Role of Active Site Tyrosine Residues in Catalysis by Human Glutathione Reductase†

Biochemistry ◽  
1998 ◽  
Vol 37 (40) ◽  
pp. 13968-13977 ◽  
Author(s):  
R. Luise Krauth-Siegel ◽  
L. David Arscott ◽  
Annette Schönleben-Janas ◽  
R. Heiner Schirmer ◽  
Charles H. Williams
Keyword(s):  
Glutathione Reductase ◽  
Active Site ◽  
Tyrosine Residues ◽  
Active Site Tyrosine

Rational Targeting of Active-Site Tyrosine Residues Using Sulfonyl Fluoride Probes

2015 ◽  
Vol 10 (4) ◽  
pp. 1094-1098 ◽  
Author(s):  
Erik C. Hett ◽  
Hua Xu ◽  
Kieran F. Geoghegan ◽  
Ariamala Gopalsamy ◽  
Robert E. Kyne ◽  
...  
Keyword(s):  
Active Site ◽  
Tyrosine Residues ◽  
Active Site Tyrosine ◽  
Sulfonyl Fluoride

The role of active site tyrosine 58 in Citrobacter freundii methionine γ-lyase

2015 ◽  
Vol 1854 (9) ◽  
pp. 1220-1228 ◽  
Author(s):  
Natalya V. Anufrieva ◽  
Nicolai G. Faleev ◽  
Elena A. Morozova ◽  
Natalia P. Bazhulina ◽  
Svetlana V. Revtovich ◽  
...  
Keyword(s):  
Active Site ◽  
Citrobacter Freundii ◽  
Active Site Tyrosine

scholarly journals The Role of the Active Site Tyrosine in the Mechanism of Lytic Polysaccharide Monooxygenase

2020 ◽  
Author(s):  
Aina McEvoy ◽  
Joel Creutzberg ◽  
Raushan Kumar Singh ◽  
Morten J. Bjerrum ◽  
Erik Hedegård
Keyword(s):  
Active Site ◽  
Density Functional ◽  
Renewable Resource ◽  
Lytic Polysaccharide Monooxygenase ◽  
Functional Theory ◽  
Polysaccharide Monooxygenases ◽  
Active Site Tyrosine ◽  
The Difference ◽  
First Time

Natural polysaccharides (such as cellulose) comprise a large bio-renewable resource. However, exploitation of this resource requires energy-efficient polysaccharide degradation, which is currently limited by the inherent recalcitrance of many naturally occurring polysaccharides. Catalytic breakdown of polysaccharides can be achieved more efficiently by means of the enzymes lytic polysaccharide monooxygenases (LPMOs). However, the LPMO mechanism has remained controversial, preventing full exploitation of their potential. One of the controversies has centered around an active site tyrosine, present in most LPMOs. Different roles for this tyrosine have been proposed without direct evidence, but two recent investigations have for the first time obtained direct (spectroscopic) evidence for that chemical modification of this tyrosine is possible. Surprisingly, the spectroscopic features obtained in the two investigations are remarkably different. In this paper we use density functional theory (DFT) in a QM/MM formulation to reconcile these (apparently) conflicting results. By modeling the spectroscopy as well as the underlying reaction mechanism we can show how formation of two isomers (both involving deprotonation of tyrosine) explain the difference in the experimental observed spectroscopic features. The link between our structures and the observed spectroscopy provides a firm ground to investigate the role of tyrosine.

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