Comparative thermodynamic studies on substrate and product binding of O-acetylserine sulfhydrylase reveals two different ligand recognition modes.
IR@IMTECH: CSIR-Institute of Microbial Technology, Chandigarh
View Archive Info| Field | Value | |
| Title |
Comparative thermodynamic studies on substrate and product binding of O-acetylserine sulfhydrylase reveals two different ligand recognition modes.
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| Creator |
Banerjee, Shrijita
Ekka, Mary Krishna Kumaran, Sangaralingam |
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| Subject |
QD Chemistry
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| Description |
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.
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| Publisher |
Biomedcentral
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| Date |
2011
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| Type |
Article
PeerReviewed |
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| Format |
application/pdf
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| Identifier |
http://crdd.osdd.net/open/465/1/kumaran11.pdf
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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| Relation |
http://www.biomedcentral.com/content/pdf/1471-2091-12-31.pdf
http://crdd.osdd.net/open/465/ |
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