The functional role of the key residues in the active site of peroxidases

1995 ◽  
Vol 23 (2) ◽  
pp. 240-244 ◽  
Author(s):  
G. Smulevich
Keyword(s):  
Active Site ◽  
Functional Role ◽  
Key Residues

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

The structure of the genomicBacillus subtilisdUTPase: novel features in the Phe-lid

2010 ◽  
Vol 66 (9) ◽  
pp. 953-961 ◽  
Author(s):  
Javier García-Nafría ◽  
Lynn Burchell ◽  
Mine Takezawa ◽  
Neil J. Rzechorzek ◽  
Mark J. Fogg ◽  
...  
Keyword(s):  
Active Site ◽  
Sequence Motifs ◽  
Conserved Sequence ◽  
General Base ◽  
Base Points ◽  
Phosphate Chain ◽  
C Terminus ◽  
Conserved Sequence Motifs ◽  
Key Residues

dUTPases are a ubiquitous family of enzymes that are essential for all organisms and catalyse the breakdown of 2-deoxyuridine triphosphate (dUTP). InBacillus subtilisthere are two homotrimeric dUTPases: a genomic and a prophage form. Here, the structures of the genomic dUTPase and of its complex with the substrate analogue dUpNHpp and calcium are described, both at 1.85 Å resolution. The overall fold resembles that of previously solved trimeric dUTPases. The C-terminus, which contains one of the conserved sequence motifs, is disordered in both structures. The crystal of the complex contains six independent protomers which accommodate six dUpNHpp molecules, with three triphosphates in thetransconformation and the other three in the activegaucheconformation. The structure of the complex confirms the role of several key residues that are involved in ligand binding and the position of the catalytic water. Asp82, which has previously been proposed to act as a general base, points away from the active site. In the complex Ser64 reorients in order to hydrogen bond the phosphate chain of the substrate. A novel feature has been identified: the position in the sequence of the `Phe-lid', which packs against the uracil moiety, is adjacent to motif III, whereas in all other dUTPase structures the lid is in a conserved position in motif V of the flexible C-terminal arm. This requires a reconsideration of some aspects of the accepted mechanism.

scholarly journals An active site at work – the role of key residues in C. diphteriae coproheme decarboxylase

2022 ◽  
pp. 111718
Author(s):  
Federico Sebastiani ◽  
Riccardo Risorti ◽  
Chiara Niccoli ◽  
Hanna Michlits ◽  
Maurizio Becucci ◽  
...  
Keyword(s):  
Active Site ◽  
Key Residues

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

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.

Sign in / Sign up

Export Citation Format

Share Document