scholarly journals Imidazole Glycerol Phosphate Synthase fromThermotoga maritima

2001 ◽  
Vol 276 (23) ◽  
pp. 20387-20396 ◽  
Author(s):  
Silke Beismann-Driemeyer ◽  
Reinhard Sterner
Keyword(s):  
Glycerol Phosphate ◽  
Imidazole Glycerol Phosphate ◽  
Phosphate Synthase

scholarly journals Crystal Structure of Imidazole Glycerol Phosphate Synthase

Structure ◽  
2001 ◽  
Vol 9 (10) ◽  
pp. 987-997 ◽  
Author(s):  
Barnali N Chaudhuri ◽  
Stephanie C Lange ◽  
Rebecca S Myers ◽  
Sridar V Chittur ◽  
V.Jo Davisson ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Glycerol Phosphate ◽  
Imidazole Glycerol Phosphate ◽  
Phosphate Synthase

scholarly journals Structural Evidence for Ammonia Tunneling across the (βα)8 Barrel of the Imidazole Glycerol Phosphate Synthase Bienzyme Complex

Structure ◽  
2002 ◽  
Vol 10 (2) ◽  
pp. 185-193 ◽  
Author(s):  
Alice Douangamath ◽  
Martina Walker ◽  
Silke Beismann-Driemeyer ◽  
M.Cristina Vega-Fernandez ◽  
Reinhard Sterner ◽  
...  
Keyword(s):  
Glycerol Phosphate ◽  
Imidazole Glycerol Phosphate ◽  
Phosphate Synthase

Significance of the Protein Interface Configuration for Allostery in Imidazole Glycerol Phosphate Synthase

Biochemistry ◽  
2020 ◽  
Vol 59 (29) ◽  
pp. 2729-2742
Author(s):  
Andrea C. Kneuttinger ◽  
Chitra Rajendran ◽  
Nadja A. Simeth ◽  
Astrid Bruckmann ◽  
Burkhard König ◽  
...  
Keyword(s):  
Protein Interface ◽  
Glycerol Phosphate ◽  
Imidazole Glycerol Phosphate ◽  
Phosphate Synthase

scholarly journals Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Jan Philip Wurm ◽  
Sihyun Sung ◽  
Andrea Christa Kneuttinger ◽  
Enrico Hupfeld ◽  
Reinhard Sterner ◽  
...  
Keyword(s):  
Molecular Basis ◽  
Dynamic Equilibrium ◽  
Underlying Mechanism ◽  
Activation Mechanism ◽  
Turnover Rates ◽  
Glycerol Phosphate ◽  
Allosteric Activation ◽  
Catalytically Active ◽  
Imidazole Glycerol Phosphate ◽  
Phosphate Synthase

AbstractImidazole glycerol phosphate synthase (HisFH) is a heterodimeric bienzyme complex operating at a central branch point of metabolism. HisFH is responsible for the HisH-catalyzed hydrolysis of glutamine to glutamate and ammonia, which is then used for a cyclase reaction by HisF. The HisFH complex is allosterically regulated but the underlying mechanism is not well understood. Here, we elucidate the molecular basis of the long range, allosteric activation of HisFH. We establish that the catalytically active HisFH conformation is only formed when the substrates of both HisH and HisF are bound. We show that in this conformation an oxyanion hole in the HisH active site is established, which rationalizes the observed 4500-fold allosteric activation compared to the inactive conformation. In solution, the inactive and active conformations are in a dynamic equilibrium and the HisFH turnover rates correlate with the population of the active conformation, which is in accordance with the ensemble model of allostery.

Distinct Allosteric Pathways in Imidazole Glycerol Phosphate Synthase from Yeast and Bacteria

2021 ◽  
Author(s):  
Federica Maschietto ◽  
Aria Gheeraert ◽  
Andrea Piazzi ◽  
Victor S. Batista ◽  
Ivan Rivalta
Keyword(s):  
Glycerol Phosphate ◽  
Imidazole Glycerol Phosphate ◽  
Phosphate Synthase
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