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Kinetic Determinants of the Interaction of Enoyl-ACP Reductase from Plasmodium falciparum with Its Substrates and Inhibitors

โœ Scribed by Mili Kapoor; M Jamal Dar; Avadhesha Surolia; Namita Surolia

Book ID
115589105
Publisher
Elsevier Science
Year
2001
Tongue
English
Weight
141 KB
Volume
289
Category
Article
ISSN
0006-291X

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๐Ÿ“œ SIMILAR VOLUMES

Effect of substrate binding loop mutatio
Effect of substrate binding loop mutations on the structure, kinetics, and inhibition of enoyl acyl carrier protein reductase from plasmodium falciparum
โœ Koustav Maity; Tanushree Banerjee; Narayanappa Prabakaran; Namita Surolia; Avadh ๐Ÿ“‚ Article ๐Ÿ“… 2011 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 713 KB

## Abstract Enoyl acyl carrier protein reductase (ENR), which catalyzes the final and rate limiting step of fatty acid elongation, has been validated as a potential drug target. Triclosan is known to be an effective inhibitor for this enzyme. We mutated the substrate binding site residue Ala372 of

Effect of substrate binding loop mutatio
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โœ Koustav Maity; Tanushree Banerjee; Narayanappa Prabakaran; Namita Surolia; Avadh ๐Ÿ“‚ Article ๐Ÿ“… 2011 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 104 KB

## Abstract PfENR A372M mutant showing a different conformation of Methionine compared to the Met206 of EcENR by Koustav Maity et al., pp 30โ€“41.