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Information on EC 1.13.11.11 - tryptophan 2,3-dioxygenase and Organism(s) Mus musculus and UniProt Accession P48776

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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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Mus musculus
UNIPROT: P48776
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The taxonomic range for the selected organisms is: Mus musculus
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
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
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
low activity
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
the enzyme has broad substrate specificity for various indoleamines such as L-tryptophan and serotonin. It catalyzes the oxidation of the pyrrole ring of tryptophan to form N-formylkynurenine, which is later metabolized to formic acid and kynurenine
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additional information
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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
D-tryptophan + O2
N-formyl-D-kynurenine
show the reaction diagram
low activity
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
?
additional information
?
-
in mouse liver homogenate, TDO activity is five times lower for D-Trp than that for L-Trp. L-Trp is the preferred substrate for nicotinamide synthesis because L-Trp metabolism is more efficient than D-Trp in mice
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heme
heme-containing enzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
expression on brain occurs in different cells as macrophages, microglia, neurons and astrocytes
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
TDO knockout mice require a minimum of 0.06% dietary L-Trp, which value is about 2 mg/d/mouse
metabolism
comparison of contribution percentage of tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) to the conversion of L-tryptophan, the calculated percentage conversions indicats that TDO and IDO oxidize 70% and 30%, respectively, of the dietary L-tryptophan. The amount of D-Trp converted to nicotinamide via indole-3-pyruvic acid (IPA) is very low, this amount of D-Trp is converted to L-Trp, which is primarily used for protein synthesis rather than catabolism via the Kyn biosynthesis pathway in mice
physiological function
the enzyme is involved in nicotinamide biosynthesis. Comparison of contribution percentage of tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) to the conversion of L-tryptophan, the calculated percentage conversions indicats that TDO and IDO oxidize 70% and 30%, respectively, of the dietary L-tryptophan. The amount of D-Trp converted to nicotinamide via indole-3-pyruvic acid (IPA) is very low, this amount of D-Trp is converted to L-Trp, which is primarily used for protein synthesis rather than catabolism via the Kyn biosynthesis pathway in mice
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
T23O_MOUSE
406
0
47756
Swiss-Prot
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
construction of TDO-knockout mice, phenotype, overview. The amount of D-Trp converted to nicotinamide via indole-3-pyruvic acid (IPA) is very low
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maeta, A.; Sano, M.; Fukuwatari, T.; Funakoshi, H.; Nakamura, T.; Shibata, K.
Contributions of tryptophan 2,3-dioxygenase and indoleamine 2,3-dioxygenase to the conversion of D-tryptophan to nicotinamide analyzed by using tryptophan 2,3-dioxygenase-knockout mice
Biosci. Biotechnol. Biochem.
78
878-881
2014
Mus musculus (P48776), Mus musculus C57BL/6 (P48776)
Manually annotated by BRENDA team
Gonzalez Esquivel, D.; Ramirez-Ortega, D.; Pineda, B.; Castro, N.; Rios, C.; Perez de la Cruz, V.
Kynurenine pathway metabolites and enzymes involved in redox reactions
Neuropharmacology
112
331-345
2017
Homo sapiens (P14902), Homo sapiens (P48775), Homo sapiens (Q6ZQW0), Mus musculus (P28776), Xanthomonas campestris pv. campestris (Q8PDA8), Xanthomonas campestris pv. campestris ATCC 33913 (Q8PDA8)
Manually annotated by BRENDA team