Active site arginine controls the stereochemistry of hydride transfer in cyclohexanone monooxygenase

2018 ◽  
Vol 659 ◽  
pp. 47-56 ◽  
Author(s):  
Osei Boakye Fordwour ◽  
Kirsten R. Wolthers
Keyword(s):  
Active Site ◽  
Hydride Transfer ◽  
Cyclohexanone Monooxygenase

scholarly journals Crystal Structure of the FAD-Containing Ferredoxin-NADP+Reductase from the Plant PathogenXanthomonas axonopodispv. citri

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
María Laura Tondo ◽  
Ramon Hurtado-Guerrero ◽  
Eduardo A. Ceccarelli ◽  
Milagros Medina ◽  
Elena G. Orellano ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Transfer Process ◽  
Plant Pathogen ◽  
Active Site ◽  
Functional Divergence ◽  
Hydride Transfer ◽  
Citrus Canker ◽  
Xanthomonas Axonopodis ◽  
C Terminus

We have solved the structure of ferredoxin-NADP(H) reductase, FPR, from the plant pathogenXanthomonas axonopodispv. citri, responsible for citrus canker, at a resolution of 1.5 Å. This structure reveals differences in the mobility of specific loops when compared to other FPRs, probably unrelated to the hydride transfer process, which contributes to explaining the structural and functional divergence between the subclass I FPRs. Interactions of the C-terminus of the enzyme with the phosphoadenosine of the cofactor FAD limit its mobility, thus affecting the entrance of nicotinamide into the active site. This structure opens the possibility of rationally designing drugs against theX. axonopodispv. citri phytopathogen.

A predictive active site model for the cyclohexanone monooxygenase catalyzed oxidation of sulfides to chiral sulfoxides

1995 ◽  
Vol 6 (6) ◽  
pp. 1375-1386 ◽  
Author(s):  
Gianluca Ottolina ◽  
Piero Pasta ◽  
Giacomo Carrea ◽  
Stefano Colonna ◽  
Sabrina Dallavalle ◽  
...  
Keyword(s):  
Active Site ◽  
Cyclohexanone Monooxygenase ◽  
Site Model ◽  
Oxidation Of Sulfides ◽  
Chiral Sulfoxides ◽  
Active Site Model ◽  
Catalyzed Oxidation

scholarly journals Structure and function of yeast alcohol dehydrogenase

2000 ◽  
Vol 65 (4) ◽  
pp. 207-227 ◽  
Author(s):  
Svetlana Trivic ◽  
Vladimir Leskovac
Keyword(s):  
Alcohol Dehydrogenase ◽  
Substrate Specificity ◽  
Primary Structure ◽  
Active Site ◽  
Hydride Transfer ◽  
Kinetic Mechanism ◽  
Structure And Function ◽  
Chemical Mechanism ◽  
And Function ◽  
Font Color

1. Introduction 2. Isoenzymes of YADH 3. Substrate specificity 4. Kinetic mechanism 5. Primary structure 6. The active site 7. Mutations in the yeast enzyme 8. Chemical mechanism 9. Binding of coenzymes 10. Hydride transfer <br><br><font color="red"><b> This article has been corrected. Link to the correction <u><a href="http://dx.doi.org/10.2298/JSC0008609E">10.2298/JSC0008609E</a><u></b></font>

scholarly journals The influence of active site conformations on the hydride transfer step of the thymidylate synthase reaction mechanism

2015 ◽  
Vol 17 (46) ◽  
pp. 30793-30804 ◽  
Author(s):  
Katarzyna Świderek ◽  
Amnon Kohen ◽  
Vicent Moliner
Keyword(s):  
Reaction Mechanism ◽  
Thymidylate Synthase ◽  
Active Site ◽  
Hydride Transfer ◽  
Md Simulations ◽  
Concerted Mechanism ◽  
X Ray ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Rate Limiting

QM/MM MD simulations from different X-ray structures support the concerted mechanism character in the rate limiting step of thymidylate synthase catalysis.

scholarly journals Mg2+ Binds to the Surface of Thymidylate Synthase and Affects Hydride Transfer at the Interior Active Site

2013 ◽  
Vol 135 (20) ◽  
pp. 7583-7592 ◽  
Author(s):  
Zhen Wang ◽  
Paul J. Sapienza ◽  
Thelma Abeysinghe ◽  
Calvin Luzum ◽  
Andrew L. Lee ◽  
...  
Keyword(s):  
Thymidylate Synthase ◽  
Active Site ◽  
Hydride Transfer

Active site model of cyclohexanone monooxygenase. 3. The case of benzyl sulfides bearing polar groups

1996 ◽  
Vol 7 (12) ◽  
pp. 3427-3430 ◽  
Author(s):  
Gianluca Ottolina ◽  
Piero Pasta ◽  
David Varley ◽  
Herbert L. Holland
Keyword(s):  
Active Site ◽  
Cyclohexanone Monooxygenase ◽  
Site Model ◽  
Polar Groups ◽  
Active Site Model

scholarly journals Structural characterization of tartrate dehydrogenase: a versatile enzyme catalyzing multiple reactions

2010 ◽  
Vol 66 (6) ◽  
pp. 673-684 ◽  
Author(s):  
Radhika Malik ◽  
Ronald E. Viola
Keyword(s):  
Active Site ◽  
Metal Ion ◽  
Substrate Binding ◽  
Hydride Transfer ◽  
Divalent Metal ◽  
Ammonium Ion ◽  
Hydroxyl Group ◽  
Metal Ion Binding ◽  
Cofactor Binding ◽  
Divalent Metal Ion

The first structure of an NAD-dependent tartrate dehydrogenase (TDH) has been solved to 2 Å resolution by single anomalous diffraction (SAD) phasing as a complex with the intermediate analog oxalate, Mg2+and NADH. This TDH structure fromPseudomonas putidahas a similar overall fold and domain organization to other structurally characterized members of the hydroxy-acid dehydrogenase family. However, there are considerable differences between TDH and these functionally related enzymes in the regions connecting the core secondary structure and in the relative positioning of important loops and helices. The active site in these complexes is highly ordered, allowing the identification of the substrate-binding and cofactor-binding groups and the ligands to the metal ions. Residues from the adjacent subunit are involved in both the substrate and divalent metal ion binding sites, establishing a dimer as the functional unit and providing structural support for an alternating-site reaction mechanism. The divalent metal ion plays a prominent role in substrate binding and orientation, together with several active-site arginines. Functional groups from both subunits form the cofactor-binding site and the ammonium ion aids in the orientation of the nicotinamide ring of the cofactor. A lysyl amino group (Lys192) is the base responsible for the water-mediated proton abstraction from the C2 hydroxyl group of the substrate that begins the catalytic reaction, followed by hydride transfer to NAD. A tyrosyl hydroxyl group (Tyr141) functions as a general acid to protonate the enolate intermediate. Each substrate undergoes the initial hydride transfer, but differences in substrate orientation are proposed to account for the different reactions catalyzed by TDH.

scholarly journals The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer

2010 ◽  
Vol 46 (47) ◽  
pp. 8974 ◽  
Author(s):  
Vanja Stojković ◽  
Laura L. Perissinotti ◽  
Jeeyeon Lee ◽  
Stephen J. Benkovic ◽  
Amnon Kohen
Keyword(s):  
Active Site ◽  
Hydride Transfer
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