Angiotensin II-Forming Activity in a Reconstructed Ancestral Chymase
Chymase
TMPRSS6
DOI:
10.1126/science.271.5248.502
Publication Date:
2006-10-27T18:30:41Z
AUTHORS (5)
ABSTRACT
The current model of serine protease diversity theorizes that the earliest molecules were simple digestive enzymes gained complex regulatory functions and restricted substrate specificities through evolution. Among chymase group proteases are convert angiotensin I to II, as well others simply degrade angiotensins. An ancestral reconstructed with use phylogenetic inference, total gene synthesis, protein expression had efficient specific II-forming activity (turnover number, about 700 per second). Thus, is more primitive state for chymases, loss such occurred later in evolution some these proteases.
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