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Amide-type local anesthetics action on the sarcoplasmic reticulum Ca-ATPase from fast-twitch skeletal muscle.

Di Croce DE1, Trinks PW, de La Cal C, Sánchez GA, Takara D.
Naunyn-Schmiedeberg's archives of pharmacology.Naunyn Schmiedebergs Arch Pharmacol.2014 Jun 20. [Epub ahead of print]
Myotoxic effects related to intracellular Ca2+ disturbances have been reported for local anesthetics. Such effects might derive from Ca-ATPase dysfunction. The aim of this work was to describe the effect of lidocaine and bupivacaine on the sarcoplasmic reticulum (SR) Ca-ATPase from fast-twitch skele
PMID 24947868

Hydrolysis of DFP and the nerve agent (S)-sarin by DFPase proceeds along two different reaction pathways: implications for engineering bioscavengers.

Wymore T1, Field MJ, Langan P, Smith JC, Parks JM.
The journal of physical chemistry. B.J Phys Chem B.2014 May 1;118(17):4479-89. doi: 10.1021/jp410422c. Epub 2014 Apr 21.
Organophosphorus (OP) nerve agents such as (S)-sarin are among the most highly toxic compounds that have been synthesized. Engineering enzymes that catalyze the hydrolysis of nerve agents ("bioscavengers") is an emerging prophylactic approach to diminish their toxic effects. Although its native func
PMID 24720808

Crystal structure of thermostable p-nitrophenylphosphatase from Bacillus Stearothermophilus (Bs-TpNPPase).

Guo Z, Wang F, Shen T, Huang J, Wang Y, Ji C1.
Protein and peptide letters.Protein Pept Lett.2014 May;21(5):483-9.
Thermostable p-nitrophenylphosphatase from Bacillus Stearothermophilus (Bs-TpNPPase) is involved in the Mg(2+)-dependent hydrolysis of the phosphoenzyme at an optimum reaction temperature of 55°C. Bs-TpNPPase has been cloned and overexpressed in the E.coli M15 strain. Based on the conserved active
PMID 24256105

Stable Structural Analog of Ca^<2+>-ATPase ADP-insensitive Phosphoenzyme with Occluded Ca^<2+> Formed by Elongation of A-domain/M1′-linker and Beryllium Fluoride Binding

大保貴嗣,Danko Stefania,Yamasaki Kazuo,Suzuki Hiroshi
Journal of Biological Chemistry 285(32), 24538-24547, 2010
… © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.We have developed a stable analog for the ADP-insensitive phosphoenzyme intermediate with two occluded Ca^<2+> … This is normally a transient intermediate state during phosphoenzyme isomerization from the ADP-sensitive to ADP-insensitive form and Ca^<2+> …
NAID 120004606780

Ca^<2+> Release to Lumen from ADP-sensitive Phosphoenzyme E1PCa_2 without Bound K^+ of Sarcoplasmic Reticulum Ca^<2+>-ATPase

山崎和生,Daiho Takashi,Danko Stefania,Suzuki Hiroshi
Journal of Biological Chemistry 285(49), 38674-38683, 2010
… transport by sarcoplasmic reticulum Ca^<2+>-ATPase, the conformation change of ADP-sensitive phosphoenzyme (E1PCa_2) to ADP-insensitive phosphoenzyme (E2PCa_2) is followed by rapid Ca^<2+> … These findings show that bound K^+ is critical for stabilizing both E1PCa_2 and E2P structures, thereby contributing to the structural changes that efficiently couple phosphoenzyme processing and Ca^<2+> …
NAID 120004606774

Roles of Tyr122-hydrophobic cluster and K+ binding in Ca2+ -releasing process of ADP-insensitive phosphoenzyme of sarcoplasmic reticulum Ca2+ -ATPase

YAMASAKI K
Journal of Biological Chemistry 283(43), 29144-29155, 2008-10
… We have previously found that Y122-HC plays critical roles in the processing of ADP-insensitive phosphoenzyme (E2P) after its formation by the isomerization from ADP-sensitive phosphoenzyme (E1PCa(2)) (Wang, G., Yamasaki, K., Daiho, T., and Suzuki, H. …
NAID 80019885824