Modification of Lys-6 and Lys-65 Affects the Structural Stability of Taiwan Cobra Phospholipase A2 View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2006-02

AUTHORS

Long-Sen Chang, Yun-Ching Cheng, Ching-Ping Chen

ABSTRACT

To assess whether chemical modification of phospholipase A2 (PLA2) enzymes may affect their fine structure and consequently alter their enzymatic activity, the present study was carried out. Both Lys-6 and Lys-65 in the Taiwan cobra (Naja naja atra) PLA2 were selectively modified with trinitrobenzene sulfonate and pyridoxal-5′-phosphate (PLP), respectively. Incorporation of either trinitrophenylated (TNP) or PLP groups on Lys-6 and Lys-65 caused a drop in PLA2 activity, but the Ca2+-binding ability and global conformation of modified derivatives were not significantly different from that of native enzyme. A distinct enhancement of stability was observed with native PLA2 when thermal unfolding was conducted in the presence of 20 mM Ca2+. Conformational transition induced by guanidine hydrochloride was also attenuated by the addition of Ca2+. Conversely, a marked decrease in the structural stability was noted with modified derivatives, and the enhancing effect of Ca2+ pronouncedly decreased. Together with the finding that the incorporated TNP and PLP groups did not equally affect enzymatic activity and structural stability of PLA2, our data suggest that an alteration in the fine structure owing to the incorporated groups should contribute to the observed decrease in PLA2 activity. More... »

PAGES

127-134

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10930-006-0004-6

DOI

http://dx.doi.org/10.1007/s10930-006-0004-6

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1000193958

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16862455


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