A Computational and Modeling Study of the Reaction Mechanism of Staphylococcus aureus Monoglycosyltransferase Reveals New Insights on the GT51 Family of Enzymes

2020 ◽  
Vol 60 (11) ◽  
pp. 5513-5528 ◽  
Author(s):  
Kenneth Goossens ◽  
Rui PP Neves ◽  
Pedro A Fernandes ◽  
Hans De Winter
Keyword(s):  
Staphylococcus Aureus ◽  
Reaction Mechanism ◽  
Modeling Study

Experimental and Kinetic Modeling Study of Autoignition Characteristics ofn-Heptane/Ethanol by Constant Volume Bomb and Detail Reaction Mechanism

2017 ◽  
Vol 31 (12) ◽  
pp. 13610-13626 ◽  
Author(s):  
Runzhao Li ◽  
Zhongchang Liu ◽  
Yongqiang Han ◽  
Manzhi Tan ◽  
Yun Xu ◽  
...  
Keyword(s):  
Reaction Mechanism ◽  
Kinetic Modeling ◽  
Constant Volume ◽  
Modeling Study

scholarly journals Structural and functional studies of SAV0551 from Staphylococcus aureus as a chaperone and glyoxalase III

2017 ◽  
Vol 37 (6) ◽  
Author(s):  
Hyo Jung Kim ◽  
Ki-Young Lee ◽  
Ae-Ran Kwon ◽  
Bong-Jin Lee
Keyword(s):  
Staphylococcus Aureus ◽  
Reaction Mechanism ◽  
Quaternary Structure ◽  
Hypothetical Protein ◽  
Catalytic Triad ◽  
Common Theme ◽  
Functional Studies ◽  
The Common ◽  
Cellular Stresses ◽  
Glyoxalase Iii

The DJ-1/ThiJ/PfpI superfamily of proteins is highly conserved across all biological kingdoms showing divergent multifunctions, such as chaperone, catalase, protease, and kinase. The common theme of these functions is responding to and managing various cellular stresses. DJ-1/ThiJ/PfpI superfamily members are classified into three subfamilies according to their quaternary structure (DJ-1-, YhbO-, and Hsp-types). The Hsp-type subfamily includes Hsp31, a chaperone and glyoxalase III. SAV0551, an Hsp-type subfamily member from Staphylococcus aureus, is a hypothetical protein that is predicted as Hsp31. Thus, to reveal the function and reaction mechanism of SAV0551, the crystal structure of SAV0551 was determined. The overall folds in SAV0551 are similar to other members of the Hsp-type subfamily. We have shown that SAV0551 functions as a chaperone and that the surface structure is crucial for holding unfolded substrates. As many DJ-1/ThiJ/PfpI superfamily proteins have been characterized as glyoxalase III, our study also demonstrates SAV0551 as a glyoxalase III that is independent of any cofactors. The reaction mechanism was evaluated via a glyoxylate-bound structure that mimics the hemithioacetal reaction intermediate. We have confirmed that the components required for reaction are present in the structure, including a catalytic triad for a catalytic action, His78 as a base, and a water molecule for hydrolysis. Our functional studies based on the crystal structures of native and glyoxylate-bound SAV0551 will provide a better understanding of the reaction mechanism of a chaperone and glyoxalase III.

Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from staphylococcus aureus

1998 ◽  
Vol 5 (5) ◽  
pp. 357-362 ◽  
Author(s):  
Michael Hennig ◽  
Allan D′Arcy ◽  
Isabella C. Hampele ◽  
Malcolm G.P. Page ◽  
Christian Oefner ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Staphylococcus Aureus ◽  
Reaction Mechanism ◽  
Dihydroneopterin Aldolase
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