Sequence of I23O2_MOUSE
EC Number:1.13.11.52
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
D-tryptophan + O2 = N-formyl-D-kynurenine
Other sequences found for EC No. 1.13.11.52
General information:
Sequence
0 MEPQSQSMTL EVPLSLGRYH ISEEYGFLLP NPLEALPDHY KPWMEIALRL PHLIENRQLR
60 AHVYRMPLLD CRFLKSYREQ RLAHMALAAI TMGFVWQEGE GQPQKVLPRS LAIPFVEVSR
120 NLGLPPILVH SDLVLTNWTK RNPEGPLEIS NLETIISFPG GESLRGFILV TVLVEKAAVP
180 GLKALVQGME AIRQHSQDTL LEALQQLRLS IQDITRALAQ MHDYVDPDIF YSVIRIFLSG
240 WKDNPAMPVG LVYEGVATEP LKYSGGSAAQ SSVLHAFDEF LGIEHCKESV GFLHRMRDYM
300 PPSHKAFLED LHVAPSLRDY ILASGPGDCL MAYNQCVEAL GELRSYHINV VARYIISAAT
360 RARSRGLTNP SPHALEDRGT GGTAMLSFLK SVREKTMEAL LCPGA
Download this sequence
in fasta formatDownload all sequences for 1.13.11.52
in fasta format
in csv (Excel, OpenOffice) formatSequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
430191
Ball H.J.,Sanchez-Perez A.,Weiser S.,Austin C.J.D.,Astelbauer F.,Miu J.,McQuillan J.A.,Stocker R.,Jermiin L.S.,Hunt N.H.
Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice.
Gene
396
203-213
2007
430192
Church D.M.,Goodstadt L.,Hillier L.W.,Zody M.C.,Goldstein S.,She X.,Bult C.J.,Agarwala R.,Cherry J.L.,DiCuccio M.,Hlavina W.,Kapustin Y.,Meric P.,Maglott D.,Birtle Z.,Marques A.C.,Graves T.,Zhou S.,Teague B.,Potamousis K.,Churas C.,Place M.,Herschleb J.,Runnheim R.,Forrest D.,Amos-Landgraf J.,Schwartz D.C.,Cheng Z.,Lindblad-Toh K.,Eichler E.E.,Ponting C.P.
Lineage-specific biology revealed by a finished genome assembly of the mouse.
PLoS Biol.
7
0-0
2009
430194
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
430195
Yuasa H.J.,Takubo M.,Takahashi A.,Hasegawa T.,Noma H.,Suzuki T.
Evolution of vertebrate indoleamine 2,3-dioxygenases.
J. Mol. Evol.
65
705-714
2007
430196
Metz R.,Duhadaway J.B.,Kamasani U.,Laury-Kleintop L.,Muller A.J.,Prendergast G.C.
Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan.
Cancer Res.
67
7082-7087
2007
430197
Huttlin E.L.,Jedrychowski M.P.,Elias J.E.,Goswami T.,Rad R.,Beausoleil S.A.,Villen J.,Haas W.,Sowa M.E.,Gygi S.P.
A tissue-specific atlas of mouse protein phosphorylation and expression.
Cell
143
1174-1189
2010
430198
Metz R.,Smith C.,DuHadaway J.B.,Chandler P.,Baban B.,Merlo L.M.,Pigott E.,Keough M.P.,Rust S.,Mellor A.L.,Mandik-Nayak L.,Muller A.J.,Prendergast G.C.
IDO2 is critical for IDO1-mediated T-cell regulation and exerts a non-redundant function in inflammation.
Int. Immunol.
26
357-367
2014
430199
Prendergast G.C.,Metz R.,Muller A.J.,Merlo L.M.,Mandik-Nayak L.
IDO2 in immunomodulation and autoimmune disease.
Front. Immunol.
5
585-585
2014
430200
van Baren N.,Van den Eynde B.J.
Tryptophan-degrading enzymes in tumoral immune resistance.
Front. Immunol.
6
34-34
2015
