Banerjee, Shrijita and Ekka, Mary Krishna and Kumaran, Sangaralingam (2011) Comparative thermodynamic studies on substrate and product binding of O-acetylserine sulfhydrylase reveals two different ligand recognition modes. BMC biochemistry, 12. p. 31. ISSN 1471-2091
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Abstract
We show that OASS from three different pathogenic bacteria bind substrate and product through two different mechanisms. Results indicate that predominantly entropy driven methionine binding is not mediated through classical hydrophobic binding, instead, may involve desolvation of the polar active site. We speculate that OASS in general, may exhibit two different binding mechanisms for recognizing substrates and products.
| Item Type: | Article |
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| Additional Information: | OPEN ACCESS |
| Uncontrolled Keywords: | Ligand Binding, Enthalpy, Entropy, Fluorescence, Isothermal Titration Calorimetry |
| Subjects: | Q Science > QD Chemistry |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 09 Dec 2011 06:55 |
| Last Modified: | 29 Mar 2012 10:05 |
| URI: | http://crdd.osdd.net/open/id/eprint/465 |
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