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Sequence of I23O1_HUMAN

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

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
D-tryptophan + O2 = N-formyl-D-kynurenine
Other sequences found for EC No. 1.13.11.52

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
430149
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
430150
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
430151
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
430154
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
430155
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
430156
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
430157
Taylor M.W.,Feng G.S.
Relationship between interferon-gamma, indoleamine 2,3-dioxygenase, and tryptophan catabolism.
FASEB J.
5
2516-2522
1991
430158
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
430159
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
430160
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
430161
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
430162
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
430163
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
430164
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
430165
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
430166
Munn D.H.,Mellor A.L.
Indoleamine 2,3 dioxygenase and metabolic control of immune responses.
Trends Immunol.
34
137-143
2013
430167
Schmidt S.V.,Schultze J.L.
New insights into IDO biology in bacterial and viral infections.
Front. Immunol.
5
384-384
2014
430168
van Baren N.,Van den Eynde B.J.
Tryptophan-degrading enzymes in tumoral immune resistance.
Front. Immunol.
6
34-34
2015
430169
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
430170
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
430171
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