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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

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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). ...
genetics metabolism enzymology chemistry 
Crystallography, X-Ray Models, Molecular Molecular Structure Xanthomonas campestris Mutagenesis, Site-Directed Catalytic Domain Tryptophan Oxygenase Animals Kinetics Point Mutation Substrate Specificity Protein Structure, Secondary Protein Binding Bacterial Proteins Histidine 
18783250  
10.1021/bi801202a  
28 (Last update: 03/18/2017 12:16:37pm)  
2BK9
3E08  
structure