330-13-2Relevant articles and documents
A Protease Mimic with Turnover Capabilities
Menger, F. M.,Whitesell, L. G.
, p. 707 - 708 (1985)
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Effect of hydrophobic interaction cooperating with double Lewis acid activation in a zinc(ii) phosphodiesterase mimic
Zhao, Meng,Zhang, Li,Chen, Huo-Yan,Wang, Han-Lu,Ji, Liang-Nian,Mao, Zong-Wan
, p. 6497 - 6499 (2010)
The novel dinuclear Zn(ii) complex (1) containing a β-CD dimer could accelerate BNPP (a DNA substitute) hydrolysis more efficiently than catalyze HPNP (a RNA substitute) transesterification with different mechanisms involved; the β-CDs played remarkably different roles.
An insight into phosphorylase mechanism from model study
Tafesse, Fikru,Eguzozie, Kennedy
, p. 826 - 830 (2010)
Mechanistic aspects of phosphorylation reaction that mimic phosphorylase enzymes have been studied in the biologically important middle pH region by utilizing nitrophenol as substrate and bistrimethylenediaminecobalt(III) phosphate complexes as the enzyme model. Significant phosphorylation was noted from reactions of 1:1 molar ratio of nitrophenol and bistrimethylenediamincobalt(III) phosphate, [Co(III)tn2Pi]. Enhanced phosphorylation was depicted for reaction solutions that contained 1:1 molar ratio of nitrophenol and di-bistrimethylenediamincobalt(III) phosphate, [(Co(III)tn2)2Pi]. Specific mechanistic features and the possible roles metal ions play in phosphorylase enzyme are highlighted. Copyright Taylor & Francis Group, LLC.
Catalytic zinc complexes for phosphate diester hydrolysis
Tirel, Emmanuel Y.,Bellamy, Zoe,Adams, Harry,Lebrun, Vincent,Duarte, Fernanda,Williams, Nicholas H.
, p. 8246 - 8250 (2014)
Creating efficient artificial catalysts that can compete with biocatalysis has been an enduring challenge which has yet to be met. Reported herein is the synthesis and characterization of a series of zinc complexes designed to catalyze the hydrolysis of phosphate diesters. By introducing a hydrated aldehyde into the ligand we achieve turnover for DNA-like substrates which, combined with ligand methylation, increases reactivity by two orders of magnitude. In contrast to current orthodoxy and mechanistic explanations, we propose a mechanism where the nucleophile is not coordinated to the metal ion, but involves a tautomer with a more effective Lewis acid and more reactive nucleophile. This data suggests a new strategy for creating more efficient metal ion based catalysts, and highlights a possible mode of action for metalloenzymes.
Carbonate-bridged dinuclear lanthanide(III) complexes of chiral macrocycle
Gerus, Aleksandra,?lepokura, Katarzyna,Lisowski, Jerzy
supporting information, p. 115 - 121 (2019/06/11)
Mononuclear Eu(III) and Dy(III) complexes of the chiral hexaaza macrocycle L, 2(R),7(R),18(R),23(R)-1,8,15,17,24,31-hexaazatricyclo[25.3.1.1.0.0]-dotriaconta-10,12,14,26,28,30-hexaene have been obtained as chloride derivatives (1 and 2, respectively) and
Characterization of wall teichoic acid degradation by the bacteriophage φ29 appendage protein GP12 using synthetic substrate analogs
Myers, Cullen L.,Ireland, Ronald G.,Garrett, Teresa A.,Brown, Eric D.
, p. 19133 - 19145 (2015/09/08)
Background: The GP12 protein from bacteriophage φ29 is a likely wall teichoic acid hydrolase. Results: GP12 is an efficient catalyst of wall teichoic acid hydrolysis that is influenced by glycosylation of the wall teichioc acid polymer. Conclusion: GP12 m