نتایج جستجو برای: phosphoryl

تعداد نتایج: 1670  

Journal: :Eukaryotic cell 2012
Matthew L Fowler Cheryl Ingram-Smith Kerry S Smith

Acetate kinase (ACK) catalyzes the reversible synthesis of acetyl phosphate by transfer of the γ-phosphate of ATP to acetate. Here we report the first biochemical and kinetic characterization of a eukaryotic ACK, that from the protist Entamoeba histolytica. Our characterization revealed that this protist ACK is the only known member of the ASKHA structural superfamily, which includes acetate ki...

Journal: :Journal of bacteriology 2004
Knut Jahreis Tom B Morrison Andrés Garzón John S Parkinson

CheA is a multidomain histidine kinase for chemotaxis in Escherichia coli. CheA autophosphorylates through interaction of its N-terminal phosphorylation site domain (P1) with its central dimerization (P3) and ATP-binding (P4) domains. This activity is modulated through the C-terminal P5 domain, which couples CheA to chemoreceptor control. CheA phosphoryl groups are donated to two response regul...

Journal: :Journal of the American Chemical Society 2000
June M Messmore Ronald T Raines

Pentavalent organo-vanadates have been put forth as transition state analogues for a variety of phosphoryl transfer reactions. In particular, uridine 2',3'-cyclic vanadate (U>v) has been proposed to resemble the transition state during catalysis by ribonuclease A (RNase A). Here, this hypothesis is tested. Lys41 of RNase A is known to donate a hydrogen bond to a nonbridging phosphoryl oxygen in...

Journal: :Glycobiology 2012
Peng Zhang Huaiyu Hu

Genetic defects in like-glycosyltransferase (LARGE) cause congenital muscular dystrophy with central nervous system manifestations. The underlying molecular pathomechanism is the hypoglycosylation of α-dystroglycan (α-DG), which is evidenced by diminished immunoreactivity to IIH6C4 and VIA4-1, antibodies that recognize carbohydrate epitopes. Previous studies indicate that LARGE participates in ...

2012
Subhash C. Bihani Shree Kumar Apte Jean-Luc Ferrer Madhusoodan V. Hosur

Alkaline phosphatase (AP) is a bi-metalloenzyme with potential applications in biotechnology and bioremediation. The enzyme hydrolyses nonspecifically phosphate monoesters under alkaline conditions to yield inorganic phosphate. The AP isolated from the bacterium Sphingomonas sp. Strain BSAR-1 (SPAP) was shown to be particularly useful for the recovery of uranium from alkaline radioactive waste....

Journal: :Chemical communications 2012
Wenbo Xiao Cong-Ying Zhou Chi-Ming Che

[Ru(IV)(por)Cl(2)] (por = porphyrin dianion) can efficiently catalyze nitrene insertion into aldehyde C-H bonds with phosphoryl azides as a nitrene source to give N-acylphosphoramidates in good to high yields.

Journal: :Acta Crystallographica Section A Foundations of Crystallography 2004

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