Probing the Functional Role of Two Conserved Active Site Aspartates in Mouse Adenosine Deaminase†

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

Functional Role of the Active Site Glutamate-368 in Rat Short Chain Acyl-CoA Dehydrogenase†

Biochemistry ◽  
1996 ◽  
Vol 35 (48) ◽  
pp. 15356-15363 ◽  
Author(s):  
Kevin P. Battaile ◽  
Al-Walid A. Mohsen ◽  
Jerry Vockley
Keyword(s):  
Active Site ◽  
Functional Role ◽  
Short Chain ◽  
Chain Acyl

Functional Role of the Conserved Active Site Proline of Triosephosphate Isomerase†,‡

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

scholarly journals Reconstruction of nitrogenase predecessors suggests origin from maturase-like enzymes

2021 ◽  
Author(s):  
Amanda K. Garcia ◽  
Bryan Kolaczkowski ◽  
Betul Kacar
Keyword(s):  
Nitrogen Fixation ◽  
Active Site ◽  
Biological Nitrogen Fixation ◽  
Functional Role ◽  
Nitrogen Fixing ◽  
Evolutionary Contingency ◽  
Phylogenetic Constraints ◽  
Essential Enzyme ◽  
Biological Nitrogen

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.

Important functional role of residue x of the presenilin GxGD protease active site motif for APP substrate cleavage specificity and substrate selectivity of γ-secretase

2013 ◽  
Vol 125 (1) ◽  
pp. 144-156 ◽  
Author(s):  
Benedikt Kretner ◽  
Akio Fukumori ◽  
Peer-Hendrik Kuhn ◽  
Blanca Isabel Pérez-Revuelta ◽  
Stefan F. Lichtenthaler ◽  
...  
Keyword(s):  
Active Site ◽  
Functional Role ◽  
Substrate Selectivity ◽  
Cleavage Specificity ◽  
Active Site Motif ◽  
Substrate Cleavage
Sign in / Sign up

Export Citation Format

Share Document