Information on EC 1.3.99.16 - Isoquinoline 1-oxidoreductase

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The expected taxonomic range for this enzyme is: Brevundimonas diminuta

EC NUMBER
COMMENTARY hide
1.3.99.16
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RECOMMENDED NAME
GeneOntology No.
Isoquinoline 1-oxidoreductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Isoquinoline + acceptor + H2O = isoquinolin-1(2H)-one + reduced acceptor
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
Isoquinoline:acceptor 1-oxidoreductase (hydroxylating)
The enzyme from Pseudomonas diminuta is specific towards N-containing N-heterocyclic substrates, including isoquinoline, isoquinolin-5-ol, phthalazine and quinazoline. Electron acceptors include 1,2-benzoquinone, cytochrome c, ferricyanide, iodonitrotetrazolium chloride, nitroblue tetrazolium, Meldola blue and phenazine methosulfate.
CAS REGISTRY NUMBER
COMMENTARY hide
155948-73-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-hydroxyisoquinoline + acceptor + H2O
1,5-dihydroisoquinoline + reduced acceptor
show the reaction diagram
isoquinoline + acceptor + H2O
1-oxo-1,2-dihydroisoquinoline + reduced acceptor
show the reaction diagram
isoquinoline + acceptor + H2O
1-oxoisoquinoline + reduced acceptor
show the reaction diagram
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acceptor: ferricyanide, 1,4-benzoquinone, cytochrome c, 2,6-dichloroindophenol,2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyl-tetrazolium chloride, phenazine methosulfate, thionine, nitroblue tetrazolium, Meldola's blue
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Isoquinoline + acceptor + H2O
?
show the reaction diagram
phthalazine + acceptor + H2O
1-oxophthalazine + reduced acceptor
show the reaction diagram
quinazoline + acceptor + H2O
4-hydroxyquinazoline + reduced acceptor
show the reaction diagram
quinazoline + acceptor + H2O
4-oxoquinazoline + reduced acceptor
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Isoquinoline + acceptor + H2O
?
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iron-sulfur centre
two distinct 2Fe-2S clusters
molybdopterin cytosine dinucleotide
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Pterin molybdenum cofactor
additional information
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enzyme contains no FAD
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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two (2Fe+2S) clusters
Iron
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enzyme contains 3.95 g-atom of iron per mol of enzyme. The iron and the acid-labile sulfur are arranged in two (2Fe-2S) clusters
Mo
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enzyme contains 0.85 g-atom of molybdenum per mol of enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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5-Hydroxyisoquinoline
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rapid and very effective inactivation in presence as well as in absence of the electron acceptors iodonitrotetrazolium chloride, phenazine methosulfate or ferricyanide
Isoquinoline
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slow inhibition in absence of an electron acceptor
p-hydroxymercuribenzoate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.34
2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyl-tetrazolium chloride
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with isoquinoline as cosubstrate
0.016
Isoquinoline
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with 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyl-tetrazolium chloride as cosubstrate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16000
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1 * 80000 + 1 * 16000, SDS-PAGE
16399
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1 * 16399 + 1 * 84429, calculation from nucleotide sequence
80000
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1 * 80000 + 1 * 16000, SDS-PAGE
84429
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1 * 16399 + 1 * 84429, calculation from nucleotide sequence
93000 - 95000
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gel filtration, analytical ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by the hanging-drop vapour-diffusion method, using two different crystallization buffers, streak-seeding and cross-linking are essential to obtain well diffracting crystals
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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5 min, rapid decrease of activity above
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by two cation-exchange chromatography steps, applying Triton X-100 overcomes retention problems of IOR in the first cation-exchange chromatography step
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including Triton X-100 in a precipitation step
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
comparative sequence analysis of the iorA and iorB genes
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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