Aerospace series. Delegated Product Release Verification

2017 ◽  
Keyword(s):  
Product Release

Substrate-induced product-release mechanism of lipocalin-type prostaglandin D synthase

2021 ◽  
Vol 569 ◽  
pp. 66-71
Author(s):  
Shigeru Shimamoto ◽  
Yusuke Nakagawa ◽  
Yuji Hidaka ◽  
Takahiro Maruno ◽  
Yuji Kobayashi ◽  
...  
Keyword(s):  
Release Mechanism ◽  
Product Release ◽  
Prostaglandin D Synthase

scholarly journals Crystal structures of an E1–E2–ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Lingmin Yuan ◽  
Zongyang Lv ◽  
Melanie J. Adams ◽  
Shaun K. Olsen
Keyword(s):  
Complex Formation ◽  
Crystal Structures ◽  
Molecular Mechanisms ◽  
Conformational State ◽  
Biochemical Data ◽  
Conformational States ◽  
Product Release ◽  
Closed Conformation ◽  
Open Conformation ◽  
Conjugating Enzymes

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.

Molecularly imprinted nanozymes with faster catalytic activity and better specificity

Nanoscale ◽  
2019 ◽  
Vol 11 (11) ◽  
pp. 4854-4863 ◽  
Author(s):  
Zijie Zhang ◽  
Yuqing Li ◽  
Xiaohan Zhang ◽  
Juewen Liu
Keyword(s):  
Activation Energy ◽  
Catalytic Activity ◽  
Molecular Imprinting ◽  
Selective Adsorption ◽  
Molecularly Imprinted ◽  
Product Release

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

Fission product release in high-burn-up UO2 oxidized to U3O8

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

scholarly journals Product inhibition studies on bovine liver carbamoyl phosphate synthetase

1974 ◽  
Vol 141 (3) ◽  
pp. 817-824 ◽  
Author(s):  
Keith R. F. Elliott ◽  
Keith F. Tipton
Keyword(s):  
Inorganic Phosphate ◽  
Substrate Binding ◽  
Inorganic Ions ◽  
Bovine Liver ◽  
Product Inhibition ◽  
Carbamoyl Phosphate Synthetase ◽  
Carbamoyl Phosphate ◽  
Product Release ◽  
Proposed Model ◽  
Inhibition Studies

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.

scholarly journals The HCM Loop Plays a Role in Actin-Activated Product Release in Myosin V

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