Any feedback?
Information on EC 1.14.13.9 - kynurenine 3-monooxygenase and Organism(s) Sus scrofa and UniProt Accession Q9MZS9
for references in articles please use BRENDA:EC1.14.13.9Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.14.13.9 kynurenine 3-monooxygenaseIUBMB Comments
A flavoprotein (FAD).
Specify your search results
Word Map
- 1.14.13.9
- mercury
- hg
-
kynurenic
- 3-hydroxykynurenine
-
quinolinic
-
2,3-dioxygenase
- kynureninase
- indoleamine
-
cronbach
- huntington
-
bartlett
-
paint
-
3-hydroxyanthranilic
-
quin
-
neuroactive
-
ochre
-
realgar
-
psychometric
-
calcite
- methylmercury
-
xanthurenic
-
eigenvalue
-
vermilion
-
hematite
-
test-retest
-
excitotoxins
-
ommochrome
-
artwork
-
geochemical
- indoleamine-2,3-dioxygenase
-
archaeological
-
varimax
-
roman
-
mineralogical
-
slovenia
-
micro-raman
- molecular biology
- medicine
- analysis
- pharmacology
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
cinnabar, kmo, kynurenine 3-monooxygenase, kynurenine 3-hydroxylase, kynurenine hydroxylase, kynurenine monooxygenase, kynurenine-3-monooxygenase, pfkmo, kyn-ohase, nadph-dependent flavin monooxygenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
kynurenine 3-hydroxylase
-
-
-
-
kynurenine hydroxylase
-
-
-
-
L-kynurenine-3-hydroxylase
-
-
-
-
oxygenase, kynurenine 3-mono-
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-kynurenine,NADPH:oxygen oxidoreductase (3-hydroxylating)
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY
9029-61-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-kynurenine + NADPH + H+ + O2
3-hydroxy-L-kynurenine + NADP+ + H2O
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the C terminus of the enzyme contains a putative outer mitochondrial membrane-targeting sequence and this portion of the molecule is required enzyme function
the C-terminal region functions as a mitochondrial targeting signal
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
KMO is downregulated in autografts and is almost completely silenced in allograft rejection
physiological function
kynurenine 3-monooxygenase (KMO) and kynureninase are reduced in ischemia-reperfusion procedure and further decreased in rejection allografts among mismatched pig KTx, molecular mechanism, overview. TEC injury in acutely rejection allografts is associated with alterations of Bcl2 family proteins, reduction of tight junction protein 1 (TJP1), and TEC-specific KMO. Three cytokines, IFNgamma, TNFalpha, and IL1beta, are identified as triggers of TEC injury by altering the expression of Bcl2, BID, and TJP1. Allograft rejection and TEC injury are always associated with a dramatic reduction of KMO. 3-Hydroxy-L-kynurenine (3HK) and hydroxyl-3 anthranilic acid (3HAA) as direct and downstream products of KMO, effectively protect TEC from injury via increasing expression of Bcl-xL and TJP1. 3HK and 3HAA effectively inhibit T cell proliferation
additional information
additional information
the C-terminal region of pig liver KMO plays a dual role. First, it is required for the enzymatic activity. Second, it functions as a mitochondrial targeting signal
additional information
-
the C-terminal region of pig liver KMO plays a dual role. First, it is required for the enzymatic activity. Second, it functions as a mitochondrial targeting signal
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). KMO_PIG
471
2
53998
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the C-terminal region is required for the enzymatic activity and functions as a mitochondrial targeting signal
additional information
-
the C-terminal region is required for the enzymatic activity and functions as a mitochondrial targeting signal
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of C-terminal truncation mutants KMODELTAC10, KMODELTAC20, KMODELTAC30, KMODELTAC50, and KMODELTAC70, that are all localized in the cytosol after recombinant expression in COS-7 cells, exept for KMODELTAC10. Two forms of C-terminal truncation, KMODELTAC10D and KMODELTAC20D retain almost full activity but KMODELTAC30D shows 1.6fold higher activity than the wild-type. The activities of KMODELTAC50 and KMODELTAC70 is highly reduced, overview. The quantity of expressed KMODELTA30D in COS-7 cellsis 1.3fold higher than the wild-type KMO
additional information
-
construction of C-terminal truncation mutants KMODELTAC10, KMODELTAC20, KMODELTAC30, KMODELTAC50, and KMODELTAC70, that are all localized in the cytosol after recombinant expression in COS-7 cells, exept for KMODELTAC10. Two forms of C-terminal truncation, KMODELTAC10D and KMODELTAC20D retain almost full activity but KMODELTAC30D shows 1.6fold higher activity than the wild-type. The activities of KMODELTAC50 and KMODELTAC70 is highly reduced, overview. The quantity of expressed KMODELTA30D in COS-7 cellsis 1.3fold higher than the wild-type KMO
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determnination and analysis, sequence comparisons, expression of FLAG-tagged wild-type enzyme and of C-terminal truncation mutants in COS-7 cells. The FLAG tag directs the wild-type enzyme to mitochondria but also to the cytosol and the plasma mambrane, overview
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
KMO is downregulated in autografts and is almost completely silenced in allograft rejection
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Uemura, T.; Hirai, K.
Purification of L-kynurenine 3-monooxygenase from mitochondrial outer membrane of pig liver
Adv. Exp. Med. Biol.
467
619-623
1999
Sus scrofa
Hirai, K.; Kuroyanagi, H.; Tatebayashi, Y.; Hayashi, Y.; Hirabayashi-Takahashi, K.; Saito, K.; Haga, S.; Uemura, T.; Izumi, S.
Dual role of the carboxyl-terminal region of pig liver L-kynurenine 3-monooxygenase: mitochondrial-targeting signal and enzymatic activity
J. Biochem.
148
639-650
2010
Sus scrofa (Q9MZS9), Sus scrofa
Smith, J.R.; Jamie, J.F.; Guillemin, G.J.
Kynurenine-3-monooxygenase a review of structure, mechanism, and inhibitors
Drug Discov. Today
21
315-324
2016
Homo sapiens (O15229), Rattus norvegicus (O88867), Pseudomonas fluorescens (Q84HF5), Sus scrofa (Q9MZS9)
EXTERNAL LINKS (specific for EC-Number 1.14.13.9)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
