scholarly journals The eukaryotic tRNA-guanine transglycosylase enzyme inserts queuine into tRNA via a sequential bi–bi mechanism

2020 ◽  
Vol 56 (27) ◽  
pp. 3915-3918
Author(s):  
Mashael A. Alqasem ◽  
Claire Fergus ◽  
J. Mike Southern ◽  
Stephen J. Connon ◽  
Vincent P. Kelly
Keyword(s):  
Mechanism Of Catalysis

The mechanism of catalysis associated with the human TGT enzyme has been elucidated and differs from that associated with its eubacterial counterpart.

Catalytic Activity of Binary and Triple Systems Based on Redox Inactive Metal Compound, LiSt and Additives of Monodentate Ligands-Modifiers: DMF, HMPA and PhOH, in Selective Ethylbenzene Oxidation with Dioxygen

2016 ◽  
Vol 10 (3) ◽  
pp. 259-270
Author(s):  
Ludmila Matienko ◽  
◽  
Larisa Mosolova ◽  
Vladimir Binyukov ◽  
Gennady Zaikov ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Triple System ◽  
Metal Compound ◽  
Ethylbenzene Oxidation ◽  
Catalytic Systems ◽  
Triple Systems ◽  
Lithium Compound ◽  
Mechanism Of Catalysis ◽  
Monodentate Ligands

Mechanism of catalysis with binary and triple catalytic systems based on redox inactive metal (lithium) compound {LiSt+L2} and {LiSt+L2+PhOH} (L2=DMF or HMPA), in the selective ethylbenzene oxidation by dioxygen into -phenylethyl hydroperoxide is researched. The results are compared with catalysis by nickel-lithium triple system {NiII(acac)2+LiSt+PhOH} in selective ethylbenzene oxidation to PEH. The role of H-bonding in mechanism of catalysis is discussed. The possibility of the stable supramolecular nanostructures formation on the basis of triple systems, {LiSt+L2+PhOH}, due to intermolecular H-bonds, is researched with the AFM method.

scholarly journals Kinetic and structural evidence for a sequential ordered Bi Bi mechanism of catalysis by Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase

1991 ◽  
Vol 266 (15) ◽  
pp. 9732-9739
Author(s):  
D.A. Rudnick ◽  
C.A. McWherter ◽  
W.J. Rocque ◽  
P.J. Lennon ◽  
D.P. Getman ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Mechanism Of Catalysis

scholarly journals Discovery of uncompetitive inhibitors of SapM that compromise intracellular survival of Mycobacterium tuberculosis

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Paulina Fernández-Soto ◽  
Joshua Casulli ◽  
Danilo Solano-Castro ◽  
Pablo Rodríguez-Fernández ◽  
Thomas A. Jowitt ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Francisella Tularensis ◽  
Virulence Factor ◽  
Chemical Properties ◽  
Full Potential ◽  
Mechanism Of Inhibition ◽  
Physico Chemical ◽  
Microbial Infections ◽  
Mechanism Of Catalysis ◽  
Antivirulence Agents

AbstractSapM is a secreted virulence factor from Mycobacterium tuberculosis critical for pathogen survival and persistence inside the host. Its full potential as a target for tuberculosis treatment has not yet been exploited because of the lack of potent inhibitors available. By screening over 1500 small molecules, we have identified new potent and selective inhibitors of SapM with an uncompetitive mechanism of inhibition. The best inhibitors share a trihydroxy-benzene moiety essential for activity. Importantly, the inhibitors significantly reduce mycobacterial burden in infected human macrophages at 1 µM, and they are selective with respect to other mycobacterial and human phosphatases. The best inhibitor also reduces intracellular burden of Francisella tularensis, which secretes the virulence factor AcpA, a homologue of SapM, with the same mechanism of catalysis and inhibition. Our findings demonstrate that inhibition of SapM with small molecule inhibitors is efficient in reducing intracellular mycobacterial survival in host macrophages and confirm SapM as a potential therapeutic target. These initial compounds have favourable physico-chemical properties and provide a basis for exploration towards the development of new tuberculosis treatments. The efficacy of a SapM inhibitor in reducing Francisella tularensis intracellular burden suggests the potential for developing broad-spectrum antivirulence agents to treat microbial infections.

Mechanism of catalysis for the hydration of substituted styrene oxides by hepatic epoxide hydrase

1978 ◽  
Vol 187 (2) ◽  
pp. 290-298 ◽  
Author(s):  
Patrick M. Dansette ◽  
Vanya B. Makedonska ◽  
Donald M. Jerina
Keyword(s):  
Mechanism Of Catalysis

scholarly journals Catalysis of cataract-associated human γD crystallin aggregation via dynamic disulfide exchange

2018 ◽  
Author(s):  
Eugene Serebryany ◽  
Shuhuai Yu ◽  
Sunia A. Trauger ◽  
Bogdan Budnik ◽  
Eugene I. Shakhnovich
Keyword(s):  
Light Scattering ◽  
Disulfide Bond ◽  
Eye Lens ◽  
Lens Protein ◽  
Biochemical Mechanism ◽  
Wild Type ◽  
Disulfide Exchange ◽  
Mechanism Of Catalysis ◽  
Eye Lens Protein

AbstractSeveral mutations in human γD-crystallin (HγD), a long-lived eye lens protein, cause misfolding and aggregation, leading to cataract. Surprisingly, wild-type HγD catalyzes aggregation of its cataract related W42Q variant while itself remaining soluble – the inverse of the classical prion-like scenario whereby misfolded polypeptides catalyze aggregation of natively folded ones. The search for a biochemical mechanism of catalysis of W42Q aggregation by WT has revealed that WT HγD can transfer a disulfide bond to the W42Q variant. The transferred disulfide kinetically traps an aggregation-prone intermediate made accessible by the W42Q mutation, facilitating light-scattering aggregation of the W42Q variant. The aggregating variant thus becomes a disulfide sink, removing the disulfides from solution. Such redox “hot potato” competitions among wild-type and mutant or modified polypeptides may be relevant for many long-lived proteins that function in oxidizing environments. In these cases aggregation may be forestalled by inhibiting disulfide flow toward damaged polypeptides.

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