Faculty Opinions recommendation of Essential role of an active-site guanine in glmS ribozyme catalysis.

Author(s):  
Robert Batey
Inorganics ◽  
2019 ◽  
Vol 7 (11) ◽  
pp. 131
Author(s):  
Michael J. Maroney ◽  
Stefano Ciurli

Following the discovery of the first specific and essential role of nickel in biology in 1975 (the dinuclear active site of the enzyme urease) [...]


2007 ◽  
Vol 129 (48) ◽  
pp. 14858-14859 ◽  
Author(s):  
Daniel J. Klein ◽  
Michael D. Been ◽  
Adrian R. Ferré-D'Amaré
Keyword(s):  

PLoS ONE ◽  
2015 ◽  
Vol 10 (2) ◽  
pp. e0117836 ◽  
Author(s):  
Eun Hye Lee ◽  
Kitaik Lee ◽  
Kwang Yeon Hwang ◽  
Hwa-Young Kim

Blood ◽  
2014 ◽  
Vol 123 (25) ◽  
pp. 3979-3987 ◽  
Author(s):  
Natalia Reglińska-Matveyev ◽  
Helena M. Andersson ◽  
Suely M. Rezende ◽  
Björn Dahlbäck ◽  
James T. B. Crawley ◽  
...  

Key Points The protein S SHBG-like domain and, more specifically, its LG1 subunit are important for binding and enhancement of TFPI. TFPI binding to the protein S SHBG-like domain likely positions TFPI Kunitz domain 2 for optimal interaction with the active site of FXa.


2005 ◽  
Vol 33 (1) ◽  
pp. 80-82 ◽  
Author(s):  
J. Cohen ◽  
K. Kim ◽  
M. Posewitz ◽  
M.L. Ghirardi ◽  
K. Schulten ◽  
...  

The [Fe]-hydrogenase enzymes are highly efficient H2 catalysts found in ecologically and phylogenetically diverse microorganisms, including the photosynthetic green alga, Chlamydomonas reinhardtii. Although these enzymes can occur in several forms, H2 catalysis takes place at a unique [FeS] prosthetic group or H-cluster, located at the active site. Significant to the function of hydrogenases is how the surrounding protein structure facilitates substrate-product transfer, and protects the active site H-cluster from inactivation. To elucidate the role of protein structure in O2 inactivation of [Fe]-hydrogenases, experimental and theoretical investigations have been performed. Molecular dynamics was used to comparatively investigate O2 and H2 diffusion in CpI ([Fe]-hydrogenase I from Clostridium pasteurianum). Our preliminary results suggest that H2 diffuses more easily and freely than O2, which is restricted to a small number of allowed pathways to and from the active site. These O2 pathways are located in the conserved active site domain, shown experimentally to have an essential role in active site protection.


2012 ◽  
Vol 50 (01) ◽  
Author(s):  
N Lange ◽  
S Sieber ◽  
A Erhardt ◽  
G Sass ◽  
HJ Kreienkamp ◽  
...  

1995 ◽  
Vol 74 (05) ◽  
pp. 1323-1328 ◽  
Author(s):  
Dominique Lasne ◽  
José Donato ◽  
Hervé Falet ◽  
Francine Rendu

SummarySynthetic peptides (TRAP or Thrombin Receptor Activating Peptide) corresponding to at least the first five aminoacids of the new N-terminal tail generated after thrombin proteolysis of its receptor are effective to mimic thrombin. We have studied two different TRAPs (SFLLR, and SFLLRN) in their effectiveness to induce the different platelet responses in comparison with thrombin. Using Indo-1/AM- labelled platelets, the maximum rise in cytoplasmic ionized calcium was lower with TRAPs than with thrombin. At threshold concentrations allowing maximal aggregation (50 μM SFLLR, 5 μM SFLLRN and 1 nM thrombin) the TRAPs-induced release reaction was about the same level as with thrombin, except when external calcium was removed by addition of 1 mM EDTA. In these conditions, the dense granule release induced by TRAPs was reduced by over 60%, that of lysosome release by 75%, compared to only 15% of reduction in the presence of thrombin. Thus calcium influx was more important for TRAPs-induced release than for thrombin-induced release. At strong concentrations giving maximal aggregation and release in the absence of secondary mediators (by pretreatment with ADP scavengers plus aspirin), SFLLRN mobilized less calcium, with a fast return towards the basal level and induced smaller lysosome release than did thrombin. The results further demonstrate the essential role of external calcium in triggering sustained and full platelet responses, and emphasize the major difference between TRAP and thrombin in mobilizing [Ca2+]j. Thus, apart from the proteolysis of the seven transmembrane receptor, another thrombin binding site or thrombin receptor interaction is required to obtain full and complete responses.


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