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Information on EC 1.14.13.2 - 4-hydroxybenzoate 3-monooxygenase and Organism(s) Comamonas testosteroni and UniProt Accession Q6SSJ6

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EC Tree
IUBMB Comments
A flavoprotein (FAD). Most enzymes from Pseudomonas are highly specific for NADPH (cf. EC 1.14.13.33 4-hydroxybenzoate 3-monooxygenase [NAD(P)H]).
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This record set is specific for:
Comamonas testosteroni
UNIPROT: Q6SSJ6
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The taxonomic range for the selected organisms is: Comamonas testosteroni
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
p-hydroxybenzoate hydroxylase, para-hydroxybenzoate hydroxylase, 4-hydroxybenzoate hydroxylase, 4-hydroxybenzoate 3-monooxygenase, 4-hydroxybenzoate 3-hydroxylase, m-hydroxybenzoate hydroxylase, 4-hba 3-hydroxylase, phbad, 4hba 3-hydroxylase, 4-hba 3-monooxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
m-hydroxybenzoate hydroxylase
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4-HBA-3-hydroxylase
-
-
-
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4-hydroxybenzoate 3-hydroxylase
-
-
-
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4-hydroxybenzoate 3-monooxygenase
-
-
-
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4-hydroxybenzoate monooxygenase
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-
-
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4-hydroxybenzoic hydroxylase
-
-
-
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oxygenase, 4-hydroxybenzoate 3-mono-
-
-
-
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p-hydroxybenzoate hydroxylase
-
-
-
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p-hydroxybenzoate-3-hydroxylase
-
-
-
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p-hydroxybenzoic acid hydrolase
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-
-
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p-hydroxybenzoic acid hydroxylase
-
-
-
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p-hydroxybenzoic hydroxylase
-
-
-
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para-hydroxybenzoate hydroxylase
-
-
-
-
PHBAD
-
-
-
-
PHBH
-
-
-
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PHBHase
-
-
-
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POHBase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
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reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
4-hydroxybenzoate,NADPH:oxygen oxidoreductase (3-hydroxylating)
A flavoprotein (FAD). Most enzymes from Pseudomonas are highly specific for NADPH (cf. EC 1.14.13.33 4-hydroxybenzoate 3-monooxygenase [NAD(P)H]).
CAS REGISTRY NUMBER
COMMENTARY hide
9059-23-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
?
2,5-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
?
3,4-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
?
3,5-dihydroxybenzoate + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
?
3-chlorophenol + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
?
3-hydroxyanthranilate + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
?
4-chlorophenol + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
?
4-chlororesorcinol + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
?
4-nitrophenol + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
?
hydroquinone + NADPH + H+ + O2
? + NADP+ + H2O
show the reaction diagram
-
-
-
?
m-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
show the reaction diagram
-
-
-
?
p-hydroxybenzoate + NADPH + O2
? + NADP+ + H2O
show the reaction diagram
is transformed to a lesser extent than m-hydroxybenzoate
-
-
?
4-hydroxybenzoate + NADPH + O2
?
show the reaction diagram
-
high degree of homology observed between the enzyme from Comamonas and of Pseudomonas and Acinetobacter indicates the common evolutionary origin of the enzyme in the divergent pathways of 4-hydroxybenzoate among these soil bacteria of different genera
-
-
?
4-hydroxybenzoate + NADPH + O2
protocatechuate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
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is not capable of hydroxylating benzoate, o-hydroxybenzoate (salicylate), 2,4-dihydroxybenzoate, 2,6-dihydroxybenzoate, 2-chlorophenol, 3-aminophenol, 4-methoxybenzoate, 3-toluate, o-cresol, m-cresol, or p-cresol
-
-
?
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-hydroxybenzoate + NADPH + O2
?
show the reaction diagram
-
high degree of homology observed between the enzyme from Comamonas and of Pseudomonas and Acinetobacter indicates the common evolutionary origin of the enzyme in the divergent pathways of 4-hydroxybenzoate among these soil bacteria of different genera
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetamide
-
reversed by dithiothreitol
N-iodosuccinimide
-
reversed by dithiothreitol
o-Iodosobenzoate
-
reversed by dithiothreitol
p-hydroxy-3-iodomethylbenzoate
-
1 mM, irreversible crosslinking to the substrate binding site
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MOBA_COMTE
639
0
70489
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
71000
-
x * 71000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 71000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A16T/S394P/D416A
low ability to hydroxylate 3-aminophenol
A400G
transforms 3-aminophenol with efficiency almost like mutant A400G/K429R
A400G/K429R
among mutants, highest enzymatic activity to hydroxylate 3-aminophenol
H135P
H135P/I217L/Y304H
low ability to hydroxylate 3-aminophenol
K326I
lacks the ability to transform phenol to catechol as the wild-type
K429R
can not transform 3-aminophenol at all
N102T/I259S/V399M
low ability to hydroxylate 3-aminophenol
N227H
is not able to transform 3-aminophenol
N227H/D416A
almost has the same transformation efficiency as mutant N227H/Q292R/D416A
N227H/Q292R/D416A
among mutants, highest enzymatic activity to hydroxylate 3-aminophenol
Q292R
is not able to transform 3-aminophenol
R152L/F364V
low ability to hydroxylate 3-aminophenol
V257A
mutation enables the mutant to transform phenol to catechol, also has enhanced ability to transform resorcinol, hydroquinone, p-hydroxybenzoate, 2,5-dihydroxybenzoate, 3,4-dihydroxybenzoate, 3-chlorophenol, 4-chlorophenol, 4-chlororesorcinol, and 4-nitrophenol, thus broadens the substrate range. Is not capable of hydroxylating benzoate, o-hydroxybenzoate (salicylate), 2,4-dihydroxybenzoate, 2,6-dihydroxybenzoate, 2-chlorophenol, 3-aminophenol, 4-methoxybenzoate, 3-toluate, o-cresol, m-cresol, or p-cresol as the wild-type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
mobA gene from pSEB2 cloned into pZR80. Random mutations introduced into the mobA gene and cloned into pCR2.1-TOPO and transformed into Escherichia coli Top10
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, R.; Scott, R.Jr.; Tsugita, A.; Hosokawa, K.
Purification and characterization of p-hydroxybenzoate 3-hydroxylase from Comamonas testosteroni
Res. Commun. Biochem. Cell Mol. Biol.
1
51-60
1997
Acinetobacter sp., Comamonas testosteroni, Pseudomonas sp., Comamonas testosteroni Kh 122-3S
-
Manually annotated by BRENDA team
Chen, R.; Oki, H.; Scott, R.P.; Yamaguchi, H.; Kusunoki, M.; Matsuura, Y.; Chaen, H.; Tsugita, A.; Hosokawa, K.
Crystallization and further characterization of meta-hydroxybenzoate 4-hydroxylase from Comamonas testosteroni
Res. Commun. Biochem. Cell Mol. Biol.
2
253-274
1998
Comamonas testosteroni
-
Manually annotated by BRENDA team
Chang, H.K.; Zylstra, G.J.
Examination and expansion of the substrate range of m-hydroxybenzoate hydroxylase
Biochem. Biophys. Res. Commun.
371
149-153
2008
Comamonas testosteroni (Q6SSJ6), Comamonas testosteroni GZ39 (Q6SSJ6), Comamonas testosteroni GZ39
Manually annotated by BRENDA team