Sequence of I23O1_HUMAN

EC Number:1.13.11.52

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
indoleamine 2,3-dioxygenase
P14902
Homo sapiens
403
45326
Reaction
L-tryptophan + O2 = N-formyl-L-kynurenine
Other sequences found for EC No. 1.13.11.52

EC Number:1.13.11.11

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
tryptophan 2,3-dioxygenase
P14902
Homo sapiens
403
45326
Reaction
L-tryptophan + O2 = N-formyl-L-kynurenine
Other sequences found for EC No. 1.13.11.11

EC Number:1.13.11.42

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
indoleamine-pyrrole 2,3-dioxygenase
P14902
Homo sapiens
403
45326
Reaction
Other sequences found for EC No. 1.13.11.42

General information:

Sequence
show sequence in fasta format
  0 MAHAMENSWT ISKEYHIDEE VGFALPNPQE NLPDFYNDWM FIAKHLPDLI ESGQLRERVE
 60 KLNMLSIDHL TDHKSQRLAR LVLGCITMAY VWGKGHGDVR KVLPRNIAVP YCQLSKKLEL
120 PPILVYADCV LANWKKKDPN KPLTYENMDV LFSFRDGDCS KGFFLVSLLV EIAAASAIKV
180 IPTVFKAMQM QERDTLLKAL LEIASCLEKA LQVFHQIHDH VNPKAFFSVL RIYLSGWKGN
240 PQLSDGLVYE GFWEDPKEFA GGSAGQSSVF QCFDVLLGIQ QTAGGGHAAQ FLQDMRRYMP
300 PAHRNFLCSL ESNPSVREFV LSKGDAGLRE AYDACVKALV SLRSYHLQIV TKYILIPASQ
360 QPKENKTSED PSKLEAKGTG GTDLMNFLKT VRSTTEKSLL KEG
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
299410
Dai W.,Gupta S.L.
Molecular cloning, sequencing and expression of human interferon-gamma-inducible indoleamine 2,3-dioxygenase cDNA.
Biochem. Biophys. Res. Commun.
168
1-8
1990
299411
Tone S.,Takikawa O.,Habara-Ohkubo A.,Kadoya A.,Yoshida R.,Kido R.
Primary structure of human indoleamine 2,3-dioxygenase deduced from the nucleotide sequence of its cDNA.
Nucleic Acids Res.
18
367-367
1990
299412
Kadoya A.,Tone S.,Maeda H.,Minatogawa Y.,Kido R.
Gene structure of human indoleamine 2,3-dioxygenase.
Biochem. Biophys. Res. Commun.
189
530-536
1992
299415
Ota T.,Suzuki Y.,Nishikawa T.,Otsuki T.,Sugiyama T.,Irie R.,Wakamatsu A.,Hayashi K.,Sato H.,Nagai K.,Kimura K.,Makita H.,Sekine M.,Obayashi M.,Nishi T.,Shibahara T.,Tanaka T.,Ishii S.,Yamamoto J.,Saito K.,Kawai Y.,Isono Y.,Nakamura Y.,Nagahari K.,Murakami K.,Yasuda T.,Iwayanagi T.,Wagatsuma M.,Shiratori A.,Sudo H.,Hosoiri T.,Kaku Y.,Kodaira H.,Kondo H.,Sugawara M.,Takahashi M.,Kanda K.,Yokoi T.,Furuya T.,Kikkawa E.,Omura Y.,Abe K.,Kamihara K.,Katsuta N.,Sato K.,Tanikawa M.,Yamazaki M.,Ninomiya K.,Ishibashi T.,Yamashita H.,Murakawa K.,Fujimori K.,Tanai H.,Kimata M.,Watanabe M.,Hiraoka S.,Chiba Y.,Ishida S.,Ono Y.,Takiguchi S.,Watanabe S.,Yosida M.,Hotuta T.,Kusano J.,Kanehori K.,Takahashi-Fujii A.,Hara H.,Tanase T.-O.,Nomura Y.,Togiya S.,Komai F.,Hara R.,Takeuchi K.,Arita M.,Imose N.,Musashino K.,Yuuki H.,Oshima A.,Sasaki N.,Aotsuka S.,Yoshikawa Y.,Matsunawa H.,Ichihara T.,Shiohata N.,Sano S.,Moriya S.,Momiyama H.,Satoh N.,Takami S.,Terashima Y.,Suzuki O.,Nakagawa S.,Senoh A.,Mizoguchi H.,Goto Y.,Shimizu F.,Wakebe H.,Hishigaki H.,Watanabe T.,Sugiyama A.,Takemoto M.,Kawakami B.,Yamazaki M.,Watanabe K.,Kumagai A.,Itakura S.,Fukuzumi Y.,Fujimori Y.,Komiyama M.,Tashiro H.,Tanigami A.,Fujiwara T.,Ono T.,Yamada K.,Fujii Y.,Ozaki K.,Hirao M.,Ohmori Y.,Kawabata A.,Hikiji T.,Kobatake N.,Inagaki H.,Ikema Y.,Okamoto S.,Okitani R.,Kawakami T.,Noguchi S.,Itoh T.,Shigeta K.,Senba T.,Matsumura K.,Nakajima Y.,Mizuno T.,Morinaga M.,Sasaki M.,Togashi T.,Oyama M.,Hata H.,Watanabe M.,Komatsu T.,Mizushima-Sugano J.,Satoh T.,Shirai Y.,Takahashi Y.,Nakagawa K.,Okumura K.,Nagase T.,Nomura N.,Kikuchi H.,Masuho Y.,Yamashita R.,Nakai K.,Yada T.,Nakamura Y.,Ohara O.,Isogai T.,Sugano S.
Complete sequencing and characterization of 21,243 full-length human cDNAs.
Nat. Genet.
36
40-45
2004
299416
Nusbaum C.,Mikkelsen T.S.,Zody M.C.,Asakawa S.,Taudien S.,Garber M.,Kodira C.D.,Schueler M.G.,Shimizu A.,Whittaker C.A.,Chang J.L.,Cuomo C.A.,Dewar K.,FitzGerald M.G.,Yang X.,Allen N.R.,Anderson S.,Asakawa T.,Blechschmidt K.,Bloom T.,Borowsky M.L.,Butler J.,Cook A.,Corum B.,DeArellano K.,DeCaprio D.,Dooley K.T.,Dorris L. III,Engels R.,Gloeckner G.,Hafez N.,Hagopian D.S.,Hall J.L.,Ishikawa S.K.,Jaffe D.B.,Kamat A.,Kudoh J.,Lehmann R.,Lokitsang T.,Macdonald P.,Major J.E.,Matthews C.D.,Mauceli E.,Menzel U.,Mihalev A.H.,Minoshima S.,Murayama Y.,Naylor J.W.,Nicol R.,Nguyen C.,O'Leary S.B.,O'Neill K.,Parker S.C.J.,Polley A.,Raymond C.K.,Reichwald K.,Rodriguez J.,Sasaki T.,Schilhabel M.,Siddiqui R.,Smith C.L.,Sneddon T.P.,Talamas J.A.,Tenzin P.,Topham K.,Venkataraman V.,Wen G.,Yamazaki S.,Young S.K.,Zeng Q.,Zimmer A.R.,Rosenthal A.,Birren B.W.,Platzer M.,Shimizu N.,Lander E.S.
DNA sequence and analysis of human chromosome 8.
Nature
439
331-335
2006
299417
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
299418
Taylor M.W.,Feng G.S.
Relationship between interferon-gamma, indoleamine 2,3-dioxygenase, and tryptophan catabolism.
FASEB J.
5
2516-2522
1991
299419
Uyttenhove C.,Pilotte L.,Theate I.,Stroobant V.,Colau D.,Parmentier N.,Boon T.,Van den Eynde B.J.
Evidence for a tumoral immune resistance mechanism based on tryptophan degradation by indoleamine 2,3-dioxygenase.
Nat. Med.
9
1269-1274
2003
299420
Vottero E.,Mitchell D.A.,Page M.J.,MacGillivray R.T.,Sadowski I.J.,Roberge M.,Mauk A.G.
Cytochrome b(5) is a major reductant in vivo of human indoleamine 2,3-dioxygenase expressed in yeast.
FEBS Lett.
580
2265-2268
2006
299421
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
299422
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
299423
Loeb S.,Koenigsrainer A.,Zieker D.,Bruecher B.L.,Rammensee H.G.,Opelz G.,Terness P.
IDO1 and IDO2 are expressed in human tumors: levo- but not dextro-1-methyl tryptophan inhibits tryptophan catabolism.
Cancer Immunol. Immunother.
58
153-157
2009
299424
Lee Y.K.,Lee H.B.,Shin D.M.,Kang M.J.,Yi E.C.,Noh S.,Lee J.,Lee C.,Min C.K.,Choi E.Y.
Heme-binding-mediated negative regulation of the tryptophan metabolic enzyme indoleamine 2,3-dioxygenase 1 (IDO1) by IDO2.
Exp. Mol. Med.
46
0-0
2014
299425
Yuasa H.J.,Mizuno K.,Ball H.J.
Low efficiency IDO2 enzymes are conserved in lower vertebrates, whereas higher efficiency IDO1 enzymes are dispensable.
FEBS J.
282
2735-2745
2015
299426
Vigneron N.,van Baren N.,Van den Eynde B.J.
Expression profile of the human IDO1 protein, a cancer drug target involved in tumoral immune resistance.
OncoImmunology
4
0-0
2015
299427
Munn D.H.,Mellor A.L.
Indoleamine 2,3 dioxygenase and metabolic control of immune responses.
Trends Immunol.
34
137-143
2013
299428
Schmidt S.V.,Schultze J.L.
New insights into IDO biology in bacterial and viral infections.
Front. Immunol.
5
384-384
2014
299429
van Baren N.,Van den Eynde B.J.
Tryptophan-degrading enzymes in tumoral immune resistance.
Front. Immunol.
6
34-34
2015
299430
Roehrig U.F.,Majjigapu S.R.,Vogel P.,Zoete V.,Michielin O.
Challenges in the discovery of indoleamine 2,3-dioxygenase 1 (IDO1) inhibitors.
J. Med. Chem.
58
9421-9437
2015
299431
Sugimoto H.,Oda S.,Otsuki T.,Hino T.,Yoshida T.,Shiro Y.
Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase.
Proc. Natl. Acad. Sci. U.S.A.
103
2611-2616
2006
299432
Tojo S.,Kohno T.,Tanaka T.,Kamioka S.,Ota Y.,Ishii T.,Kamimoto K.,Asano S.,Isobe Y.
Crystal structures and structure-activity relationships of imidazothiazole derivatives as IDO1 inhibitors.
ACS Med. Chem. Lett.
5
1119-1123
2014