KEGG   ENZYME: 1.14.11.61
Entry
EC 1.14.11.61               Enzyme                                 

Name
feruloyl-CoA 6-hydroxylase
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
Sysname
feruloyl-CoA,2-oxoglutarate:oxygen oxidoreductase (6-hydroxylating)
Reaction(IUBMB)
trans-feruloyl-CoA + 2-oxoglutarate + O2 = trans-6-hydroxyferuloyl-CoA + succinate + CO2 [RN:R11549]
Reaction(KEGG)
R11549
Substrate
trans-feruloyl-CoA [CPD:C00406];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007]
Product
6-hydroxyferuloyl-CoA [CPD:C21459];
succinate [CPD:C00042];
CO2 [CPD:C00011]
Comment
Requires iron(II) and ascorbate. The product spontaneously undergoes trans-cis isomerization and lactonization to form scopoletin, liberating CoA in the process. The enzymes from the plants Ruta graveolens and Ipomoea batatas also act on trans-4-coumaroyl-CoA. cf. EC 1.14.11.62, trans-4-coumaroyl-CoA 2-hydroxylase.
History
EC 1.14.11.61 created 2019
Pathway
ec00940  Phenylpropanoid biosynthesis
ec01110  Biosynthesis of secondary metabolites
Orthology
K06892  feruloyl-CoA 6-hydroxylase
K23378  feruloyl-CoA 6-hydroxylase / trans-4-coumaroyl-CoA 2-hydroxylase
Genes
ATH: AT1G55290 AT3G13610
ALY: 9318972 9321041
CRB: 17893417
CSAT: 104742969 104745611 104765146 104778096
EUS: EUTSA_v10021003mg
BRP: 103842722 103859525 103870109
BNA: 106345852 106351698 106387021 106395905 106440607 106452295
BOE: 106326584 106334207 106343388
RSZ: 108805589 108807602 108856971 108860815
THJ: 104810332 104811207 104822670
CPAP: 110809597
VRA: 106773844
VAR: 108347270
LJA: Lj3g3v0652730.1(Lj3g3v0652730.1) Lj6g3v1007880.2(Lj6g3v1007880.2)
ADU: 107472881
LANG: 109363590
FVE: 101291326
PPER: 18772442
MDM: 103423180
PXB: 103937496
CSV: 101214138
MCHA: 111021233
SIND: 105170982
BVG: 104889861
NNU: 104612098
 » show all
Reference
1  [PMID:18547395]
  Authors
Kai K, Mizutani M, Kawamura N, Yamamoto R, Tamai M, Yamaguchi H, Sakata K, Shimizu B
  Title
Scopoletin is biosynthesized via ortho-hydroxylation of feruloyl CoA by a 2-oxoglutarate-dependent dioxygenase in Arabidopsis thaliana.
  Journal
Plant J 55:989-99 (2008)
DOI:10.1111/j.1365-313X.2008.03568.x
  Sequence
Reference
2  [PMID:19004461]
  Authors
Bayoumi SA, Rowan MG, Blagbrough IS, Beeching JR
  Title
Biosynthesis of scopoletin and scopolin in cassava roots during post-harvest physiological deterioration: the E-Z-isomerisation stage.
  Journal
Phytochemistry 69:2928-36 (2008)
DOI:10.1016/j.phytochem.2008.09.023
Reference
3  [PMID:22168819]
  Authors
Vialart G, Hehn A, Olry A, Ito K, Krieger C, Larbat R, Paris C, Shimizu B, Sugimoto Y, Mizutani M, Bourgaud F
  Title
A 2-oxoglutarate-dependent dioxygenase from Ruta graveolens L. exhibits p-coumaroyl CoA 2'-hydroxylase activity (C2'H): a missing step in the synthesis of umbelliferone in plants.
  Journal
Plant J 70:460-70 (2012)
DOI:10.1111/j.1365-313X.2011.04879.x
Reference
4  [PMID:22169019]
  Authors
Matsumoto S, Mizutani M, Sakata K, Shimizu B
  Title
Molecular cloning and functional analysis of the ortho-hydroxylases of p-coumaroyl coenzyme A/feruloyl coenzyme A involved in formation of umbelliferone and scopoletin in sweet potato, Ipomoea batatas (L.) Lam.
  Journal
Phytochemistry 74:49-57 (2012)
DOI:10.1016/j.phytochem.2011.11.009
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.14.11.61
IUBMB Enzyme Nomenclature: 1.14.11.61
ExPASy - ENZYME nomenclature database: 1.14.11.61
BRENDA, the Enzyme Database: 1.14.11.61
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