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Information on EC 1.13.11.11 - tryptophan 2,3-dioxygenase and Organism(s) Xanthomonas campestris pv. campestris and UniProt Accession Q8PDA8

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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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Xanthomonas campestris pv. campestris
UNIPROT: Q8PDA8
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The taxonomic range for the selected organisms is: Xanthomonas campestris pv. campestris
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
5-fluoro-L-tryptophan + O2
5-fluoro-N-formyl-L-kynurenine
show the reaction diagram
-
-
-
?
indole-3-pyruvic acid + O2
?
show the reaction diagram
-
-
-
?
L-tryptophan + O2
N-formyl-L-kynurenine
show the reaction diagram
-
-
-
?
additional information
?
-
no activity witth D-Trp. No evidence for the accumulation of Compound II during TDO catalysis, instead a ternary [Fe(II)-O2, L-Trp] complex is detected under steady state conditions. Absence of a Compound II species in the steady state in TDO is not due to an intrinsic inability of the TDO enzyme to form ferryl heme, because Compound II can be formed directly through a different route in which ferrous heme is reacted with peroxide
-
-
?
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
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
ferryl heme, formation of ferrous-oxy TDO
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
stopped-flow, pre-steady-state, and steady-state kinetics
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
indoleamine 2,3-dioxygenase (IDO, EC 1.13.11.52) and tryptophan 2,3-dioxygenase (TDO) are heme-containing enzymes that catalyze the O2-dependent oxidation of L-tryptophan (L-Trp) in biological systems following different reaction mechanisms, the rate-limiting step in the IDO and TDO mechanisms is not the same
additional information
no evidence for the accumulation of Compound II during TDO catalysis, instead a ternary [Fe(II)-O2, L-Trp] complex is detected under steady state conditions. Absence of a Compound II species in the steady state in TDO is not due to an intrinsic inability of the TDO enzyme to form ferryl heme, because Compound II can be formed directly through a different route in which ferrous heme is reacted with peroxide
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme in complex with L-kynurenine
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene kynA, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Basran, J.; Booth, E.S.; Lee, M.; Handa, S.; Raven, E.L.
Analysis of reaction intermediates in tryptophan 2,3-dioxygenase a comparison with indoleamine 2,3-dioxygenase
Biochemistry
55
6743-6750
2016
Homo sapiens (P48775), Xanthomonas campestris pv. campestris (Q8PDA8), Xanthomonas campestris pv. campestris ATCC 33913 (Q8PDA8)
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
Basran, J.; Booth, E.S.; Campbell, L.P.; Thackray, S.J.; Jesani, M.H.; Clayden, J.; Moody, P.C.E.; Mowat, C.G.; Kwon, H.; Raven, E.L.
Binding of L-kynurenine to X. campestris tryptophan 2,3-dioxygenase
J. Inorg. Biochem.
225
111604
2021
Xanthomonas campestris, Xanthomonas campestris pv. campestris (Q8PDA8), Xanthomonas campestris pv. campestris ATCC 33913 (Q8PDA8)
Manually annotated by BRENDA team