Mössbauer Studies of the Formation and Reactivity of a Quasi-Stable Peroxo Intermediate of Stearoyl-Acyl Carrier Protein Δ9-Desaturase†

Biochemistry ◽  
1999 ◽  
Vol 38 (38) ◽  
pp. 12197-12204 ◽  
Author(s):  
John A. Broadwater ◽  
Catalina Achim ◽  
Eckard Münck ◽  
Brian G. Fox
Keyword(s):  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Mössbauer Studies ◽  
Δ9 Desaturase ◽  
Peroxo Intermediate

EXAFS and Mössbauer characterization of the Diiron(III) site in stearoyl-acyl carrier protein Δ9– desaturase

1998 ◽  
Vol 3 (4) ◽  
pp. 392-400 ◽  
Author(s):  
Lijin Shu ◽  
John A. Broadwater ◽  
Catalina Achim ◽  
Brian G. Fox ◽  
Eckard Münck ◽  
...  
Keyword(s):  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Δ9 Desaturase

scholarly journals Some properties, including the substrate in vivo, of the Δ9-desaturase in Micrococcus cryophilus

1983 ◽  
Vol 209 (2) ◽  
pp. 345-353 ◽  
Author(s):  
M Foot ◽  
R Jeffcoat ◽  
N J Russell
Keyword(s):  
Desaturase Activity ◽  
Acyl Carrier Protein ◽  
Thiol Group ◽  
Carrier Protein ◽  
Psychrophilic Bacterium ◽  
Ph Optimum ◽  
Δ9 Desaturase ◽  
Membrane Bound ◽  
Delta 9 Desaturase

The delta 9-desaturase of the psychrophilic bacterium Micrococcus cryophilus is shown to be a membrane-bound enzyme that is probably linked to a cyanide- (and azide-) sensitive respiratory chain with oxygen as the final acceptor. It has a pH optimum of 8.7 and contains an essential thiol group, but has no special ion requirements. The desaturase activity of washed membranes could not be increased by adding supernatant or NADH and NADPH, possibly owing to the endogenous generation of reduced cofactors by the membranes. The substrate for the desaturase is not acyl-CoA and is probably not acyl-acyl-carrier protein. Evidence is presented that the substrate in vivo is saturated phospholipid and a scheme for the possible routes of incorporation of exogenous stearic acid into oleoyl-phospholipid is presented.

4-Aryl-1,4-Dihydropyridines as Potential Enoyl-Acyl Carrier Protein Reductase Inhibitors: Antitubercular Activity and Molecular Docking Study

2020 ◽  
Vol 20 ◽  
Author(s):  
Katharigatta N. Venugopala ◽  
Christophe Tratrat ◽  
Melendhran Pillay ◽  
Pran Kishore Deb ◽  
Deepak Chopra ◽  
...  
Keyword(s):  
Drug Resistance ◽  
Acyl Carrier Protein ◽  
Phenyl Group ◽  
Antitubercular Activity ◽  
Docking Study ◽  
Benzyl Ester ◽  
Multi Drug Resistance ◽  
Carrier Protein ◽  
Molecular Docking Study ◽  
Lipinski’S Rule

Background: Tuberculosis remains one of the most deadly infectious diseases worldwide due to the emergence of multi-drug resistance (MDR) and extensively drug resistance (XDR) strains of Mycobacterium tuberculosis (MTB). Materials and Methods: Herein, the screening of a total of eight symmetrical 1,4-dihydropyridine (1,4-DHP) derivatives (4a-4h) was carried out for whole-cell anti-TB activity against the susceptible H37Rv and MDR strains of MTB. Results and Discussion: Most of the compounds exhibited moderate to excellent activity against the susceptible H37Rv. Moreover, the most promising compound 4f (against H37Rv) having para-trifluoromethyl phenyl group at 4-position and bis para-methoxy benzyl ester group at 3- and 5-positions of 1,4-dihydropyridine pharmacophore, exhibited no toxicity, but demonstrated weak activity against MTB strains resistant to isoniazid and rifampicin. In light of the inhibitory profile of the title compounds, enoyl-acyl carrier protein reductase (InhA) appeared to be the appropriate molecular target. Docking study of these derivatives against InhA receptor revealed favorable binding interactions. Further, in silico predicted ADME properties of these compounds 4a-4h were found to be in the acceptable ranges including satisfactory Lipinski’s rule of five, thereby indicating their potential as drug-like molecules. Conclusion: In particular, the 1,4-DHP derivative 4f can be considered as an attractive lead molecule for further exploration and development of more potent anti-TB agents as InhA inhibitors.

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