Structural and mutational analyses reveal the functional role of active-site Lys-154 and Asp-173 of Salmonella typhimurium AphA protein

2007 ◽  
Vol 464 (1) ◽  
pp. 70-79 ◽  
Author(s):  
Ravindra D. Makde ◽  
Gagan D. Gupta ◽  
Suresh K. Mahajan ◽  
Vinay Kumar
Biochemistry ◽  
1996 ◽  
Vol 35 (48) ◽  
pp. 15356-15363 ◽  
Author(s):  
Kevin P. Battaile ◽  
Al-Walid A. Mohsen ◽  
Jerry Vockley

Biochemistry ◽  
2006 ◽  
Vol 45 (51) ◽  
pp. 15483-15494 ◽  
Author(s):  
Marco G. Casteleijn ◽  
Markus Alahuhta ◽  
Katrin Groebel ◽  
Ibrahim El-Sayed ◽  
Koen Augustyns ◽  
...  

Biochemistry ◽  
1996 ◽  
Vol 35 (24) ◽  
pp. 7862-7872 ◽  
Author(s):  
Vera Sideraki ◽  
Khalid A. Mohamedali ◽  
David K. Wilson ◽  
Zengyi Chang ◽  
Rodney E. Kellems ◽  
...  

2021 ◽  
Author(s):  
Amanda K. Garcia ◽  
Bryan Kolaczkowski ◽  
Betul Kacar

The evolution of biological nitrogen fixation, uniquely catalyzed by nitrogenase enzymes, has been one of the most consequential biogeochemical innovations over life's history. Though understanding the early evolution of nitrogen fixation has been a longstanding goal from molecular, biogeochemical, and planetary perspectives, its origins remain enigmatic. In this study, we reconstructed the evolutionary histories of nitrogenases, as well as homologous maturase proteins that participate in the assembly of the nitrogenase active-site cofactor but are not able to fix nitrogen. We combined phylogenetic and ancestral sequence inference with an analysis of predicted functionally divergent sites between nitrogenases and maturases to infer the nitrogen-fixing capabilities of their shared ancestors. Our results provide phylogenetic constraints to the emergence of nitrogen fixation and suggest that nitrogenases likely emerged from maturase-like predecessors. Though the precise functional role of such a predecessor protein remains speculative, our results highlight evolutionary contingency as a significant factor shaping the evolution of a biogeochemically essential enzyme.


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