scholarly journals Catalytic mechanism of the colistin resistance protein MCR-1

2021 ◽  
Author(s):  
Reynier Suardíaz ◽  
Emily Lythell ◽  
Philip Hinchliffe ◽  
Marc van der Kamp ◽  
James Spencer ◽  
...  
Keyword(s):  
Reaction Mechanism ◽  
Antimicrobial Resistance ◽  
Dft Calculations ◽  
Catalytic Reaction ◽  
Catalytic Mechanism ◽  
Cluster Models ◽  
Colistin Resistance ◽  
Resistance Protein ◽  
Catalytic Reaction Mechanism

Elucidation of the catalytic reaction mechanism of MCR-1 enzyme, responsible for the antimicrobial resistance to colistin, using DFT calculations on cluster models.

scholarly journals Catalytic Mechanism of the Colistin Resistance Protein MCR-1

2020 ◽  
Author(s):  
Reynier Suardiaz ◽  
Emily Lythell ◽  
Philip Hinchliffed ◽  
Marc van der Kamp ◽  
James Spencer ◽  
...  
Keyword(s):  
Reaction Mechanism ◽  
Lipid A ◽  
Catalytic Mechanism ◽  
Second Step ◽  
Colistin Resistance ◽  
Membrane Bound ◽  
Resistance Protein ◽  
Phosphoethanolamine Transferases ◽  
Bacterial Lipid ◽  
Rate Limiting

<div> <div> <div> <p>The mcr-1 gene encodes a membrane-bound Zn2+-metalloenzyme, MCR-1, which catalyzes phosphoethanolamine transfer onto bacterial lipid A, making bacteria resistant to colistin, a last-resort antibiotic. Mechanistic understanding of this process remains incomplete. Here, we investigate possible catalytic pathways using DFT and ab initio calculations on cluster models and identify a complete two-step reaction mechanism. The first step, formation of a covalent phosphointermediate via trans-fer of phosphoethanolamine from a membrane phospholipid donor to the acceptor Thr285, is rate-limiting and proceeds with a single Zn2+ ion. The second step, transfer of the phosphoethanolamine group to lipid A, requires an additional Zn2+. The calculations suggest the involment of the Zn2+ orbitals directly in the reaction is limited, with the second Zn2+ acting to bind incoming lipid A and direct phosphoethanolamine addition. The new level of mechanistic detail obtained here, which distinguishes these enzymes from other phosphotransferases, will aid in the development of inhibitors specific to MCR-1 and related bacterial phosphoethanolamine transferases. </p> </div> </div> </div>

scholarly journals Catalytic Mechanism of the Colistin Resistance Protein MCR-1

2020 ◽  
Author(s):  
Reynier Suardiaz ◽  
Emily Lythell ◽  
Philip Hinchliffed ◽  
Marc van der Kamp ◽  
James Spencer ◽  
...  
Keyword(s):  
Reaction Mechanism ◽  
Lipid A ◽  
Catalytic Mechanism ◽  
Second Step ◽  
Colistin Resistance ◽  
Membrane Bound ◽  
Resistance Protein ◽  
Phosphoethanolamine Transferases ◽  
Bacterial Lipid ◽  
Rate Limiting

<div> <div> <div> <p>The mcr-1 gene encodes a membrane-bound Zn2+-metalloenzyme, MCR-1, which catalyzes phosphoethanolamine transfer onto bacterial lipid A, making bacteria resistant to colistin, a last-resort antibiotic. Mechanistic understanding of this process remains incomplete. Here, we investigate possible catalytic pathways using DFT and ab initio calculations on cluster models and identify a complete two-step reaction mechanism. The first step, formation of a covalent phosphointermediate via trans-fer of phosphoethanolamine from a membrane phospholipid donor to the acceptor Thr285, is rate-limiting and proceeds with a single Zn2+ ion. The second step, transfer of the phosphoethanolamine group to lipid A, requires an additional Zn2+. The calculations suggest the involment of the Zn2+ orbitals directly in the reaction is limited, with the second Zn2+ acting to bind incoming lipid A and direct phosphoethanolamine addition. The new level of mechanistic detail obtained here, which distinguishes these enzymes from other phosphotransferases, will aid in the development of inhibitors specific to MCR-1 and related bacterial phosphoethanolamine transferases. </p> </div> </div> </div>

Catalytic Reaction Mechanism of Mn-Doped Nanoporous Aluminophosphates for the Aerobic Oxidation of Hydrocarbons

2010 ◽  
Vol 16 (46) ◽  
pp. 13638-13645 ◽  
Author(s):  
Luis Gómez-Hortigüela ◽  
Furio Corà ◽  
Gopinathan Sankar ◽  
Claudio M. Zicovich-Wilson ◽  
C. Richard A. Catlow
Keyword(s):  
Reaction Mechanism ◽  
Catalytic Reaction ◽  
Aerobic Oxidation ◽  
Oxidation Of Hydrocarbons ◽  
Mn Doped ◽  
Catalytic Reaction Mechanism

scholarly journals Structural Analysis on the Catalytic Reaction Mechanism of AfcA Fucosidase from Bifidobacterium Bifidum

2008 ◽  
Vol 50 (2) ◽  
pp. 138-143
Author(s):  
Masamichi NAGAE ◽  
Atsuko TSUCHIYA ◽  
Kenji YAMAMOTO ◽  
Takane KATAYAMA ◽  
Soichi WAKATSUKI ◽  
...  
Keyword(s):  
Reaction Mechanism ◽  
Structural Analysis ◽  
Catalytic Reaction ◽  
Bifidobacterium Bifidum ◽  
Catalytic Reaction Mechanism

scholarly journals Theoretical Study of Catalytic Reaction Mechanism of CO with N2O by Cu+

2013 ◽  
Vol 25 (17) ◽  
pp. 9460-9464
Author(s):  
Dong-Ping Chen ◽  
Ke Gai ◽  
Chao Kong ◽  
Yan-Xia Han ◽  
Li-Jie Hou ◽  
...  
Keyword(s):  
Reaction Mechanism ◽  
Catalytic Reaction ◽  
Theoretical Study ◽  
Catalytic Reaction Mechanism
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