Any feedback?
Information on EC 1.14.13.63 - 3-hydroxyphenylacetate 6-hydroxylase
for references in articles please use BRENDA:EC1.14.13.63Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.14.13.63 3-hydroxyphenylacetate 6-hydroxylaseIUBMB Comments
3-hydroxyphenylacetate 6-hydroxylase from Flavobacterium sp. is highly specific for 3-hydroxyphenylacetate and uses NADH and NADPH as electron donors with similar efficiency.
Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
3-hydroxyphenylacetate 6-hydroxylase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3,4-dihydroxyphenylacetate 6-hydroxylase
3-Hydroxyphenylacetate 6-monooxygenase
-
-
-
-
CYP504B
m-Hydroxyphenylacetate 6-hydroxylase
-
-
-
-
Oxygenase, 3-hydroxyphenylacetate 6-mono
-
-
-
-
additional information
additional information
the enzyme is a member of a the CYP450 subfamily
additional information
the enzyme is a member of a the CYP450 subfamily
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-hydroxyphenylacetate + NAD(P)H + H+ + O2 = 2,5-dihydroxyphenylacetate + NAD(P)+ + H2O
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
3-hydroxyphenylacetate,NAD(P)H:oxygen oxidoreductase (6-hydroxylating)
3-hydroxyphenylacetate 6-hydroxylase from Flavobacterium sp. is highly specific for 3-hydroxyphenylacetate and uses NADH and NADPH as electron donors with similar efficiency.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
114705-01-0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,4-dihydroxyphenylacetate + NAD(P)H + O2 + H+
2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O
3-Hydroxyphenylacetate + NAD(P)H + O2
?
-
enzyme in the 3-hydroxyphenylacetate catabolism
-
-
?
4-Hydroxyphenylacetate + NADH + O2
2,4-Dihydroxyphenylacetate + NAD+
-
-
-
?
2-hydroxyphenoxyacetate + NADH + O2
?
-
20% of the activity with 3-hydroxyphenylacetate
-
-
?
2-hydroxyphenoxyacetate + NADH + O2
?
-
20% of the activity with 3-hydroxyphenylacetate
-
-
?
2-hydroxyphenylacetate + NAD(P)H + O2
2,5-dihydroxyphenylacetate + NAD(P)+ + H2O
low activity
-
-
?
2-hydroxyphenylacetate + NAD(P)H + O2
2,5-dihydroxyphenylacetate + NAD(P)+ + H2O
low activity, step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview
-
-
?
2-hydroxyphenylacetate + NAD(P)H + O2
2,5-dihydroxyphenylacetate + NAD(P)+ + H2O
low activity
-
-
?
2-hydroxyphenylacetate + NAD(P)H + O2
2,5-dihydroxyphenylacetate + NAD(P)+ + H2O
low activity, step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview
-
-
?
3,4-dihydroxyphenylacetate + NAD(P)H + O2
2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O
-
-
-
?
3,4-dihydroxyphenylacetate + NAD(P)H + O2
2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O
step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview
the product is a substrate for homogentisate dioxygenase
-
?
3,4-dihydroxyphenylacetate + NAD(P)H + O2
2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O
-
-
-
?
3,4-dihydroxyphenylacetate + NAD(P)H + O2
2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O
step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview
the product is a substrate for homogentisate dioxygenase
-
?
3,4-dihydroxyphenylacetate + NAD(P)H + O2 + H+
2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O
-
-
-
?
3,4-dihydroxyphenylacetate + NAD(P)H + O2 + H+
2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O
-
-
-
?
3,4-Dihydroxyphenylacetate + NADH + O2
2,4,5-Trihydroxyphenylacetate + NAD+
-
-
-
?
3,4-Dihydroxyphenylacetate + NADH + O2
2,4,5-Trihydroxyphenylacetate + NAD+
-
-
-
?
3-hydroxyphenylacetate + NAD(P)H + O2
2,5-dihydroxyphenylacetate + NAD(P)+ + H2O
-
-
-
?
3-hydroxyphenylacetate + NAD(P)H + O2
2,5-dihydroxyphenylacetate + NAD(P)+ + H2O
step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview
the product is a substrate for homogentisate dioxygenase
-
?
3-hydroxyphenylacetate + NAD(P)H + O2
2,5-dihydroxyphenylacetate + NAD(P)+ + H2O
-
-
-
?
3-Hydroxyphenylacetate + NADH + O2
2,5-Dihydroxyphenylacetate + NAD+
-
NADPH and NADH are oxidized at a comparable rate
-
?
3-Hydroxyphenylacetate + NADH + O2
2,5-Dihydroxyphenylacetate + NAD+
-
NADPH and NADH are oxidized at a comparable rate
-
?
3-Hydroxyphenylacetate + NADH + O2
2,5-Dihydroxyphenylacetate + NAD+
-
-
-
-
?
3-Hydroxyphenylacetate + NADH + O2
2,5-Dihydroxyphenylacetate + NAD+
-
enables growth on 3-hydroxyphenylacetate as sole carbon source
-
-
?
3-Hydroxyphenylacetate + NADH + O2
2,5-Dihydroxyphenylacetate + NAD+
-
-
-
-
?
3-Hydroxyphenylacetate + NADH + O2
2,5-Dihydroxyphenylacetate + NAD+
-
enables growth on 3-hydroxyphenylacetate as sole carbon source
-
-
?
3-Hydroxyphenylacetate + NADPH + O2
2,5-Dihydroxyphenylacetate + NADP+
-
NADPH and NADH are oxidized at a comparable rate
-
?
3-Hydroxyphenylacetate + NADPH + O2
2,5-Dihydroxyphenylacetate + NADP+
-
NADPH and NADH are oxidized at a comparable rate
-
?
additional information
?
-
-
in the absence of oxygen the free enzyme is slowly reduced by NADPH or NADH
-
-
?
additional information
?
-
-
in the absence of oxygen the free enzyme is slowly reduced by NADPH or NADH
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-hydroxyphenylacetate + NAD(P)H + O2
2,5-dihydroxyphenylacetate + NAD(P)+ + H2O
step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview
the product is a substrate for homogentisate dioxygenase
-
?
3-Hydroxyphenylacetate + NAD(P)H + O2
?
-
enzyme in the 3-hydroxyphenylacetate catabolism
-
-
?
2-hydroxyphenylacetate + NAD(P)H + O2
2,5-dihydroxyphenylacetate + NAD(P)+ + H2O
low activity, step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview
-
-
?
2-hydroxyphenylacetate + NAD(P)H + O2
2,5-dihydroxyphenylacetate + NAD(P)+ + H2O
low activity, step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview
-
-
?
3,4-dihydroxyphenylacetate + NAD(P)H + O2
2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O
step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview
the product is a substrate for homogentisate dioxygenase
-
?
3,4-dihydroxyphenylacetate + NAD(P)H + O2
2,4,5-trihydroxyphenylacetate + NAD(P)+ + H2O
step in the 2,5-dihydroxyphenylacetate, i.e.homogentisic acid, catabolic pathway, overview
the product is a substrate for homogentisate dioxygenase
-
?
3-Hydroxyphenylacetate + NADH + O2
2,5-Dihydroxyphenylacetate + NAD+
-
enables growth on 3-hydroxyphenylacetate as sole carbon source
-
-
?
3-Hydroxyphenylacetate + NADH + O2
2,5-Dihydroxyphenylacetate + NAD+
-
enables growth on 3-hydroxyphenylacetate as sole carbon source
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
the enzyme is a cytochrome P450 monooxygenase containing a heme iron
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
phenylacetate and its hydroxyderivatives strongly induce the enzyme
-
additional information
-
phenylacetate and its hydroxyderivatives strongly induce the enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
highest enzyme activity when grown on 3-hydroxyphenylacetate
-
-
brenda
highest enzyme activity when grown on 3-hydroxyphenylacetate
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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). PHACB_EMEND
517
0
58096
Swiss-Prot
other Location (Reliability: 4)
A0A8J8WGC7_9EURO
551
0
61969
TrEMBL
Mitochondrion (Reliability: 4)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
a phacB-disrupted strain DELTAphacB does not grow on 3-hydroxy-, 4-hydroxy-, or 3,4-dihydroxy-phenylacetate, overview
additional information
-
a phacB-disrupted strain DELTAphacB does not grow on 3-hydroxy-, 4-hydroxy-, or 3,4-dihydroxy-phenylacetate, overview
additional information
-
a phacB-disrupted strain DELTAphacB does not grow on 3-hydroxy-, 4-hydroxy-, or 3,4-dihydroxy-phenylacetate, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression pattern, sequence comparison, expression in a recombinant Aspergillus nidulans strain
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
1.8fold higher expression in ochratoxin A producer strain compared to the non-producer strain
1.8fold higher expression in ochratoxin A producer strain compared to the non-producer strain
1.8fold higher expression in ochratoxin A producer strain compared to the non-producer strain
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
van Berkel, W.J.H.; van den Tweel, W.J.J.
Purification and characterisation of 3-hydroxyphenylacetate 6-hydroxylase: a novel FAD-dependent monooxygenase from a Flavobacterium species
Eur. J. Biochem.
201
585-591
1991
Flavobacterium sp., Flavobacterium sp. JS-7
brenda
Van den Tweel, W.J.J.; Smits, J.P.; de Bont, J.A.M.
Catabolism of DL-alpha-phenylhydracrylic, phenylacetic and 3- and 4-hydroxyphenylacetic acid via homogentisic acid in a Flavobacterium sp.
Arch. Microbiol.
149
207-213
1988
Flavobacterium sp.
-
brenda
Suemori, A.; Nakajima, K.; Kurane, R.; Nakamura, Y.
Purification and characterization of o-hydroxyphenylacetate 5-hydroxylase, m-hydroxyphenylacetate 6-hydroxylase and p-hydroxyphenylacetate 1-hydroxylase from Rhodococcus erythropolis
J. Ferment. Bioeng.
81
133-137
1996
Rhodococcus erythropolis, Rhodococcus erythropolis S1
-
brenda
Ferrer-Sevillano, F.; Fernandez-Canon, J.M.
Novel phacB-encoded cytochrome P450 monooxygenase from Aspergillus nidulans with 3-hydroxyphenylacetate 6-hydroxylase and 3,4-dihydroxyphenylacetate 6-hydroxylase activities
Eukaryot. Cell
6
514-520
2007
Aspergillus nidulans (Q078T0), Aspergillus nidulans, Aspergillus nidulans BiA1 (Q078T0)
brenda
Sartori, D.; Massi, F.P.; Ferranti, L.S.; Fungaro, M.H.
Identification of genes differentially expressed between Ochratoxin-producing and non-producing strains of Aspergillus westerdijkiae
Indian J. Microbiol.
54
41-45
2014
Aspergillus westerdijkiae (E2EB14), Aspergillus westerdijkiae UEL91 (E2EB14)
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.14.13.63)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
