scholarly journals Oxidation-State-Dependent Binding Properties of the Active Site in a Mo-Containing Formate Dehydrogenase

2017 ◽  
Vol 139 (29) ◽  
pp. 9927-9936 ◽  
Author(s):  
William E. Robinson ◽  
Arnau Bassegoda ◽  
Erwin Reisner ◽  
Judy Hirst
Keyword(s):  
Oxidation State ◽  
Active Site ◽  
Formate Dehydrogenase ◽  
Binding Properties ◽  
State Dependent

In silico assessment of kinetics and state dependent binding properties of drugs causing acquired LQTS

2016 ◽  
Vol 120 (1-3) ◽  
pp. 89-99 ◽  
Author(s):  
William Lee ◽  
Stefan A. Mann ◽  
Monique J. Windley ◽  
Mohammad S. Imtiaz ◽  
Jamie I. Vandenberg ◽  
...  
Keyword(s):  
In Silico ◽  
Binding Properties ◽  
State Dependent

A transient post-translational modification of active site cysteine alters binding properties of the parkinsonism protein DJ-1

2018 ◽  
Vol 504 (1) ◽  
pp. 328-333 ◽  
Author(s):  
Arman Mussakhmetov ◽  
Igor A. Shumilin ◽  
Raushan Nugmanova ◽  
Ivan G. Shabalin ◽  
Timur Baizhumanov ◽  
...  
Keyword(s):  
Active Site ◽  
Post Translational Modification ◽  
Binding Properties ◽  
Active Site Cysteine

scholarly journals Design and Characterisation of Inhibitory Peptides against Bleg1_2478, an Evolutionary Divergent B3 Metallo-β-lactamase

Molecules ◽  
2020 ◽  
Vol 25 (24) ◽  
pp. 5797
Author(s):  
Gayathri Selvaraju ◽  
Thean Chor Leow ◽  
Abu Bakar Salleh ◽  
Yahaya M. Normi
Keyword(s):  
Active Site ◽  
Protein Complexes ◽  
Hypothetical Protein ◽  
Titration Calorimetry ◽  
Binding Properties ◽  
Vitro Assay ◽  
In Silico Docking ◽  
Inhibitory Peptides ◽  
Catalytic Function

Previously, a hypothetical protein (HP) termed Bleg1_2437 (currently named Bleg1_2478) from Bacillus lehensis G1 was discovered to be an evolutionary divergent B3 subclass metallo-β-lactamase (MBL). Due to the scarcity of clinical inhibitors for B3 MBLs and the divergent nature of Bleg1_2478, this study aimed to design and characterise peptides as inhibitors against Bleg1_2478. Through in silico docking, RSWPWH and SSWWDR peptides with comparable binding energy to ampicillin were obtained. In vitro assay results showed RSWPWH and SSWWDR inhibited the activity of Bleg1_2478 by 50% at concentrations as low as 0.90 µM and 0.50 µM, respectively. At 10 µM of RSWPWH and 20 µM of SSWWDR, the activity of Bleg1_2478 was almost completely inhibited. Isothermal titration calorimetry (ITC) analyses showed slightly improved binding properties of the peptides compared to ampicillin. Docked peptide–protein complexes revealed that RSWPWH bound near the vicinity of the Bleg1_2478 active site while SSWWDR bound at the center of the active site itself. We postulate that the peptides caused the inhibition of Bleg1_2478 by reducing or blocking the accessibility of its active site from ampicillin, thus hampering its catalytic function.

scholarly journals Exploring Oxidation State-Dependent Selectivity in Polymerization of Cyclic Esters and Carbonates with Zinc(II) Complexes

iScience ◽  
2018 ◽  
Vol 7 ◽  
pp. 120-131 ◽  
Author(s):  
Mark Abubekerov ◽  
Vojtěch Vlček ◽  
Junnian Wei ◽  
Matthias E. Miehlich ◽  
Stephanie M. Quan ◽  
...  
Keyword(s):  
Oxidation State ◽  
Cyclic Esters ◽  
State Dependent

scholarly journals Overcoming Oxidation State-Dependent Spectral Interferences: Online Monitoring of U(VI) Reduction to U(IV) via Raman and UV–vis Spectroscopy

2020 ◽  
Vol 59 (19) ◽  
pp. 8894-8901 ◽  
Author(s):  
Amanda M. Lines ◽  
Gabriel B. Hall ◽  
Sergey Sinkov ◽  
Tatiana Levitskaia ◽  
Neal Gallagher ◽  
...  
Keyword(s):  
Oxidation State ◽  
Online Monitoring ◽  
Spectral Interferences ◽  
State Dependent ◽  
Vis Spectroscopy

scholarly journals The mechanism of action of dd-peptidases: the role of Threonine-299 and -301 in the Streptomyces R61 dd-peptidase

1994 ◽  
Vol 301 (2) ◽  
pp. 477-483 ◽  
Author(s):  
J M Wilkin ◽  
A Dubus ◽  
B Joris ◽  
J M Frère
Keyword(s):  
Amino Acids ◽  
Active Site ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Peptide Substrate ◽  
Binding Properties ◽  
Beta Lactamases ◽  
Penicillin Binding Proteins ◽  
Active Site Cavity

The side chains of residues Thr299 and Thr301 in the Streptomyces R61 DD-peptidase have been modified by site-directed mutagenesis. These amino acids are part of a beta-strand which forms a wall of the active-site cavity. Thr299 corresponds to the second residue of the Lys-Thr(Ser)-Gly triad, highly conserved in active-site beta-lactamases and penicillin-binding proteins (PBPs). Modification of Thr301 resulted only in minor alterations of the catalytic and penicillin-binding properties of the enzyme. No selective decrease of the rate of acylation was observed for any particular class of compounds. By contrast, the loss of the hydroxy group of the residue in position 299 yielded a seriously impaired enzyme. The rates of inactivation by penicillins were decreased 30-50-fold, whereas the reactions with cephalosporins were even more affected. The efficiency of hydrolysis against the peptide substrate was also seriously decreased. More surprisingly, the mutant was completely unable to catalyse transpeptidation reactions. The conservation of an hydroxylated residue in this position in PBPs is thus easily explained by these results.

Oxidation state dependent light sensitivity of a ferrocene/dihydroazulene conjugate

1990 ◽  
Vol 31 (22) ◽  
pp. 3113-3116 ◽  
Author(s):  
Jörg Daub ◽  
Sebastian Gierisch ◽  
Josef Salbeck
Keyword(s):  
Oxidation State ◽  
Light Sensitivity ◽  
State Dependent
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