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Information on EC 1.14.15.B3 - berberine 11-hydroxylase
for references in articles please use BRENDA:EC1.14.15.B3
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preliminary BRENDA-supplied EC number
EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
1.14.15.B3 berberine 11-hydroxylase
The expected taxonomic range for this enzyme is: Burkholderia sp. CJ1
Synonyms
BBR 11-hydroxylase, berberine 11-hydroxylase oxygenase, BrhA, multicomponent BBR 11-hydroxylase, PAL 11-hydroxylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
berberine 11-hydroxylase oxygenase
A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
UniProt
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SYSTEMATIC NAME
IUBMB Comments
alkaloid,reduced-ferredoxin:oxygen oxidoreductase (11beta-hydroxylating)
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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
9-O-ethylberberine + 2 reduced ferredoxin + O2 + 2 H+
11-hydroxy-9-O-ethylberberine + 2 oxidized ferredoxin + H2O
A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
Substrates: -
Products: -
Products: -
?
9-O-isopropylberberine + 2 reduced ferredoxin + O2 + 2 H+
11-hydroxy-9-O-isopropylberberine + 2 oxidized ferredoxin + H2O
A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
Substrates: lower activity
Products: -
Products: -
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9-O-propylberberine + 2 reduced ferredoxin + O2 + 2 H+
11-hydroxy-9-O-propylberberine + 2 oxidized ferredoxin + H2O
A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
Substrates: lower activity
Products: -
Products: -
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berberine + 2 reduced ferredoxin + O2 + 2 H+
11-hydroxyberberine + 2 oxidized ferredoxin + H2O
A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
Substrates: -
Products: -
Products: -
?
palmatine + 2 reduced ferredoxin + O2 + 2 H+
11-hydroxypalmatine + 2 oxidized ferredoxin + H2O
additional information
?
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A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
Substrates: in vitro reconsititution of the functional BrhA, BrhB, and BrhC combined enzyme
Products: -
Products: -
?
palmatine + 2 reduced ferredoxin + O2 + 2 H+
11-hydroxypalmatine + 2 oxidized ferredoxin + H2O
A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
Substrates: -
Products: -
Products: -
?
palmatine + 2 reduced ferredoxin + O2 + 2 H+
11-hydroxypalmatine + 2 oxidized ferredoxin + H2O
A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
Substrates: best substrate
Products: -
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
berberine + 2 reduced ferredoxin + O2 + 2 H+
11-hydroxyberberine + 2 oxidized ferredoxin + H2O
A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
Substrates: -
Products: -
Products: -
?
palmatine + 2 reduced ferredoxin + O2 + 2 H+
11-hydroxypalmatine + 2 oxidized ferredoxin + H2O
A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
Substrates: -
Products: -
Products: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ferredoxin
A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
contains a Rieske non-heme [2Fe-2S] domain with the consensus sequence Cys-X-X-X-X-X-Cys-X-X-Cys-(inserted 36 or 37 of any amino acid, X)-Cys (CX5CX2CX36/37C)
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additional information
A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
the enzyme is a Rieske non-heme iron oxygenase (RO) requiring ferredoxin (Fd) and ferredoxin reductase (FdR) cofactors as electron transport chain (ETC) components, they are encoded by genes brhB (UniProt ID A0A5H2YIA2) and brhC (UniProt ID A0A5H2YFF1), respectively, in Burkholderia strain CJ1. No significant difference in BBR hydroxylation activity is observed when comparing between NADH- and NADPH-containing reactions in the presence of all 3 enzyme (BrhA, BrhB, and BrhC). The production of H-BBR is observed only in the presence of the 3-enzyme mixture supplemented with both NAD(P)H and Fe2+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
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
encoded by genes brhA, brhB, and brhC, encoding the oxygenase, reductase, and ferredoxin components of the berberine 11-hydroxylase
A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
UniProt
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
evolution
A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
BrhA is belonging to the Rieske non-heme iron oxygenase (RO) family, a class of enzymes known to catalyze the first step in bacterial aromatic ring hydroxylation of alkaloid protoberberine
metabolism
A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
existence of two distinct pathways for the bacterial metabolism of berberine (BBR), whhich are demethylenation via demethyleneberberine (D-BBR) and 11-hydroxylation via 11-hydroxyberberine (H-BBR)
physiological function
A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
berberine (BBR) is a protoberberine alkaloid extracted from plants such as Coptis japonica (Ranunculaceae). Existence of an 11-hydroxylation pathway employed by BBR-utilizing bacteria living on the plants for metabolism of BBR. BrhA belongs to the Rieske non-heme iron oxygenase (RO) family catalyzing the first step in bacterial aromatic ring hydroxylation of alkaloid protoberberine. BrhA activity requires BrhB (ferredoxin reductase) and BrhC (ferredoxin) as electron transport chain components. BrhA shows hydroxylation activity for BBR and derivatives that possess a protoberberine skeleton
additional information
A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
the enzyme is a Rieske non-heme iron oxygenase (RO) requiring ferredoxin (Fd) and ferredoxin reductase (FdR) cofactors as electron transport chain (ETC) components, they are encoded by genes brhB (UniProt ID A0A5H2YIA2) and brhC (UniProt ID A0A5H2YFF1), respectively, in Burkholderia strain CJ1. The production of H-BBR is observed only in the presence of the 3-enzyme mixture supplemented with both NAD(P)H and Fe2+
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
brhA complementation experiment is performed by constructing a CJ1DELTA7340/pJB7340 strain, in which a plasmid carrying brhA is introduced into the DELTA7340 mutant. A control strain (CJ1DELTA7340/pJB861) is generated by introducing the empty vector (pJB861) into the same background. The loss of BBR hydroxylation activity reflects the brhA gene defect
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene brhA-brhC, DNA and amino acid sequence determination and analysis using a BD3100 transposon mutant library generated by random mutagenesis of the BD3100 genome with the EZ-Tn5 transposon, screening for mutants with 11-hydroxylation ability. Genes brhA, brhB, and brhC are encoding a multicomponent BBR 11-hydroxylase in Burkholderia sp. strain CJ1
A0A5H2YUI4; A0A5H2YIA2; A0A5H2YFF1
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoshida, H.; Takeda, H.; Wakana, D.; Sato, F.; Hosoe, T.
Identification of a multi-component berberine 11-hydroxylase from Burkholderia sp. strain CJ1
Biosci. Biotechnol. Biochem.
84
1274-1284
2020
Burkholderia sp. CJ1 (A0A5H2YUI4 AND A0A5H2YIA2 AND A0A5H2YFF1)
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Release 2026.1 (March 2026)
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