Information on EC 1.5.7.1 - methylenetetrahydrofolate reductase (ferredoxin)

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The expected taxonomic range for this enzyme is: Clostridium formicaceticum

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EC NUMBER
COMMENTARY hide
1.5.7.1
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RECOMMENDED NAME
GeneOntology No.
methylenetetrahydrofolate reductase (ferredoxin)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-methyltetrahydrofolate + 2 oxidized ferredoxin = 5,10-methylenetetrahydrofolate + 2 reduced ferredoxin + 2 H+
show the reaction diagram
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
folate transformations I
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Metabolic pathways
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One carbon pool by folate
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reductive acetyl coenzyme A pathway I (homoacetogenic bacteria)
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reductive acetyl coenzyme A pathway
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SYSTEMATIC NAME
IUBMB Comments
5-methyltetrahydrofolate:ferredoxin oxidoreductase
An iron-sulfur flavoprotein that also contains zinc. The enzyme from Clostridium formicoaceticum catalyses the reduction of methylene blue, menadione, benzyl viologen, rubredoxin or FAD with 5-methyltetrahydrofolate and the oxidation of reduced ferredoxin or FADH2 with 5,10-methylenetetrahydrofolate. However, unlike EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H], there is no activity with NAD(P)H.
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CAS REGISTRY NUMBER
COMMENTARY hide
9028-69-7
cf. EC 1.7.99.5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5,10-methylenetetrahydrofolate + FADH2
5,10-methylenetetrahydrofolate + FAD
show the reaction diagram
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-
-
-
?
5,10-methylenetetrahydrofolate + reduced ferredoxin
5-methyltetrahydrofolate + ferredoxin
show the reaction diagram
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-
-
-
?
5-methyltetrahydrofolate + benzyl viologen
5,10-methylenetetrahydrofolate + reduced benzyl viologen
show the reaction diagram
5-methyltetrahydrofolate + FAD
5,10-methylenetetrahydrofolate + FADH2
show the reaction diagram
-
11% of the activity with methylene blue
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-
?
5-methyltetrahydrofolate + menadione
5,10-methylenetetrahydrofolate + reduced menadiol
show the reaction diagram
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25% of the activity with methylene blue
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-
?
5-methyltetrahydrofolate + rubredoxin
5,10-methylenetetrahydrofolate + reduced rubredoxin
show the reaction diagram
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11% of the activity with methylene blue
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-
?
additional information
?
-
-
no activity with pyridine nucleotides
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-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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contains 1.7 FAD per 237000 Da enzyme
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
-
iron-sulfur protein, contains 15.2 iron and 19.5 acid labile sulfide per 237000 Da enzyme
Zinc
-
enzyme contains 2.3 zinc per 237000 Da enzyme
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
5-methyltetrahydrofolate
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-
11.1
benzyl viologen
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-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26000
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alpha4beta4, 4 * 26000 + 4 * 35000, SDS-PAGE
35000
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alpha4beta4, 4 * 26000 + 4 * 35000, SDS-PAGE
237000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
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alpha4beta4, 4 * 26000 + 4 * 35000, SDS-PAGE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1 - 7.6
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the enzyme is more stable in Tris/HCl than in triethanolamine/HCl or phosphate buffer
437714
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme loses 50% of the activity within 2 h in aerobic buffer (0.1 M Tris/HCl buffer, pH 7.4) with or without a reducing agent and in anaerobic buffer without a reducing agent
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437714
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
10°C, pH 7.4, 50 mM Tris/HCl containing 20% glycerol and 2 mM dithionite in an anaerobic chamber
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.5.7.1)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)