Information on EC 1.3.1.105 - 2-methylene-furan-3-one reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.3.1.105
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RECOMMENDED NAME
GeneOntology No.
2-methylene-furan-3-one reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-hydroxy-2,5-dimethylfuran-3(2H)-one + NADP+ = 4-hydroxy-5-methyl-2-methylenefuran-3(2H)-one + NADPH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
furaneol and mesifurane biosynthesis
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homofuraneol biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxy-2,5-dimethylfuran-3(2H)-one:NAD(P)+ oxidoreductase
The enzyme was dicovered in strawberry (Fragaria x ananassa), where it produces furaneol, one of the major aroma compounds in the fruits. It has also been detected in tomato (Solanum lycopersicum) and pineapple (Ananas comosus). The enzyme can also act on derivatives substituted at the methylene functional group. The enzyme from the yeast Saccharomyces cerevisiae acts on (2E)-2-ethylidene-4-hydroxy-5-methylfuran-3(2H)-one and produces homofuraneol, an important aroma compound in soy sauce and miso. NADPH is the preferred cofactor.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
(2R)-4-hydroxy-2,5-dimethyl-3(2H)-furanone is synthesized during the fruit-ripening process as a major aroma compound (55 mg/kg) of strawberry fruits
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E)-2-butylidene-4-hydroxy-5-methyl-3(2H)-furanone + NADH + H+
2-butyl-4-hydroxy-5-methyl-3(2H)-furanone + NAD+
show the reaction diagram
(2E)-4-hydroxy-5-methyl-2-propylidene-3(2H)-furanone + NADH + H+
4-hydroxy-5-methyl-2-propyl-3(2H)-furanone + NAD+
show the reaction diagram
(2E)-ethylidene-4-hydroxy-5-methyl-3(2H)-furanone + NADH + H+
2-ethyl-4-hydroxy-5-methyl-3(2H)-furanone + NAD+
show the reaction diagram
(2E)-ethylidene-4-hydroxy-5-methyl-3(2H)-furanone + NADPH + H+
2-ethyl-4-hydroxy-5-methyl-3(2H)-furanone + 5-ethyl-4-hydroxy-2-methyl-3(2H)-furanone + NADP+
show the reaction diagram
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?
4-hydroxy-5-methyl-2-methylene-3(2H)-furanone + NADH + H+
(2R)-4-hydroxy-2,5-dimethyl-3(2H)-furanone + NAD+
show the reaction diagram
kcat/Km for NADH is 7.5fold lower than for NADPH, Re-specific, i.e. the 4R-hydride of NAD(P)H is transferred
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?
4-hydroxy-5-methyl-2-methylene-3(2H)-furanone + NADH + H+
4-hydroxy-2,5-dimethyl-3(2H)-furanone + NAD+
show the reaction diagram
4-hydroxy-5-methyl-2-methylene-3(2H)-furanone + NADPH + H+
(2R)-4-hydroxy-2,5-dimethyl-3(2H)-furanone + NADP+
show the reaction diagram
kcat/Km for NADH is 7.5fold lower than for NADPH, Re-specific, i.e. the 4R-hydride of NAD(P)H is transferred
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?
4-hydroxy-5-methyl-2-methylene-3(2H)-furanone + NADPH + H+
4-hydroxy-2,5-dimethyl-3(2H)-furanone + NADP+
show the reaction diagram
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?
9,10-phenanthrenequinone + NADH + H+
? + NAD+
show the reaction diagram
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additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-hydroxy-5-methyl-2-methylene-3(2H)-furanone + NADH + H+
4-hydroxy-2,5-dimethyl-3(2H)-furanone + NAD+
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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cofactor occurs in a mix of both oxidation states
NADPH
preferred cofactor, Re-specific, i.e. the 4R-hydride of NAD(P)H is transferred
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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presence of EDTA induces monomerization
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.82 - 1.13
(2E)-2-butylidene-4-hydroxy-5-methyl-3(2H)-furanone
1.04 - 2.41
(2E)-4-hydroxy-5-methyl-2-propylidene-3(2H)-furanone
1.59 - 2.14
(2E)-ethylidene-4-hydroxy-5-methyl-3(2H)-furanone
0.012
9,10-phenanthrenequinone
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0.1 M Na2HPO4/NaH2PO4, pH 7, 30°C, cofactor NADH
0.361
NADH
0.1 M K2HPO4/KH2PO4, pH 5.0 or 7.0, 30°C
0.325
NADPH
0.1 M K2HPO4/KH2PO4, pH 5.0 or 7.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15 - 1.43
(2E)-2-butylidene-4-hydroxy-5-methyl-3(2H)-furanone
0.34 - 2.69
(2E)-4-hydroxy-5-methyl-2-propylidene-3(2H)-furanone
0.39 - 1.94
(2E)-ethylidene-4-hydroxy-5-methyl-3(2H)-furanone
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.14 - 1.9
(2E)-2-butylidene-4-hydroxy-5-methyl-3(2H)-furanone
0.14 - 2.6
(2E)-4-hydroxy-5-methyl-2-propylidene-3(2H)-furanone
0.25 - 0.9
(2E)-ethylidene-4-hydroxy-5-methyl-3(2H)-furanone
650
9,10-phenanthrenequinone
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0.1 M Na2HPO4/NaH2PO4, pH 7, 30°C, cofactor NADH
20
NADH
0.1 M K2HPO4/KH2PO4, pH 5.0 or 7.0, 30°C
150
NADPH
0.1 M K2HPO4/KH2PO4, pH 5.0 or 7.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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protein contains a calmodulin-binding region
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34300
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x * 37000, SDS-PAGE, x * 34300, calculation from amino acid sequence
37000
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x * 37000, SDS-PAGE, x * 34300, calculation from amino acid sequence
83800
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 37000, SDS-PAGE, x * 34300, calculation from amino acid sequence
dimer
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2 * 42000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallisation in complex with NADPH and 4-hydroxy-2,5-dimethyl-3(2H)-furanone or in complex with NADPH and 4-hydroxy-5-methyl-3(2H)-furanone. The crystal structure of FaEO was solved by molecular replacement using a published X-ray structure of a quinone oxidoreductase from Thermus thermophilus. The structure belongs to the zinc-independent medium chain dehydrogenase/reductase family
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gel filtration, anion exchange chromatography
gel filtration, ion exchange chromatography
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solubilization from membrane using n-dodecyl-beta-D-maltoside or n-octyl-beta-D-glucopyranoside
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli K-12
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
protein may be expressed in different isoforms by alternative gene splicing
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