Aerospace series. Delegated Product Release Verification

2017 ◽  
Keyword(s):  
2021 ◽  
Vol 569 ◽  
pp. 66-71
Author(s):  
Shigeru Shimamoto ◽  
Yusuke Nakagawa ◽  
Yuji Hidaka ◽  
Takahiro Maruno ◽  
Yuji Kobayashi ◽  
...  

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Lingmin Yuan ◽  
Zongyang Lv ◽  
Melanie J. Adams ◽  
Shaun K. Olsen

AbstractE1 enzymes function as gatekeepers of ubiquitin (Ub) signaling by catalyzing activation and transfer of Ub to tens of cognate E2 conjugating enzymes in a process called E1–E2 transthioesterification. The molecular mechanisms of transthioesterification and the overall architecture of the E1–E2–Ub complex during catalysis are unknown. Here, we determine the structure of a covalently trapped E1–E2–ubiquitin thioester mimetic. Two distinct architectures of the complex are observed, one in which the Ub thioester (Ub(t)) contacts E1 in an open conformation and another in which Ub(t) instead contacts E2 in a drastically different, closed conformation. Altogether our structural and biochemical data suggest that these two conformational states represent snapshots of the E1–E2–Ub complex pre- and post-thioester transfer, and are consistent with a model in which catalysis is enhanced by a Ub(t)-mediated affinity switch that drives the reaction forward by promoting productive complex formation or product release depending on the conformational state.


Nanoscale ◽  
2019 ◽  
Vol 11 (11) ◽  
pp. 4854-4863 ◽  
Author(s):  
Zijie Zhang ◽  
Yuqing Li ◽  
Xiaohan Zhang ◽  
Juewen Liu

Molecular imprinting accelerates nanozyme catalysis and improves specificity attributable to selective adsorption of imprinted substrate, decreasing activation energy and facilitating product release.


2006 ◽  
Vol 348 (3) ◽  
pp. 229-242 ◽  
Author(s):  
J.Y. Colle ◽  
J.-P. Hiernaut ◽  
D. Papaioannou ◽  
C. Ronchi ◽  
A. Sasahara

1974 ◽  
Vol 141 (3) ◽  
pp. 817-824 ◽  
Author(s):  
Keith R. F. Elliott ◽  
Keith F. Tipton

A study of the product-inhibition patterns of carbamoyl phosphate synthetase from bovine liver is reported. Inhibition by adenosine, AMP and inorganic ions is also reported. The results are in agreement with the previously proposed model in which the order of substrate binding is ATPMg, followed by HCO3−, ATPMg and NH4+. The order of product release on the basis of the reported results is carbamoyl phosphate, followed by ADPMg, ADPMg and inorganic phosphate.


2011 ◽  
Vol 100 (3) ◽  
pp. 117a
Author(s):  
William C. Unrath ◽  
Pallavi Penumetcha ◽  
Darshan Trivedi ◽  
Christopher M. Yengo
Keyword(s):  
Myosin V ◽  

Sign in / Sign up

Export Citation Format

Share Document