- Molecular Basis for the Substrate Stereoselectivity in Tryptophan Dioxygenase
[作者:Capece, L; Lewis-Ballester, A; Marti, MA; Estrin, DA; Yeh, SR,期刊:Biochemistry, 页码:10910-10918 , 文章类型: Article,,卷期:2011年50-50]
- Tryptophan dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) are the only two heme proteins that catalyze the oxidation reaction of tryptophan (Trp) to N-formylkynurenine. While human IDO is able to oxidize both L-...
- A Typical Preparation of Francisella tularensis O-Antigen Yields a Mixture of Three Types of Saccharides
[作者:Wang, Q; Shi, XF; Leymarie, N; Madico, G; Sharon, J; Costello, CE; Zaia, J,期刊:Biochemistry, 页码:10941-10950 , 文章类型: Article,,卷期:2011年50-50]
- Tularemia is a severe infectious disease in humans caused by the Gram-negative bacterium Francisella tularensis (Ft). Because of its low infectious dose, high mortality rate, and the threat of its large-scale disseminati...
- The Siderophore-Interacting Protein YqjH Acts as a Ferric Reductase in Different Iron Assimilation Pathways of Escherichia coli
[作者:Miethke, M; Hou, J; Marahiel, MA,期刊:Biochemistry, 页码:10951-10964 , 文章类型: Article,,卷期:2011年50-50]
- Siderophore-interacting proteins (SIPs), such as YqjH from Escherichia coil, are widespread among bacteria and commonly associated with iron-dependent induction and siderophore utilization. In this study, we show by deta...
- Current Computer Modeling Cannot Explain Why Two Highly Similar Sequences Fold into Different Structures
[作者:Allison, JR; Bergeler, M; Hansen, N; van Gunsteren, WF,期刊:Biochemistry, 页码:10965-10973 , 文章类型: Article,,卷期:2011年50-50]
- The remarkable recent creation of two proteins that fold into two completely different and stable structures, exhibit different functions, yet differ by only a few amino acids poses a conundrum to those hoping to underst...
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