|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5675 |
| Enzyme 1 Name |
Tryptophan 2,3-dioxygenase |
| Enzyme 1 Synonyms |
- TDO
- Tryptamin 2,3-dioxygenase
- Tryptophan oxygenase
- TO
- TRPO
- Tryptophan pyrrolase
- Tryptophanase
|
| Enzyme 1 Gene Name |
TDO2 |
| Enzyme 1 Protein Sequence |
>Tryptophan 2,3-dioxygenase
MSGCPFLGNNFGYTFKKLPVEGSEEDKSQTGVNRASKGGLIYGNYLHLEKVLNAQELQSE
TKGNKIHDEHLFIITHQAYELWFKQILWELDSVREIFQNGHVRDERNMLKVVSRMHRVSV
ILKLLVQQFSILETMTALDFNDFREYLSPASGFQSLQFRLLENKIGVLQNMRVPYNRRHY
RDNFKGEENELLLKSEQEKTLLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEFIR
IQAKEESEEKEEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRALQGALMIYFYRE
EPRFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSKAGTGGSSGYHYLRSTVSDRYK
VFVDLFNLSTYLIPRHWIPKMNPTIHKFLYTAEYCDSSYFSSDESD
|
| Enzyme 1 Number of Residues |
406 |
| Enzyme 1 Molecular Weight |
47871.2 |
| Enzyme 1 Theoretical pI |
6.93 |
| Enzyme 1 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on single donors with incorporation of molecular oxygen
- oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
- transition metal ion binding
- tryptophan 2,3-dioxygenase activity
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid derivative metabolic process
- cellular biogenic amine metabolic process
- cellular metabolic process
- indolalkylamine metabolic process
- metabolic process
- oxidation reduction
- tryptophan catabolic process
- tryptophan catabolic process to kynurenine
- tryptophan metabolic process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in tryptophan 2,3-dioxygenase activity |
| Enzyme 1 Specific Function |
Incorporates oxygen into the indole moiety of tryptophan. Has a broad specificity towards tryptamine and derivatives including D- and L-tryptophan, 5-hydroxytryptophan and serotonin |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- L-tryptophan + O2 = N-formyl-L-kynurenine [RN:R00678]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
Not Available |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P48775  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
T23O_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1221 bp
ATGAGTGGGTGCCCATTTTTAGGAAACAACTTTGGATATACTTTTAAAAAACTCCCCGTA
GAAGGCAGCGAAGAAGACAAATCACAAACTGGTGTGAATAGAGCCAGCAAAGGAGGTCTT
ATCTATGGGAACTACCTGCATTTGGAAAAAGTTTTGAATGCACAAGAACTGCAAAGTGAA
ACAAAAGGAAATAAAATCCATGATGAACATCTTTTTATCATAACTCATCAAGCTTATGAA
CTCTGGTTTAAGCAAATCCTCTGGGAGTTGGATTCTGTTCGAGAGATCTTTCAGAATGGC
CATGTCAGAGATGAAAGGAACATGCTTAAGGTTGTTTCTCGGATGCACCGAGTGTCAGTG
ATCCTGAAACTGCTGGTGCAGCAGTTTTCCATTCTGGAGACGATGACAGCCTTGGACTTC
AATGACTTCAGAGAGTACTTATCTCCAGCATCAGGCTTCCAGAGTTTGCAATTCCGACTA
TTAGAAAACAAGATAGGTGTTCTTCAGAACATGAGAGTCCCTTATAACAGAAGACATTAT
CGTGATAACTTCAAAGGAGAAGAAAATGAACTGCTACTTAAATCTGAGCAGGAAAAGACA
CTTCTGGAATTAGTGGAGGCATGGCTGGAAAGAACTCCAGGTTTAGAGCCACATGGATTT
AACTTCTGGGGAAAGCTTGAAAAAAATATCACCAGAGGCCTGGAAGAGGAATTCATAAGG
ATTCAGGCTAAAGAAGAGTCTGAAGAAAAAGAGGAACAGGTGGCTGAATTTCAGAAGCAA
AAAGAGGTGCTACTGTCCTTATTTGATGAGAAACGTCATGAACATCTCCTTAGTAAAGGT
GAAAGACGGCTGTCATACAGAGCACTTCAGGGAGCATTGATGATATATTTTTACAGGGAA
GAGCCTAGGTTCCAGGTGCCTTTTCAGTTGCTGACTTCTCTTATGGACATAGATTCACTG
ATGACCAAATGGAGATATAACCATGTGTGCATGGTGCACAGAATGCTGGGCAGCAAAGCT
GGCACCGGTGGTTCCTCAGGCTATCACTACCTGCGATCAACTGTGAGTGATAGGTACAAG
GTATTTGTAGATTTATTTAATCTTTCAACATACCTGATTCCCCGACACTGGATACCGAAG
ATGAACCCAACCATTCACAAATTTCTATATACAGCAGAATACTGTGATAGCTCCTACTTC
AGCAGTGATGAATCAGATTAA
|
| Enzyme 1 GenBank Gene ID |
U32989  |
| Enzyme 1 GeneCard ID |
TDO2  |
| Enzyme 1 GenAtlas ID |
TDO2  |
| Enzyme 1 HGNC ID |
HGNC:11708  |
| Enzyme 1 Chromosome Location |
4 |
| Enzyme 1 Locus |
4q31-q32 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Comings DE, Muhleman D, Dietz G, Sherman M, Forest GL: Sequence of human tryptophan 2,3-dioxygenase (TDO2): presence of a glucocorticoid response-like element composed of a GTT repeat and an intronic CCCCT repeat. Genomics. 1995 Sep 20;29(2):390-6. [PubMed
]
- 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 TO, 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. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Tao WA, Wollscheid B, O'Brien R, Eng JK, Li XJ, Bodenmiller B, Watts JD, Hood L, Aebersold R: Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry. Nat Methods. 2005 Aug;2(8):591-8. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
13059 |
| Enzyme 2 Name |
Probable arylformamidase |
| Enzyme 2 Synonyms |
- Kynurenine formamidase
- KF
|
| Enzyme 2 Gene Name |
AFMID |
| Enzyme 2 Protein Sequence |
>Probable arylformamidase
MMDVSGVGFPSKVPWKKMSAEELENQYCPSRWVVRLGAEEALRTYSQIGIEATTRARATR
KSLLHVPYGDGEGEKVDIYFPDESSEALPFFLFFHGGYWQSGSKDESAFMVHPLTAQGVA
VVIVAYGIAPKGTLDHMVDQVTRSVAFVQKRYPSNKGIYLCGHSAGAHLAAMMLLADWTK
HGVTPNLRGFFLVSGVFDLEPIVYTSQNVALQLTLEDAQRNSPQLKVAQAQPVDPTCRVL
VVVGQFDSPEFHRQSWEFYQTLCQGEWKASFEELHDVDHFEIVENLTQKDNVLTQIILKT
IFQ
|
| Enzyme 2 Number of Residues |
303 |
| Enzyme 2 Molecular Weight |
33991.5 |
| Enzyme 2 Theoretical pI |
5.78 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in hydrolase activity |
| Enzyme 2 Specific Function |
Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the conversion of tryptophan to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites |
| Enzyme 2 Pathways |
- Glyoxylate and Dicarboxylate Metabolism (map00630
)
- Tryptophan Metabolism (map00380
)
|
| Enzyme 2 Reactions |
- N-formyl-L-kynurenine + H2O = formate + L-kynurenine [RN:R01959]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
124375910  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q63HM1  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
AFMID_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>912 bp
ATGATGGATGTGTCTGGTGTGGGTTTCCCAAGCAAGGTTCCTTGGAAGAAGATGTCTGCA
GAGGAGCTGGAGAATCAGTACTGTCCCAGCCGATGGGTTGTCCGACTGGGAGCAGAGGAA
GCCTTGAGGACCTACTCACAGATAGGAATTGAAGCCACCACAAGGGCCCGGGCCACCAGG
AAGAGCCTGCTGCATGTCCCCTATGGAGACGGCGAAGGGGAGAAAGTGGACATTTACTTC
CCCGACGAGTCGTCTGAAGCCTTGCCTTTCTTCCTGTTCTTTCACGGAGGATACTGGCAG
AGCGGAAGTAAGGATGAGTCTGCCTTCATGGTCCACCCGCTGACGGCACAGGGAGTGGCC
GTGGTAATAGTGGCTTACGGCATCGCCCCCAAAGGCACCCTGGACCACATGGTAGACCAG
GTGACCCGCAGCGTTGCGTTTGTCCAGAAGCGGTATCCAAGCAACAAGGGAATTTACCTG
TGTGGACACTCAGCCGGGGCCCACCTGGCTGCCATGATGCTCCTGGCCGACTGGACCAAG
CATGGGGTCACGCCCAACCTCAGAGGCTTTTTCCTGGTGAGTGGGGTCTTTGACCTGGAG
CCCATCGTGTATACTTCACAGAACGTTGCTCTCCAGCTGACCCTGGAGGACGCTCAGAGG
AATAGCCCCCAGCTGAAGGTGGCCCAGGCACAGCCGGTGGACCCCACCTGCCGTGTGCTG
GTGGTCGTGGGCCAGTTCGACTCCCCCGAATTCCACCGACAGTCCTGGGAGTTTTACCAG
ACCCTGTGTCAAGGAGAGTGGAAAGCCTCATTTGAAGAGCTCCACGATGTGGACCACTTT
GAAATTGTTGAGAATCTGACCCAGAAGGACAACGTGCTCACCCAGATTATCTTGAAAACA
ATCTTCCAGTAG
|
| Enzyme 2 GenBank Gene ID |
BC132824  |
| Enzyme 2 GeneCard ID |
AFMID  |
| Enzyme 2 GenAtlas ID |
AFMID  |
| Enzyme 2 HGNC ID |
HGNC:20910  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
17q25.3 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
13115 |
| Enzyme 3 Name |
Indoleamine 2,3-dioxygenase 2 |
| Enzyme 3 Synonyms |
- IDO-2
- Indoleamine 2,3-dioxygenase-like protein 1
- Indoleamine-pyrrole 2,3-dioxygenase-like protein 1
|
| Enzyme 3 Gene Name |
IDO2 |
| Enzyme 3 Protein Sequence |
>Indoleamine 2,3-dioxygenase 2
MEPHRPNVKTAVPLSLESYHISEEYGFLLPDSLKELPDHYRPWMEIANKLPQLIDAHQLQ
AHVDKMPLLSCQFLKGHREQRLAHLVLSFLTMGYVWQEGEAQPAEVLPRNLALPFVEVSR
NLGLPPILVHSDLVLTNWTKKDPDGFLEIGNLETIISFPGGESLHGFILVTALVEKEAVP
GIKALVQATNAILQPNQEALLQALQRLRLSIQDITKTLGQMHDYVDPDIFYAGIRIFLSG
WKDNPAMPAGLMYEGVSQEPLKYSGGSAAQSTVLHAFDEFLGIRHSKESGDFLYRMRDYM
PPSHKAFIEDIHSAPSLRDYILSSGQDHLLTAYNQCVQALAELRSYHITMVTKYLITAAA
KAKHGKPNHLPGPPQALKDRGTGGTAVMSFLKSVRDKTLESILHPRG
|
| Enzyme 3 Number of Residues |
407 |
| Enzyme 3 Molecular Weight |
45423.9 |
| Enzyme 3 Theoretical pI |
6.84 |
| Enzyme 3 GO Classification |
| Function |
- binding
- cation binding
- heme binding
- ion binding
- iron ion binding
- metal ion binding
- transition metal ion binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in heme binding |
| Enzyme 3 Specific Function |
Catalyzes the first and rate-limiting step in the kynurenine pathway of tryptophan catabolism |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
Not Available |
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
145204985  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q6ZQW0  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
I23O2_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1224 bp
ATGGAGCCCCACAGACCGAATGTGAAGACAGCAGTGCCATTGTCTTTGGAAAGCTATCAC
ATATCTGAAGAGTATGGCTTTCTTCTTCCAGATTCTCTGAAAGAACTTCCAGATCATTAT
AGGCCTTGGATGGAAATTGCCAACAAACTTCCTCAATTGATTGATGCTCACCAGCTTCAA
GCTCATGTGGACAAGATGCCCCTGCTGAGCTGCCAGTTCCTGAAGGGTCACCGGGAGCAG
CGCCTGGCCCACCTGGTCCTGAGCTTCCTCACCATGGGTTATGTCTGGCAGGAAGGAGAG
GCGCAGCCTGCAGAGGTCCTGCCAAGGAATCTTGCCCTTCCATTTGTCGAAGTCTCCAGG
AACTTGGGGCTCCCTCCTATCCTGGTCCACTCAGACTTGGTGCTGACGAACTGGACCAAA
AAAGATCCAGACGGATTCCTGGAAATTGGGAACCTGGAGACCATCATCTCATTTCCTGGG
GGAGAGAGCCTGCATGGTTTTATACTGGTGACTGCTTTGGTAGAGAAAGAAGCAGTGCCT
GGGATAAAGGCTCTTGTTCAGGCCACGAATGCTATCTTGCAGCCCAACCAGGAGGCCCTG
CTCCAAGCCCTGCAGCGACTGAGACTGTCTATTCAGGACATCACCAAAACCTTAGGACAG
ATGCATGATTATGTAGATCCAGACATATTTTATGCAGGCATCCGGATCTTTCTCTCTGGA
TGGAAAGACAACCCAGCAATGCCTGCAGGGCTGATGTATGAAGGAGTTTCCCAAGAGCCC
CTGAAATACTCCGGCGGGAGTGCAGCTCAGAGCACAGTGCTTCATGCCTTTGATGAGTTC
TTAGGCATTCGTCATAGCAAGGAAAGTGGTGACTTTCTGTACAGAATGAGGGATTACATG
CCTCCTTCCCATAAGGCCTTCATAGAAGACATCCACTCAGCACCTTCCCTGAGGGACTAC
ATCCTGTCCTCTGGACAGGACCACTTGCTGACAGCTTATAACCAGTGTGTGCAGGCCCTG
GCAGAGCTGCGGAGCTATCACATCACCATGGTCACCAAATACCTCATCACAGCTGCAGCC
AAGGCAAAGCATGGGAAGCCAAACCATCTCCCAGGGCCTCCTCAGGCTTTAAAAGACAGG
GGCACAGGTGGAACCGCAGTTATGAGCTTTCTTAAGAGTGTCAGGGATAAGACCTTGGAG
TCAATCCTTCACCCACGTGGTTAG
|
| Enzyme 3 GenBank Gene ID |
EF052681  |
| Enzyme 3 GeneCard ID |
IDO2  |
| Enzyme 3 GenAtlas ID |
IDO2  |
| Enzyme 3 HGNC ID |
HGNC:27269  |
| Enzyme 3 Chromosome Location |
8 |
| Enzyme 3 Locus |
8p11.21 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Ball HJ, Sanchez-Perez A, Weiser S, Austin CJ, Astelbauer F, Miu J, McQuillan JA, Stocker R, Jermiin LS, Hunt NH: Characterization of an indoleamine 2,3-dioxygenase-like protein found in humans and mice. Gene. 2007 Jul 1;396(1):203-13. Epub 2007 Apr 18. [PubMed
]
- 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 TO, 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. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Metz R, Duhadaway JB, Kamasani U, Laury-Kleintop L, Muller AJ, Prendergast GC: 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. 2007 Aug 1;67(15):7082-7. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
13117 |
| Enzyme 4 Name |
cDNA FLJ75236, highly similar to Human tryptophan oxygenase |
| Enzyme 4 Synonyms |
- TDOmRNA
- Tryptophan 2,3-dioxygenase, isoform CRA_b
|
| Enzyme 4 Gene Name |
TDO2 |
| Enzyme 4 Protein Sequence |
>cDNA FLJ75236, highly similar to Human tryptophan oxygenase
MSGCPFLGNNFGYTFKKLPVEGSEEDKSQTGVNRASKGGLIYGNYLHLEKVLNAQELQSE
TKGNKIHDEHLFIITHQAYELWFKQILWELDSVREIFQNGHVRDERNMLKVVSRMHRVSV
ILKLLVQQFSILETMTALDFNDFREYLSPASGFQSLQFRLLENKIGVLQNMRVPYNRRHY
RDNFKGEENELLLKSEQEKTLLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEFIR
IQAKEESEEKEEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRALQGALMIYFYRE
EPRFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSKAGTGGSSGYHYLRSTVSDRYK
VFVDLFNLSTYLIPRHWIPKMNPTIHKFLYTAEYCDSSYFSSDESD
|
| Enzyme 4 Number of Residues |
406 |
| Enzyme 4 Molecular Weight |
47872 |
| Enzyme 4 Theoretical pI |
6.93 |
| Enzyme 4 GO Classification |
Not Available |
| Enzyme 4 General Function |
Amino acid transport and metabolism |
| Enzyme 4 Specific Function |
Not Available |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
Not Available |
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
158259859  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
A8K053  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
A8K053_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
Not Available |
| Enzyme 4 GenBank Gene ID |
AK289418  |
| Enzyme 4 GeneCard ID |
A8K053  |
| Enzyme 4 GenAtlas ID |
Not Available |
| Enzyme 4 HGNC ID |
Not Available |
| Enzyme 4 Chromosome Location |
Not Available |
| Enzyme 4 Locus |
Not Available |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
Not Available |
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
13118 |
| Enzyme 5 Name |
Kynureninase (L-kynurenine hydrolase) |
| Enzyme 5 Synonyms |
- SubName: Kynureninase (L-kynurenine hydrolase), isoform CRA_a
|
| Enzyme 5 Gene Name |
KYNU |
| Enzyme 5 Protein Sequence |
>Kynureninase (L-kynurenine hydrolase)
MEPSSLELPADTVQRIAAELKCHPTDERVALHLDEEDKLRHFRECFYIPKIQDLPPVDLS
LVNKDENAIYFLGNSLGLQPKMVKTYLEEELDKWAKIAAYGHEVGKRPWITGDESIVGLM
KDIVGANEKEIALMNALTVNLHLLMLSFFKPTPKRYKILLEAKAFPSDHYAIESQLQLHG
LNIEESMRMIKPREGEETLRIEDILEVIEKEGDSIAVILFSGVHFYTGQHFNIPAITKAG
QAKGCYVGFDLAHAVGNVELYLHDWGVDFACWCSYKYLNAGAGGIAGAFIHEKHAHTIKP
ARSEFFN
|
| Enzyme 5 Number of Residues |
307 |
| Enzyme 5 Molecular Weight |
34634.5 |
| Enzyme 5 Theoretical pI |
5.71 |
| Enzyme 5 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- hydrolase activity
- hydrolase activity, acting on acid carbon-carbon bonds
- hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
- kynureninase activity
- pyridoxal phosphate binding
|
| Process |
- NAD biosynthetic process
- cellular amino acid and derivative metabolic process
- cellular amino acid derivative metabolic process
- cellular biogenic amine metabolic process
- cellular metabolic process
- coenzyme biosynthetic process
- coenzyme metabolic process
- cofactor metabolic process
- indolalkylamine metabolic process
- metabolic process
- nicotinamide nucleotide biosynthetic process
- pyridine nucleotide biosynthetic process
- tryptophan catabolic process
- tryptophan metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 5 General Function |
Involved in metabolic process |
| Enzyme 5 Specific Function |
Not Available |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
12654129  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q9BVW3  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
Q9BVW3_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>924 bp
ATGGAGCCTTCATCTCTTGAGCTGCCGGCTGACACAGTGCAGCGCATTGCGGCTGAACTC
AAATGCCACCCAACGGATGAGAGGGTGGCTCTCCACCTAGATGAGGAAGATAAGCTGAGG
CACTTCAGGGAGTGCTTTTATATTCCCAAAATACAGGATCTGCCTCCAGTTGATTTATCA
TTAGTGAATAAAGATGAAAATGCCATCTATTTCTTGGGAAATTCTCTTGGCCTTCAACCA
AAAATGGTTAAAACATATCTTGAAGAAGAACTAGATAAGTGGGCCAAAATAGCAGCCTAT
GGTCATGAAGTGGGGAAGCGTCCTTGGATTACAGGAGATGAGAGTATTGTAGGCCTTATG
AAGGACATTGTAGGAGCCAATGAGAAAGAAATAGCCCTAATGAATGCTTTGACTGTAAAT
TTACATCTTCTAATGTTATCATTTTTTAAGCCTACGCCAAAACGATATAAAATTCTTCTA
GAAGCCAAAGCCTTCCCTTCTGATCATTATGCTATTGAGTCACAACTACAACTTCACGGA
CTTAACATTGAAGAAAGTATGCGGATGATAAAGCCAAGAGAGGGGGAAGAAACCTTAAGA
ATAGAGGATATCCTTGAAGTAATTGAGAAGGAAGGAGACTCAATTGCAGTGATCCTGTTC
AGTGGGGTGCATTTTTACACTGGACAGCACTTTAATATTCCTGCCATCACAAAAGCTGGA
CAAGCGAAGGGTTGTTATGTTGGCTTTGATCTAGCACATGCAGTTGGAAATGTTGAACTC
TACTTACATGACTGGGGAGTTGATTTTGCCTGCTGGTGTTCCTACAAGTATTTAAATGCA
GGAGCAGGAGGAATTGCTGGTGCCTTCATTCATGAAAAGCATGCCCATACGATTAAACCT
GCGAGATCGGAGTTCTTTAATTAG
|
| Enzyme 5 GenBank Gene ID |
BC000879  |
| Enzyme 5 GeneCard ID |
KYNU  |
| Enzyme 5 GenAtlas ID |
KYNU  |
| Enzyme 5 HGNC ID |
HGNC:6469  |
| Enzyme 5 Chromosome Location |
2 |
| Enzyme 5 Locus |
2q22.2 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |