On a Possible Neutral Charge State for the Catalytic Dyad in β-Secretase When Bound to Hydroxyethylene Transition State Analogue Inhibitors

2011 ◽  
Vol 54 (8) ◽  
pp. 3081-3085 ◽  
Author(s):  
Fredy Sussman ◽  
José M. Otero ◽  
M. Carmen Villaverde ◽  
Marian Castro ◽  
José L. Domínguez ◽  
...  
Keyword(s):  
Transition State ◽  
Charge State ◽  
Transition State Analogue ◽  
Transition State Analogue Inhibitors ◽  
Catalytic Dyad ◽  
Neutral Charge State

scholarly journals Transition State Analogue Inhibitors of 5′-Deoxyadenosine/5′-Methylthioadenosine Nucleosidase from Mycobacterium tuberculosis

Biochemistry ◽  
2017 ◽  
Vol 56 (38) ◽  
pp. 5090-5098 ◽  
Author(s):  
Hilda A. Namanja-Magliano ◽  
Gary B. Evans ◽  
Rajesh K. Harijan ◽  
Peter C. Tyler ◽  
Vern L. Schramm
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Transition State ◽  
Transition State Analogue ◽  
Transition State Analogue Inhibitors

DFT and Docking Study of Potential Transition State Analogue Inhibitors of Glycosyltransferases

2008 ◽  
Vol 73 (5) ◽  
pp. 591-607 ◽  
Author(s):  
Lucie Sihelniková ◽  
Stanislav Kozmon ◽  
Igor Tvaroška
Keyword(s):  
Transition State ◽  
Density Functional ◽  
Density Functional Theory Method ◽  
Docking Study ◽  
Binding Mode ◽  
Functional Theory ◽  
Sulfate Anion ◽  
Transition State Analogue ◽  
Transition State Analogue Inhibitors ◽  
Energy Maps

Conformational behavior of the [(2S,3R,4R,5S)-3,4,5-trihydroxy-2-(phenylsulfanyl)tetrahydrofuran-2-yl]methyl sulfate anion (2), which is the potential transition state (TS) analogue of the inverting glycosyltransferases, was studied by means of two-dimensional potential-energy maps, using a density functional theory method at the B3LYP/6-31+G* level. The maps revealed the presence of eight low-energy domains which were refined at the B3LYP/6-311++G** level and led to six conformers in vacuum. In aqueous solution, two conformers dominate at equilibrium. The preferred conformers superimpose well with the transition state structure, as determined previously for glycosyltransferase GnT-I. The conformations of 2 in the active site of glycosyltransferase GnT-I were obtained by docking methods. It was found that one of the two best docking poses mimics the binding mode of TS. These results suggest that the proposed TS mimics 2 have the potential to be used as a scaffold for the design of TS analogue inhibitors.

Targeting the Polyamine Pathway with Transition-State Analogue Inhibitors of 5‘-Methylthioadenosine Phosphorylase

2004 ◽  
Vol 47 (12) ◽  
pp. 3275-3281 ◽  
Author(s):  
Gary B. Evans ◽  
Richard H. Furneaux ◽  
Vern L. Schramm ◽  
Vipender Singh ◽  
Peter C. Tyler
Keyword(s):  
Transition State ◽  
Methylthioadenosine Phosphorylase ◽  
Transition State Analogue ◽  
Transition State Analogue Inhibitors
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