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Asp-49 is not an absolute prerequisite for the enzymic activity of low-M(r) phospholipases A2: purification, characterization and computer modelling of an enzymically active Ser-49 phospholipase A2, ecarpholin S, from the venom of Echis carinatus sochureki (saw-scaled viper).

Several studies have shown that Asp-49 is the residue that controls calcium binding in, and so plays a critical role in the calcium-mediated activation of, low-M(r) group I-III phospholipases A2 (PLA2s). The present paper provides experimental evidence that Asp-49 is not an absolute prerequisite for...

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Autori principali: Polgár, J, Magnenat, E M, Peitsch, M C, Wells, T N, Clemetson, K J
Natura: Artigo
Lingua:Inglês
Pubblicazione: 1996
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC1217882/
https://ncbi.nlm.nih.gov/pubmed/8921006
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