Structural highlights
Function
T23O_HUMAN 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 (By similarity).
Publication Abstract from PubMed
Tryptophan 2,3-dioxygenase (TDO), one of the two key enzymes in the kynurenine pathway, catalyzes the indole ring cleavage at the C2-C3 bond of L-tryptophan. This is a rate-limiting step in the regulation of tryptophan concentration in vivo, and is thus important in drug discovery for cancer and immune diseases. Here, we report the crystal structure of human TDO (hTDO) without the heme cofactor to 2.90 A resolution. The overall fold and the tertiary assembly of hTDO into a tetramer, as well as the active site architecture, are well conserved and similar to the structures of known orthologues. Kinetic and mutational studies confirmed that eight residues play critical roles in L-tryptophan oxidation.
Structural and functional analyses of human tryptophan 2,3-dioxygenase.,Meng B, Wu D, Gu J, Ouyang S, Ding W, Liu ZJ Proteins. 2014 Nov;82(11):3210-6. doi: 10.1002/prot.24653. Epub 2014 Aug 30. PMID:25066423[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Meng B, Wu D, Gu J, Ouyang S, Ding W, Liu ZJ. Structural and functional analyses of human tryptophan 2,3-dioxygenase. Proteins. 2014 Nov;82(11):3210-6. doi: 10.1002/prot.24653. Epub 2014 Aug 30. PMID:25066423 doi:http://dx.doi.org/10.1002/prot.24653
