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Information on EC 1.14.14.9 - 4-hydroxyphenylacetate 3-monooxygenase and Organism(s) Geobacillus sp. and UniProt Accession Q4L1M7

for references in articles please use BRENDA:EC1.14.14.9
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EC Tree
IUBMB Comments
The enzyme from Escherichia coli attacks a broad spectrum of phenolic compounds. The enzyme uses FADH2 as a substrate rather than a cofactor . FADH2 is provided by EC 1.5.1.36, flavin reductase (NADH) [5,6].
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This record set is specific for:
Geobacillus sp.
UNIPROT: Q4L1M7
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Word Map
The taxonomic range for the selected organisms is: Geobacillus sp.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
hpabc, 4-hydroxyphenylacetate 3-hydroxylase, p-hydroxyphenylacetate 3-hydroxylase, p-hydroxyphenylacetate hydroxylase, 4-hpa hydroxylase, 4-hydroxyphenylacetate 3-monooxygenase, 4-hydroxyphenylacetic acid 3-hydroxylase, 4hpa3h, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4-HPA hydroxylase
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4 HPA 3-hydroxyylase
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4-hydroxyphenylacetate 3-hydroxylase
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4-hydroxyphenylacetic acid 3-hydroxylase
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p-hydroxyphenylacetate 3-hydroxylase
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p-hydroxyphenylacetate hydroxylase
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p-hydroxyphenylacetic 3-hydroxylase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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hydroxylation
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxyphenylacetate,FAD:oxygen oxidoreductase (3-hydroxylating)
The enzyme from Escherichia coli attacks a broad spectrum of phenolic compounds. The enzyme uses FADH2 as a substrate rather than a cofactor [4]. FADH2 is provided by EC 1.5.1.36, flavin reductase (NADH) [5,6].
CAS REGISTRY NUMBER
COMMENTARY hide
37256-71-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-hydroxyphenylacetate + NADH + H+ + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-hydroxyphenylacetate + NADH + H+ + O2
3,4-dihydroxyphenylacetate + NAD+ + H2O
show the reaction diagram
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene hpaH
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56000
x * 56269, sequence calculation, x * 56000, recombinant enzyme, SDS-PAGE
56269
x * 56269, sequence calculation, x * 56000, recombinant enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 56269, sequence calculation, x * 56000, recombinant enzyme, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain DH5alpha by affinity chromatography on a 4-hydroxyphenylacetate-coupled amino-agarose column to near homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene hpaH, DNA and amino acid sequence determination and analysis, sequence comparisons, expression in enzyme-deficient Escherichia coli strain DH5alpha
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hawumba, J.F.; Broezel, V.S.; Theron, J.
Cloning and characterization of a 4-hydroxyphenylacetate 3-hydroxylase from the thermophile Geobacillus sp. PA-9
Curr. Microbiol.
55
480-484
2007
Geobacillus sp. (Q4L1M7), Geobacillus sp. PA-9 (Q4L1M7)
Manually annotated by BRENDA team