View publication

Histidine 55 of tryptophan 2,3-dioxygenase is not an active site base but regulates catalysis by controlling substrate binding.

Thackray SJ, Bruckmann C, Anderson JL, Campbell LP, Xiao R, Zhao L, Mowat CG, Forouhar F, Tong L, Chapman SK,
Biochemistry (2008) 47:10677-84 PublishedPSI:Phase 2  
Northeast Structural Genomics Consortium

(click to unfold)
Tryptophan 2,3-dioxygenase (TDO) from Xanthomonas campestris is a highly specific heme-containing enzyme from a small family of homologous enzymes, which includes indoleamine 2,3-dioxygenase (IDO). ...
metabolism chemistry genetics enzymology 
Catalytic Domain Crystallography, X-Ray Animals Models, Molecular Protein Binding Protein Structure, Secondary Histidine Bacterial Proteins Kinetics Substrate Specificity Molecular Structure Mutagenesis, Site-Directed Point Mutation Xanthomonas campestris Tryptophan Oxygenase 
18783250  
10.1021/bi801202a  
31 (Last update: 08/11/2018 5:22:14pm)  
2BK9
3E08  
structure