Sequence of I23O2_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
Q6ZQW0
Homo sapiens
420
47075
Reaction
L-tryptophan + O2 = N-formyl-L-kynurenine
Other sequences found for EC No. 1.13.11.11

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
Q6ZQW0
Homo sapiens
420
47075
Reaction
L-tryptophan + O2 = N-formyl-L-kynurenine
Other sequences found for EC No. 1.13.11.52

General information:

Sequence
show sequence in fasta format
  0 MLHFHYYDTS NKIMEPHRPN VKTAVPLSLE SYHISEEYGF LLPDSLKELP DHYRPWMEIA
 60 NKLPQLIDAH QLQAHVDKMP LLSCQFLKGH REQRLAHLVL SFLTMGYVWQ EGEAQPAEVL
120 PRNLALPFVE VSRNLGLPPI LVHSDLVLTN WTKKDPDGFL EIGNLETIIS FPGGESLHGF
180 ILVTALVEKE AVPGIKALVQ ATNAILQPNQ EALLQALQRL RLSIQDITKT LGQMHDYVDP
240 DIFYAGIRIF LSGWKDNPAM PAGLMYEGVS QEPLKYSGGS AAQSTVLHAF DEFLGIRHSK
300 ESGDFLYRMR DYMPPSHKAF IEDIHSAPSL RDYILSSGQD HLLTAYNQCV QALAELRSYH
360 ITMVTKYLIT AAAKAKHGKP NHLPGPPQAL KDRGTGGTAV MSFLKSVRDK TLESILHPRG
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
299442
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
299443
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
299444
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
299445
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
299446
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
299447
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
299448
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
299449
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
299450
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
299451
van Baren N.,Van den Eynde B.J.
Tryptophan-degrading enzymes in tumoral immune resistance.
Front. Immunol.
6
34-34
2015