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Information on EC 1.13.11.11 - tryptophan 2,3-dioxygenase and Organism(s) Rattus norvegicus and UniProt Accession P21643

for references in articles please use BRENDA:EC1.13.11.11
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IUBMB Comments
A protohemoprotein. In mammals, the enzyme appears to be located only in the liver. This enzyme, together with EC 1.13.11.52, indoleamine 2,3-dioxygenase, catalyses the first and rate-limiting step in the kynurenine pathway, the major pathway of tryptophan metabolism . The enzyme is specific for tryptophan as substrate, but is far more active with L-tryptophan than with D-tryptophan .
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Rattus norvegicus
UNIPROT: P21643
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
tryptophan 2,3-dioxygenase, indoleamine 2,3-dioxygenase 1, ido-1, tryptophan-2,3-dioxygenase, indoleamine 2,3-dioxygenase 2, ido-2, tryptophan 2,3-dioxygenase 2, xctdo, l-tryptophan:oxygen 2,3-oxidoreductase (decyclizing), more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tryptophan 2,3-dioxygenase 2
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-tryptophan:oxygen 2,3-oxidoreductase (decyclizing)
A protohemoprotein. In mammals, the enzyme appears to be located only in the liver. This enzyme, together with EC 1.13.11.52, indoleamine 2,3-dioxygenase, catalyses the first and rate-limiting step in the kynurenine pathway, the major pathway of tryptophan metabolism [5]. The enzyme is specific for tryptophan as substrate, but is far more active with L-tryptophan than with D-tryptophan [2].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
?
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
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.221
L-tryptophan
pH 7.0, 37°C
additional information
additional information
Michaelis-Menten kinetics
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
immune cells express high amount of the enzyme (TDO2) at the peak stage of adjuvant-induced arthritis
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) enzymes have independently evolved to catalyze the first step in the catabolism of tryptophan (L-Trp) through the kynurenine pathway. Enzyme TDO is found in almost all metazoan and many bacterial species, but not in fungi, distribution of IDO/TDO genes among invertebrates, overview
malfunction
pharmacological inhibition or knockdown of the enzyme (TDO2) in adjuvant-induced arthritis-fibroblast-like synoviocytes results in a reduced proliferation, secretion, migration and invasion
physiological function
the enzyme plays a key role in regulating the activation of fibroblast-like synoviocytes in autoimmune arthritis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
T23O_RAT
406
0
47857
Swiss-Prot
other Location (Reliability: 2)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene TDO, DNA and amino acid sequence determination and analysis, sequence and genetic structure comparisons, and phylogenetic analysis, functional complementation of the enzyme-deficient Saccharomyces cerevisiae
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is strongly increased in synovial tissue and fibroblast-like synoviocytes of rheumatoid arthritis and adjuvant-induced arthritis. Immune cells express high amount of the enzyme (TDO2) at the peak stage of adjuvant-induced arthritis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yuasa, H.J.; Ball, H.J.
Efficient tryptophan-catabolizing activity is consistently conserved through evolution of TDO enzymes, but not IDO enzymes
J. Exp. Zool. B
324
128-140
2015
Branchiostoma floridae (C3XXE6), Caenorhabditis elegans (Q09474), Drosophila melanogaster (P20351), Homo sapiens (P48775), Monosiga brevicollis (A9V766), Nematostella vectensis (A7RFF0), no activity in Brugia malayi, no activity in Saccharomyces cerevisiae, no activity in Schistosoma mansoni, Rattus norvegicus (P21643), Strongylocentrotus purpuratus
Manually annotated by BRENDA team
Chang, Y.; Han, P.; Wang, Y.; Jia, C.; Zhang, B.; Zhao, Y.; Li, S.; Li, S.; Wang, X.; Yang, X.; Wei, W.
Tryptophan 2,3-dioxygenase 2 plays a key role in regulating the activation of fibroblast-like synoviocytes in autoimmune arthritis
Br. J. Pharmacol.
179
3024-3042
2022
Rattus norvegicus (P21643), Homo sapiens (P48775)
Manually annotated by BRENDA team