cs+ are grown by vapor diffusion from 46% saturated ammonium sulfate, 1 mM dithiothreitol and 1% polyehtylene glycol 1000 in 50 mM potassium maleate buffer, pH 7.6, crystals diffract to 3.0-3.2 A resolution
-
native protein, folate complex, ADP-formylphosphate complex, and ZD9331-formylphosphate complex, hanging drop vapor diffusion method. High salt conditions contain 38-46% (w/v) saturated ammonium sulfate, 1 mM , and dithiohtreitol, 1-3.5% (w/v) PEG 1000 or PEG 1450, in 50-75 mM KMB (pH 7.0-8.0). Low salt conditions contain 18-22% (w/v) PEG 6-8K, 0.2 M ammonium sulfate, 1 mM dithiothreitol, in 75 mM KMB pH 7.0-8.5
-
Se-Met FTHFS is crystallized by hanging-drop vapor-diffusion, crystals diffract to 2.5 A
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
-
unstable below pH 6.5 and above pH 9.0
1506
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23
-
,the large domain of the multifuncional enzyme, that contains the active site for the 10-formyltetrahydrofolate synthetase is more stable at 23C than at 0C
1532
47
-
transition at 47C is due to the denaturation of a domain which binds MgATP2- and contains the synthetase active site
1532
69
-
in the absence of monovalent cation
649939
70
-
10 min stable
1502
70
-
rapid inactivation in absence of NH4Cl. In presence of 50 mM NH4Cl, about 50% loss of activity after 15 min and no more loss of activity thereafter
1513
75
-
rapid denaturation
1502
79
-
in the presence of 200 mM K+
649939
additional information
-
the binding of tetrahydropteroylpolyglutamate, MgATP2-, and NH4+ increases the denaturation temperature by 12C and abolishes the cold lability of the enzyme
1503
additional information
-
NH4+ and K+, but not Na+ increase the thermostability
1513
additional information
-
thermolability is reduced by magnesium adenosine triphosphate and eliminated by the substrate analog folate pentaglutamate, suggesting that folate status may modulate impact of the variant R653Q
698187
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
photooxidation in presence of methylene blue results in a pseudo-first order loss of enzymatic activity and destruction of histidine residues
Clostridium acidi-urici
-
addition of monovalent cations to the dissociated enzyme causes the inactive monomers to reassociate to the active tetramer. The order of cation effectiveness is NH4+ > Tl+ > Rb+ ~ K+ > Cs+ > Na+ ~ Li+. The rate and extent of reactivation is influenced by the counter ion: sulfate and phosphate stimulate reassociation, thiocyanate, trichloroacetate, and perchlorate completly inhibit reassociation. The extent of reactivation is dependent upon protein concentration. The optimum protein concentration depends on the pH at which reactivation is performed
-
purified enzyme as crystalline suspension, 15% loss of activity after 1 month
-
tetramer is stabilized by 0.1 M sulfate in absence of an active monovalent cation
-
unstable in absence of monovalent cations
-
unstable in presence of urea and guanidinium chloride
-
K+ or NH4+ increase stability of the large domain of the multifuncional enzyme, that contains the active site for the 10-formyltetrahydrofolate synthetase
-
the binding of tetrahydropteroylpolyglutamate, MgATP2-, and NH4+ alters the susceptibility to digestion by chymotrypsin
-
enzyme is unstable in phosphate buffers in the absence of high concentrations of salt
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, in presence of PMSF, minimal loss of activity after several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
Clostridium acidi-urici
-
by anion-exchange chromatography
-
recombinant enzyme is partially purified from HEK-293 cells by subcellular fractionation
recombinant maltose-binding protein fusion mitochondrial isozyme from Escherichia coli by metal affinity chromatography and gel filtration, the MBP-tag is cleaved off by TEV protease
-
TALON cobalt metal affinity resin chromatography
-
ammonium sulfate, Phenyl Sepharose, Source15Q, hydroxyapatite, Resource Q
heparin agarose column chromatography and phenyl Sepharose column chromatography
-
recombinant FTHFS
-
recombinant FTHFS, heparin Agarose, Phenyl Sepharose
TALON cobalt metal affinity resin chromatography
-
large-scale purification
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene FTHFS, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genetic clusters, overview. Cloning and expression in Escherichia coli
-
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
gene FTHFS, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genetic clusters, overview. Cloning and expression in Escherichia coli
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
gene FTHFS, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genetic clusters, overview. Cloning and expression in Escherichia coli
-
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
-
Clostridium acidi-urici
-
expression in Escherichia coli
-
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
gene FTHFS, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genetic clusters, overview. Cloning and expression in Escherichia coli
-
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
-
gene FTHFS, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genetic clusters, overview. Cloning and expression in Escherichia coli
-
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
-
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109; gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
gene FTHFS, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genetic clusters, overview. Cloning and expression in Escherichia coli
-
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
expressed in CHO cells and Escherichia coli
-
expressed in Escherichia coli
-
expression in CHO cells and Saccharomyces cerevisiae
expression in Escherichia coli, localization of the interdomain region of the trifunctional enzyme by site-directed mutagenesis
-
expression of the mitochondrial isozyme as maltose-binding protein fusion protein in Escherichia coli, overexpression in yeast
-
gene DKFZp586G1517, DNA and amino acid sequence determination and analysis, overexpression of mitochondrial enzyme in HEK-293 cells, unlabeled or FLAG-tagged, stimulates cell growth
the wild type and R653Q mutant pBKeDCS constructs are transformed into Escherichia coli BL21 DE3 to express the full-length protein
-
overexpression of FTL using the multicopy episomal vector pXNG4-FTL
-
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
Mesorhizobium loti, Mesorhizobium sp.
-
expressed in Escherichia coli strain Y1
-
expression in Escherichia coli
-
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
DNA sequence determination and analysis
gene FTHFS, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genetic clusters, overview. Cloning and expression in Escherichia coli
-
expressed in CHO cells and Escherichia coli
-
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
-
deletion of the MIS1 gene has little effect
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
-
gene FTHFS, DNA and amino acid sequence determination and analysis, phylogenetic analysis, genetic clusters, overview. Cloning and expression in Escherichia coli
-
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
-
gene fths, DNA and amino acid sequence determination and analysis, quantitative expression analysis by real-time PCR, phylogenetic analysis, cloning and expression in Escherichia coli strain JM109
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H125S
-
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
-
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
-
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
-
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 42C, 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
E98D
-
36% of wild-type activity
E98Q
-
93% of wild-type activity, slight increase in thermal stability in the absence of monovalent cation
E98S
-
61% of wild-type activity
R97E
-
no activity
R97S
-
35% of wild-type kcat
G1958A
-
the mutation is not associated with depression in postmenopausal women
additional information
-
the recombinant protein product (short isoform) of the alternatively spliced short transcript of the mitochondrial isozyme is not enzymatically active
K386E
-
the mutation completely abrogates synthetase activity
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
R653Q
-
the mutation reduces metabolic activity in cells by about 26%
additional information
-
the recombinant protein product (short isoform) of the alternatively spliced short transcript of the mitochondrial isozyme is not enzymatically active
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzymes denatured in 6 M urea and 4 M guanidinium chloride refold upon dilution of the denaturant-protein solution to give final concentrations of 0.5 M urea or 0.1 M guanidinium chloride. In presence of NH4+, but not in its absence the refolded proteins associate to produce the catalytically active tetramer. 80% of the enzymatic acitivity is recovered
Clostridium acidi-urici, Clostridium cylindrosporum
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
the enzyme might be a target for colorectal cancer therapy