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Information on EC 6.3.3.2 - 5-formyltetrahydrofolate cyclo-ligase and Organism(s) Arabidopsis thaliana and UniProt Accession Q8L539

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EC Tree
     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.3 Cyclo-ligases
                6.3.3.2 5-formyltetrahydrofolate cyclo-ligase
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q8L539 not found.
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
mthfd1, mthfs, methenyltetrahydrofolate synthetase, 5,10-methenyltetrahydrofolate synthetase, 5-fcl, 5-formyltetrahydrofolate cyclo-ligase, fau1p, 5-cho-thf cycloligase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5,10-methenyl-tetrahydrofolate synthetase
-
-
-
-
5,10-Methenyltetrahydrofolate synthetase
5,10-Methenyltetrahydropteroylglutamate synthetase
-
-
-
-
5-CHO-THF cycloligase
-
-
5-Formyltetrahydrofolate cyclodehydrase
-
-
-
-
CH+-THF synthetase
-
-
-
-
Formyltetrahydrofolic cyclodehydrase
-
-
-
-
Methenyl THFS
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-
-
-
Methenyl-THF synthetase
-
-
-
-
Methenyltetrahydrofolate synthetase
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-
-
-
MTHFS
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-
-
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N5-Formyltetrahydrofolic acid cyclodehydrase
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-
-
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Synthetase, methenyltetrahydrofolate
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heteroatomic ring closure
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heteroatomic ring closure
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
5-formyltetrahydrofolate cyclo-ligase (ADP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
37318-64-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
show the reaction diagram
-
-
ir
ATP + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methylenetetrahydrofolate
show the reaction diagram
-
-
ir
ATP + 5-formyltetrahydrofolate-pentaglutamate
ADP + phosphate + 5,10-methylenetetrahydrofolate-pentaglutamate
show the reaction diagram
preferred substrate to the monoglutamyl form
-
ir
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
show the reaction diagram
additional information
?
-
enzyme is specific for the 6S-isomer
-
?
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 + 5-formyltetrahydrofolate
ADP + phosphate + 5,10-methenyltetrahydrofolate
show the reaction diagram
-
-
ir
ATP + 5-formyltetrahydrofolate
ADP + 5,10-methenyltetrahydrofolate + phosphate
show the reaction diagram
-
recycling reaction
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.3
5-formyltetrahydrofolate
truncated recombinant enzyme, pH 6.0, 23°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
activity of recombinant enzyme lacking the mitochondrial targeting sequence is significantly higher than the activity of the full length recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
bicine buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 9
linear increase of activity to maximum at pH 8.5
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
5FCL_ARATH
277
0
31233
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26500
1 * 26500, recombinant truncated enzyme, amino acid sequence determination
27000
recombinant truncated enzyme, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 26500, recombinant truncated enzyme, amino acid sequence determination
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
insertional mutation of the gene encoding the enzyme, At5g13050 or 28D07, reduces the growth rate of the mutant plants by 20% and delayes flowering by 1 week, and leads to accumulation of 5-formyltetrahydrofolate and glycine in leaves under photorespiratory conditions, effect of 5-formyltetrahydrofolate feeding, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to near homogeneity, recombinant enzyme from Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination and analysis, expression in Escherichia coli BL21 as full length or truncated protein, the latter lacking the mitochondrial targeting sequence, functional complementation of enzyme deficient yeast fau1 mutant, yeast strain WHY1.3.1
insertional mutant DNA sequence determination and analysis
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Roje, S.; Janave, M.T.; Ziemak, M.J.; Hanson, A.D.
Cloning and characterization of mitochondrial 5-formyltetrahydrofolate cycloligase from higher plants
J. Biol. Chem.
277
42748-42754
2002
Pisum sativum, Arabidopsis thaliana (Q8L539), Solanum lycopersicum (Q8LKF6), Solanum lycopersicum
Manually annotated by BRENDA team
Goyer, A.; Collakova, E.; Diaz de la Garza, R.; Quinlivan, E.P.; Williamson, J.; Gregory, J.F., 3rd; Shachar-Hill, Y.; Hanson, A.D.
5-Formyltetrahydrofolate is an inhibitory but well tolerated metabolite in Arabidopsis leaves
J. Biol. Chem.
280
26137-26142
2005
Arabidopsis thaliana
Manually annotated by BRENDA team