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Comparative thermodynamic studies on substrate and product binding of O-acetylserine sulfhydrylase reveals two different ligand recognition modes.

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Comparative thermodynamic studies on substrate and product binding of O-acetylserine sulfhydrylase reveals two different ligand recognition modes.
 
Creator Banerjee, Shrijita
Ekka, Mary Krishna
Kumaran, Sangaralingam
 
Subject QD Chemistry
 
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.
 
Publisher Biomedcentral
 
Date 2011
 
Type Article
PeerReviewed
 
Format application/pdf
 
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
 
Relation http://www.biomedcentral.com/content/pdf/1471-2091-12-31.pdf
http://crdd.osdd.net/open/465/