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Information on EC 1.14.11.60 - scopoletin 8-hydroxylase
for references in articles please use BRENDA:EC1.14.11.60
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
1.14.11.60 scopoletin 8-hydroxylase
IUBMB Comments
Requires iron(II) and ascorbate. A protein involved in biosynthesis of iron(III)-chelating coumarins in higher plants.
The enzyme appears in viruses and cellular organisms
showSynonyms
at3g12900, scopoletin 8-hydroxylase, at3g12900 protein, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
At3g12900
At3g12900 protein
S8H
S8H
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
scopoletin + 2-oxoglutarate + O2 = fraxetin + succinate + CO2
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
scopoletin,2-oxoglutarate:oxygen oxidoreductase (8-hydroxylating)
Requires iron(II) and ascorbate. A protein involved in biosynthesis of iron(III)-chelating coumarins in higher plants.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
isoscopoletin + 2-oxoglutarate + O2
fraxetin + succinate + CO2
Substrates: 55% conversion
Products: -
Products: -
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scopoletin + 2-oxoglutarate + O2
fraxetin + succinate + CO2
Substrates: -
Products: -
Products: -
?
scopoletin + 2-oxoglutarate + O2
fraxetin + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
scopoletin + 2-oxoglutarate + O2
fraxetin + succinate + CO2
Substrates: the enzyme is involved in biosynthesis of iron(III)-chelating coumarins in higher plants
Products: -
Products: -
?
scopoletin + 2-oxoglutarate + O2
fraxetin + succinate + CO2
Substrates: the enzyme is involved in coumarin biosynthesis and iron-deficiency responses in Arabidopsis
Products: -
Products: -
?
scopoletin + 2-oxoglutarate + O2
fraxetin + succinate + CO2
Substrates: the enzyme participates in Fe acquisition by mediating the biosynthesis of fraxetin (7,8-dihydroxy-6-methoxycoumarin), a coumarin derived from the scopoletin pathway
Products: -
Products: -
?
scopoletin + 2-oxoglutarate + O2
fraxetin + succinate + CO2
Substrates: 84.8% conversion
Products: -
Products: -
?
scopoletin + 2-oxoglutarate + O2
fraxetin + succinate + CO2
Substrates: -
Products: -
Products: -
?
scopoletin + 2-oxoglutarate + O2
fraxetin + succinate + CO2
Substrates: the enzyme is involved in coumarin biosynthesis and iron-deficiency responses in Arabidopsis
Products: -
Products: -
?
scopoletin + 2-oxoglutarate + O2
fraxetin + succinate + CO2
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: esculetin, and scoparone
Products: -
Products: -
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additional information
?
-
-
Substrates: no substrates: esculetin, isoscopoletin, and scoparone
Products: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
scopoletin + 2-oxoglutarate + O2
fraxetin + succinate + CO2
Substrates: the enzyme is involved in biosynthesis of iron(III)-chelating coumarins in higher plants
Products: -
Products: -
?
scopoletin + 2-oxoglutarate + O2
fraxetin + succinate + CO2
Substrates: the enzyme is involved in coumarin biosynthesis and iron-deficiency responses in Arabidopsis
Products: -
Products: -
?
scopoletin + 2-oxoglutarate + O2
fraxetin + succinate + CO2
Substrates: the enzyme participates in Fe acquisition by mediating the biosynthesis of fraxetin (7,8-dihydroxy-6-methoxycoumarin), a coumarin derived from the scopoletin pathway
Products: -
Products: -
?
scopoletin + 2-oxoglutarate + O2
fraxetin + succinate + CO2
Substrates: the enzyme is involved in coumarin biosynthesis and iron-deficiency responses in Arabidopsis
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe2+
concentrations above 0.05 mM significantly reduce the enzyme activity, leading to decreased fraxetin synthesis
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expressed most strongly in the root epidermal layer under iron-deficient conditions
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
mutants defective in the expression of S8H show increased sensitivity to growth on pH 7.0 media supplemented with an immobile source of Fe and reduced secretion of fraxetin. Transgenic lines overexpressing S8H exhibit an opposite phenotype. Supplementing the media containing immobile Fe with fraxetin partially rescues the s8h mutants
metabolism
physiological function
the enzyme participates in Fe acquisition by mediating the biosynthesis of fraxetin (7,8-dihydroxy-6-methoxycoumarin), a coumarin derived from the scopoletin pathway. Fraxetin secretion is a decisive factor for calcicole-calcifuge behavior (i.e. the ability/inability to thrive on alkaline soils) of plants
metabolism
the enzyme is involved in biosynthesis of iron(III)-chelating coumarins in higher plants. Under iron-deficiency conditions, a branch of the phenylpropanoid pathway consisting of feruloyl-CoA 6'-hydroxylase 1, scopoletin 8-hydroxylase, and CYP82C4 is strongly induced, thus leading to the synthesis of scopoletin and its conversion into redox-active fraxetin and sideretin. In the rhizosphere, the redox-active coumarins act in concert with other components of the strategy I iron acquisition machinery by solubilizing and reducing iron from sparingly available sources
metabolism
the enzyme is involved in coumarin biosynthesis and is part of mechanisms used by plants to assimilate iron
metabolism
the enzyme participates in Fe acquisition by mediating the biosynthesis of fraxetin (7,8-dihydroxy-6-methoxycoumarin), a coumarin derived from the scopoletin pathway. Fraxetin secretion is a decisive factor for calcicole-calcifuge behavior (i.e. the ability/inability to thrive on alkaline soils) of plants
metabolism
-
the enzyme is involved in coumarin biosynthesis and is part of mechanisms used by plants to assimilate iron
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). S8H_ARATH
357
0
39716
Swiss-Prot
other Location (Reliability: 3)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis of fraxetin by three distinct routes, from ferulic acid, esculetin, and scopoletin. An Escherichia coli strain harboring S8H synthesizes 84.8 microM fraxetin from 100 microM scopoletin. The other two approaches lead to less than half of this amount
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ectopic expression of the peptides IRONMAN (IMA1 and IMA2)leads to increased expression of MYB72 and scopoletin 8-hydrxylase. The response is strictly dependent on elevated environmental pH
iron-deficiency-dependent upregulation. The iron-deficiency-dependent upregulation is mainly confined to roots
the enzyme is highly induced in roots of Fe-deficient plants both at the transcript and protein levels
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
ectopic expression of the peptides IRONMAN (IMA1 and IMA2) improves growth on calcareous soil by inducing biosynthesis and secretion of the catecholic coumarin 7,8-dihydroxy-6-methoxycoumarin (fraxetin) via increased expression of MYB72 and scopoletin 8-hydrxylase. The response is strictly dependent on elevated environmental pH
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Siwinska, J.; Siatkowska, K.; Olry, A.; Grosjean, J.; Hehn, A.; Bourgaud, F.; Meharg, A.A.; Carey, M.; Lojkowska, E.; Ihnatowicz, A.
Scopoletin 8-hydroxylase a novel enzyme involved in coumarin biosynthesis and iron-deficiency responses in Arabidopsis
J. Exp. Bot.
69
1735-1748
2018
Arabidopsis thaliana (Q9LE86), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q9LE86)
brenda
Rajniak, J.; Giehl, R.; Chang, E.; Murgia, I.; Von Wiren, N.; Sattely, E.
Biosynthesis of redox-active metabolites in response to iron deficiency in plants
Nat. Chem. Biol.
14
442-450
2018
Arabidopsis thaliana (Q9LE86)
brenda
Tsai, H.H.; Rodriguez-Celma, J.; Lan, P.; Wu, Y.C.; Velez-Bermudez, I.C.; Schmidt, W.
Scopoletin 8-hydroxylase-mediated fraxetin production is crucial for iron mobilization
Plant Physiol.
177
194-207
2018
Arabidopsis thaliana (Q9LE86), Arabidopsis thaliana
brenda
An, S.; Choi, G.; Ahn, J.
Biosynthesis of fraxetin from three different substrates using engineered Escherichia coli
Appl. Biol. Chem.
63
55
2020
Oryza sativa, Arabidopsis thaliana (Q9LE86)
-
brenda
Gautam, C.K.; Tsai, H.H.; Schmidt, W.
IRONMAN tunes responses to iron deficiency in concert with environmental pH
Plant Physiol.
187
1728-1745
2021
Arabidopsis thaliana (Q9LE86)
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.11.60)
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Release 2023.1 (January 2023)
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