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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 6.3.4.3 - formate-tetrahydrofolate ligase and Organism(s) Moorella thermoacetica and UniProt Accession P21164

for references in articles please use BRENDA:EC6.3.4.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.4 Other carbon-nitrogen ligases
                6.3.4.3 formate-tetrahydrofolate ligase
IUBMB Comments
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Moorella thermoacetica
UNIPROT: P21164
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Moorella thermoacetica
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
fthfs, formyltetrahydrofolate synthetase, c1-thf synthase, mthfd, 10-formyltetrahydrofolate synthetase, c1-tetrahydrofolate synthase, 10-formyl-thf synthetase, methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase-formyltetrahydrofolate synthetase, methylenetetrahydrofolate dehydrogenase 1-like, n10-formyltetrahydrofolate synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Formyltetrahydrofolate synthetase
-
N10-formyltetrahydrofolate synthetase
-
10-Formyltetrahydrofolate synthetase
-
-
-
-
FHS
-
-
-
-
formate-tetrahydrofolate ligase
-
-
-
-
formate:tetrahydrofolate ligase (ADP-forming)
-
-
-
-
Formyl-THF synthetase
-
-
-
-
Formyltetrahydrofolate synthetase
-
-
-
-
FTHFS
Synthetase, formyl tetrahydrofolate
-
-
-
-
Tetrahydrofolate formylase
-
-
-
-
Tetrahydrofolic formylase
-
-
-
-
THFS
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
formylation
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-66-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
ADP + carbamoylphosphate + tetrahydrofolate
ATP + ?
show the reaction diagram
-
-
-
?
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
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + formate + tetrahydrofolate
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
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
ADP + phosphate + 10-formyltetrahydrofolate
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
monovalent cation required for activity
NH4+
monovalent cation required for activity
Rb+
-
activates synthesis of 10-formyltetrahydrofolate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-dipyridyl disulfide
-
-
Fluorescein mercuric acetate
-
-
p-hydroxymercuribenzoate
-
-
Tetranitromethane
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.087 - 0.16
ATP
0.46 - 0.95
formate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.39 - 6.08
ATP
0.4 - 6.08
formate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
780
recombinant FTHFS
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FTHS_MOOTH
559
0
59993
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
59983
-
x * 59983, calculation from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
4 * 60000, X-ray crystallography
tetramer
4 * 60000, SDS-PAGE
?
-
x * 59983, calculation from nucleotide sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
69
in the absence of monovalent cation
79
in the presence of 200 mM K+
75
-
rapid denaturation
additional information
-
NH4+ and K+, but not Na+ increase the thermostability
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
heparin agarose column chromatography and phenyl Sepharose column chromatography
recombinant FTHFS, heparin Agarose, Phenyl Sepharose
recombinant FTHFS
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lovell, C.R.; Przybyla, A.; Ljungdahl, L.G.
Cloning and expression in Escherichia coli of the Clostridium thermoaceticum gene encoding thermostable formyltetrahydrofolate synthetase
Arch. Microbiol.
149
280-285
1988
Moorella thermoacetica
Manually annotated by BRENDA team
Buttlaire, D.H.
Purification and properties of formyltetrahydrofolate synthetase
Methods Enzymol.
66
585-599
1980
Clostridium acidi-urici, Clostridium cylindrosporum, Escherichia coli, Gallus gallus, Homo sapiens, Micrococcus aerogenes, Moorella thermoacetica, Neurospora crassa, Oryctolagus cuniculus, Ovis aries, Pigeon, Pisum sativum, Priestia megaterium, Proteus vulgaris, Saccharomyces cerevisiae, Spinacia oleracea, Veillonella parvula
Manually annotated by BRENDA team
Elliott, J.I.; Ljungdahl, L.G.
Chemical modification of cysteine and tyrosine residues in formyltetrahydrofolate synthetase from Clostridium thermoaceticum
Arch. Biochem. Biophys.
215
245-252
1982
Moorella thermoacetica
Manually annotated by BRENDA team
Shoaf, W.T.; Neece, S.H.; Ljungdahl, L.G.
Effects of temperature and ammonium ions on formyltetrahydrofolate synthetase from Clostridium thermoaceticum
Biochim. Biophys. Acta
334
448-458
1974
Moorella thermoacetica
-
Manually annotated by BRENDA team
Lewinski, K.; Hui, Y.; Jakob, C.G.; Lovell, C.R.; Lebioda, L.
Crystallization and preliminary crystallographic data for formyltetrahydrofolate synthetase from Clostridium thermoaceticum
J. Mol. Biol.
229
1153-1156
1993
Moorella thermoacetica
Manually annotated by BRENDA team
Lovell, C.R.; Przybyla, A.; Ljungdahl, L.G.
Primary structure of the thermostable formyltetrahydrofolate synthetase from Clostridium thermoaceticum
Biochemistry
29
5687-5694
1990
Moorella thermoacetica
Manually annotated by BRENDA team
Leaphart, A.B.; Trent Spencer, H.; Lovell, C.R.
Site-directed mutagenesis of a potential catalytic and formyl phosphate binding site and substrate inhibition of N10-formyltetrahydrofolate synthetase
Arch. Biochem. Biophys.
408
137-143
2002
Moorella thermoacetica
Manually annotated by BRENDA team
Radfar, R.; Leaphart, A.; Brewer, J.M.; Minor, W.; Odom, J.D.; Dunlap, R.B.; Lovell, C.R.; Lebioda, L.
Cation binding and thermostability of FTHFS monovalent cation binding sites and thermostability of N10-formyltetrahydrofolate synthetase from Moorella thermoacetica
Biochemistry
39
14481-14486
2000
Moorella thermoacetica (P21164), Moorella thermoacetica
Manually annotated by BRENDA team
Radfar, R.; Shin, R.; Sheldrick, G.M.; Minor, W.; Lovell, C.R.; Odom, J.D.; Dunlap, R.B.; Lebioda, L.
The crystal structure of N(10)-formyltetrahydrofolate synthetase from Moorella thermoacetica
Biochemistry
39
3920-3926
2000
Moorella thermoacetica (P21164)
Manually annotated by BRENDA team
Xu, K.; Liu, H.; Du, G.; Chen, J.
Real-time PCR assays targeting formyltetrahydrofolate synthetase gene to enumerate acetogens in natural and engineered environments
Anaerobe
15
204-213
2009
Clostridium perfringens, Sphingomonas paucimobilis, Mesorhizobium loti, Rhizobium leguminosarum, Sinorhizobium meliloti, Treponema denticola, Mesorhizobium sp., Sinorhizobium medicae, Desulfovibrio piger, Rhodobacterales, Gottschalkia acidurici (P13419), Moorella thermoacetica (P21164), Acetobacterium carbinolicum (Q15K82), Treponema primitia (Q8GIN9), Eubacterium limosum (Q8GJ02), Eubacterium limosum (Q9AHR7), Acetobacterium psammolithicum (Q8GMP9), Caldanaerobacter subterraneus subsp. tengcongensis (Q8R7L3), Sporomusa termitida (Q9AHR4), Sporomusa ovata (Q9AHR5), Blautia producta (Q9AHR6), Clostridium aceticum (Q9AHR8), Thermoanaerobacter kivui (Q9AHR9), Clostridium formicaceticum (Q9AHS1), Acetobacterium woodii (Q9AHS2), Thermoplasma acidophilum (Q9HI67), Mesorhizobium sp. BNC1
Manually annotated by BRENDA team
Celeste, L.R.; Chai, G.; Bielak, M.; Minor, W.; Lovelace, L.L.; Lebioda, L.
Mechanism of N10-formyltetrahydrofolate synthetase derived from complexes with intermediates and inhibitors
Protein Sci.
21
219-228
2012
Moorella thermoacetica (P21164), Moorella thermoacetica
Manually annotated by BRENDA team