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Information on EC 1.14.13.24 - 3-hydroxybenzoate 6-monooxygenase and Organism(s) Klebsiella oxytoca and UniProt Accession Q5EXK1

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IUBMB Comments
A flavoprotein (FAD). Acts also on a number of analogues of 3-hydroxybenzoate substituted in the 2, 4, 5 and 6 positions; NADPH can act instead of NADH, but more slowly.
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This record set is specific for:
Klebsiella oxytoca
UNIPROT: Q5EXK1
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Word Map
The taxonomic range for the selected organisms is: Klebsiella oxytoca
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
3-hydroxybenzoate 6-hydroxylase, 3hb6h, 3-hydroxybenzoate-6-hydroxylase, 3-hba-6-hydroxylase, ncgl2923, mnx2p, 3-hydroxybenzoate 6-monooxygenase, m-hydroxybenzoate 6-hydroxylase, 3-hydroxybenzoic acid-6-hydroxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-hydroxybenzoate 6-hydroxylase
-
3-HBA-6-hydroxylase
-
-
-
-
3-hydroxybenzoate 6-hydroxylase
-
-
-
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3-hydroxybenzoic acid-6-hydroxylase
-
-
-
-
m-hydroxybenzoate 6-hydroxylase
-
-
-
-
oxygenase, 3-hydroxybenzoate 6-mono-
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-hydroxybenzoate + NADH + H+ + O2 = 2,5-dihydroxybenzoate + NAD+ + H2O
show the reaction diagram
Arg169 is essential for catalytic activity
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
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reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
3-hydroxybenzoate,NADH:oxygen oxidoreductase (6-hydroxylating)
A flavoprotein (FAD). Acts also on a number of analogues of 3-hydroxybenzoate substituted in the 2, 4, 5 and 6 positions; NADPH can act instead of NADH, but more slowly.
CAS REGISTRY NUMBER
COMMENTARY hide
51570-26-4
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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
3-hydroxybenzoate + NADH + O2
2,5-dihydroxybenzoate + NAD+ + H2O
show the reaction diagram
-
i.e. gentisate
-
?
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
3-hydroxybenzoate + NADH + O2
2,5-dihydroxybenzoate + NAD+ + H2O
show the reaction diagram
-
i.e. gentisate
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.53
recombinant wild-type enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene mhbM
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
3HBH_KLEOX
397
1
43887
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
x * 44000, about, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 44000, about, SDS-PAGE
additional information
Ser166 and Arg169 form the highly conserved SXXR motif important for structure and function of the enzyme
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R169E
site-directed mutagenesis, inactive mutant
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene mhbM, DNA and amino acid sequence determination and analysis, expression of wild-type and mutant enzymes in Escherichia coli strain DH5alpha
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liu, D.Q.; Liu, H.; Gao, X.L.; Leak, D.J.; Zhou, N.Y.
Arg169 is essential for catalytic activity of 3-hydroxybenzoate 6-hydroxylase from Klebsiella pneumoniae M5a1
Microbiol. Res.
160
53-59
2005
Klebsiella oxytoca (Q5EXK1)
Manually annotated by BRENDA team