Lei Wei

TL;DR: The structure reveals the determinants of substrate preference for tyrosine rather than serine or threonine and a novel autoinhibition mechanism whereby one of the tyrosines that is autophosphorylated in response to insulin, Tyr 1,162, is bound in the active site.

TL;DR: Observations provide strong evidence that ACE possesses two independent catalytic domains and suggest that they may have different functions.

TL;DR: Current understanding of the molecular mechanisms underlying DOX-induced cardiomyocyte death, including the major primary mechanism of excess production of reactive oxygen species (ROS) and other recently discovered ROS-independent mechanisms are focused on.

TL;DR: The substrate specificity of the two active sites of ACE was compared using wild-type recombinant ACE and mutants, where one active site is suppressed by deletion or inactivated by mutations of 2 histidines coordinating an essential zinc atom, and suggests physiologically important differences between the subsites of theTwo active centers, and different substrate specificity, despite the high degree of sequence homology.

TL;DR: The present study shows that both the N and C domains of ACE contain a high affinity inhibitor binding site, and the different inhibitor binding properties of the two domains observed provide strong evidence for the presence of structural differences between the two active sites of ACE.