Information on EC 1.14.99.2 - kynurenine 7,8-hydroxylase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)
Please login to have access to the AMENDA and FRENDA data

The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
1.14.99.2
-
top print hide
RECOMMENDED NAME
GeneOntology No.
kynurenine 7,8-hydroxylase
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
kynurenate + AH2 + O2 = 7,8-dihydro-7,8-dihydroxykynurenate + A
show the reaction diagram
-
-
-
-
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
top print hide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Tryptophan metabolism
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
kynurenate,hydrogen-donor:oxygen oxidoreductase (hydroxylating)
-
top
top print hide
CAS REGISTRY NUMBER
COMMENTARY hide
9029-63-4
-
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATCC 11299b
-
-
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
top print hide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
kynurenate + NADH + O2
7,8-dihydro-7,8-dihydroxykynurenate + NAD+
show the reaction diagram
kynurenate + NADPH + O2
7,8-dihydro-7,8-dihydroxykynurenate + NADP+
show the reaction diagram
top print hide
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
kynurenate + NADH + O2
7,8-dihydro-7,8-dihydroxykynurenate + NAD+
show the reaction diagram
kynurenate + NADPH + O2
7,8-dihydro-7,8-dihydroxykynurenate + NADP+
show the reaction diagram
top print hide
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
top print hide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetate
-
inhibition reversed by addition of GSH or cysteine
Kynurenate
-
competitive inhibition at 0.2 mM
p-chloromercuribenzoate
-
inhibition reversed by addition of GSH or cysteine
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.008
Kynurenate
-
-
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
-
stable in presence 10 mM cysteine
390584
top print hide
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
5 min, complete inactivation
top print hide
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol stabilizes activity
-
cysteine stabilizes activity
-
GSH stabilizes activity
-
precipitation of supernatant with ammonium sulfate in the absence of cysteine, complete loss of activity
-
thioglycolate stabilizes activity
-
top print hide
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10°C, ammonium sulfate fractions, loss of activity after a few days
-
-10°C, supernatant after high speed centrifugation of crude extract, several months, no loss in activity
-
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
top
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 1.14.99.2)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)