Saccharopolyspora hirsuta 367 encodes clustered genes similar to ketoacyl synthase, ketoacyl reductase, acyl carrier protein, and biotin carboxyl carrier protein

1993 ◽  
Vol 240 (1) ◽  
pp. 146-150 ◽  
Author(s):  
Christian Le Gouill ◽  
Danielle Desmarais ◽  
Claude V. Déry
Keyword(s):  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Biotin Carboxyl Carrier Protein ◽  
Ketoacyl Synthase ◽  
Saccharopolyspora Hirsuta

Acyl carrier protein (ACP) inhibition and other differences between β-ketoacyl synthase (KAS) I and II

2000 ◽  
Vol 28 (6) ◽  
pp. 607-610 ◽  
Author(s):  
K. Arnvig McGuire ◽  
J. N. McGuire ◽  
P. von Wettstein-Knowles
Keyword(s):  
Transfer Reaction ◽  
Acyl Carrier Protein ◽  
Laser Desorption ◽  
Acid Synthesis ◽  
Carrier Protein ◽  
Binding Affinities ◽  
Laser Desorption Ionization ◽  
Physiological Concentration ◽  
Ionization Time ◽  
Ketoacyl Synthase

Escherichia coli β-ketoacyl synthases (KAS) I and II carry out the elongation steps in fatty acid synthesis. Analyses using the cross-linker BSa [bis(sulphosuccinimidyl) suberate] and surfaceenhanced laser desorption/ionization-time-offlight MS disclosed only monomeric and dimeric forms of KAS II, whereas KAS I also forms higher multimers. The binding affinities for KAS I and KAS II to C14-acyl carrier protein (ACP) as well as for C14-ACP to KAS I and KAS II were determined. KAS I is sensitive to the ACP released during the transfer reaction, with 50% inhibition at 0.17 μM ACP close to the physiological concentration of ACP (0.13 μM). KAS I and II also differ in carrying out the decarboxylation step of the elongation reaction.

scholarly journals Acyl Carrier Protein Cyanylation Delivers a Ketoacyl Synthase–Carrier Protein Cross-Link

Biochemistry ◽  
2017 ◽  
Vol 56 (20) ◽  
pp. 2533-2536 ◽  
Author(s):  
Grace A. R. Thiele ◽  
Connie P. Friedman ◽  
Kathleen J. S. Tsai ◽  
Joris Beld ◽  
Casey H. Londergan ◽  
...  
Keyword(s):  
Acyl Carrier Protein ◽  
Carrier Protein ◽  
Cross Link ◽  
Ketoacyl Synthase

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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