130-49-4Relevant articles and documents
Dinuclear copper(II) complex that hydrolyzes RNA
Young, Mary Jane,Chin, Jik
, p. 10577 - 10578 (1995)
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Hetero-dinuclear metal complexes for RNA hydrolysis
Kamitani, Jun,Kawahara, Ryuto,Yashiro, Morio,Komiyama, Makoto
, p. 1047 - 1048 (1998)
In the presence of a ligand having two metal-binding sites, Fe(III)/Zn(II) and Fe(III)/Cd(II) combinations hydrolyze adenylyl(3′-5′)adenosine. The notable activities are ascribed to the synergetic cooperation between the two kinds of metal ions in the hetero-dinuclear complexes.
A Stark Contrast to Modern Earth: Phosphate Mineral Transformation and Nucleoside Phosphorylation in an Iron- and Cyanide-Rich Early Earth Scenario
Burcar, Bradley,Casta?eda, Alma,Lago, Jennifer,Daniel, Mischael,Pasek, Matthew A.,Hud, Nicholas V.,Orlando, Thomas M.,Menor-Salván, César
, p. 16981 - 16987 (2019)
Organophosphates were likely an important class of prebiotic molecules. However, their presence on the early Earth is strongly debated because the low availability of phosphate, which is generally assumed to have been sequestered in insoluble calcium and iron minerals, is widely viewed as a major barrier to organophosphate generation. Herein, we demonstrate that cyanide (an essential prebiotic precursor) and urea-based solvents could promote nucleoside phosphorylation by transforming insoluble phosphate minerals in a “warm little pond” scenario into more soluble and reactive species. Our results suggest that cyanide and its derivatives (metal cyanide complexes, urea, ammonium formate, and formamide) were key reagents for the participation of phosphorus in chemical evolution. These results allow us to propose a holistic scenario in which an evaporitic environment could concentrate abiotically formed organics and transform the underlying minerals, allowing significant organic phosphorylation under plausible prebiotic conditions.
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Brown,Todd
, p. 44,46 (1952)
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Synergetic Catalysis by Two Non-lanthanide Metal Ions for Hydrolysis of Diribonucleotides
Irisawa, Makoto,Takeda, Naoya,Komiyama, Makoto
, p. 1221 - 1222 (1995)
Adenylyl(3'-5')adenosine and uridylyl(3'-5')uridine are efficiently hydrolysed at pH 7 by bimetallic cooperation of zinc(ii) with tin(iv), indium(iii), iron(iii) or aluminium(iii).
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Lipkin et al.
, p. 6075,6198,6202 (1959)
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Rapid hydrolysis of 2',3'-cAMP with a Cu(II) complex: Effect of intramolecular hydrogen bonding on the basicity and reactivity of a metal- bound hydroxide
Wall, Mark,Linkletter, Barry,Williams, Dan,Lebuis, Anne-Marie,Hynes, Rosemary C.,Chin, Jik
, p. 4710 - 4711 (1999)
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Kinetic Analysis of Diamine-Catalyzed RNA Hydrolysis
Komiyama, Makoto,Yoshinari, Koichi
, p. 2155 - 2160 (1997)
The catalysis of various amines for the hydrolysis of RNA has been kinetically investigated, and the catalytic rate constants for each of the ionic states of these amines are determined. Ethylenediamine and 1,3-propanediamine are highly active under the physiological conditions, mainly because they preferentially take the catalytically active monocationic forms. The catalysis of these diamines is further promoted by the intramolecular acid-base cooperation of the neutral amine and the ammonium ion. In contrast, monoamines overwhelmingly exist at pH 7 as the inactive cations. Potential application of the catalysis by the diamines and the related oligoamines is discussed.
Kinetics and mechanisms for reactions of adenosine 2'- and 3'-monophosphates in aqueous acid: Competition between phosphate migration, dephosphorylation, and depurination
Oivanen,Lonnberg
, p. 2556 - 2560 (1989)
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THE PREPARATION OF PERMANGANATE-OXIDISED RIBONUCLEIC ACID AND ITS
HOLBROOK,JONES,WELCH
, p. 3998 - 4004 (1965)
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Natural occurrence of 2′,5′-linked heteronucleotides in marine sponges
Lopp, Annika,Reintamm, Tonu,Kuusksalu, Anne,Tammiste, Indrek,Pihlak, Arno,Kelve, Merike
experimental part, p. 235 - 254 (2010/10/19)
2′,5′-oligoadenylate synthetases (OAS) as a component of mammalian interferon-induced antiviral enzymatic system catalyze the oligomerization of cellular ATP into 2′,5′-linked oligoadenylates (2-5A). Though vertebrate OASs have been characterized as 2′-nucleotidyl transferases under in vitro conditions, the natural occurrence of 2′,5′-oligonucleotides other than 2-5A has never been demonstrated. Here we have demonstrated that OASs from the marine sponges Thenea muricata and Chondrilla nucula are able to catalyze in vivo synthesis of 2-5A as well as the synthesis of a series 2′,5′-linked heteronucleotides which accompanied high levels of 2′,5′-diadenylates. In dephosphorylated perchloric acid extracts of the sponges, these heteronucleotides were identified as A2′p5′G, A2′p5′U, A2′p5′C, G2′p5′A and G2′p5′U. The natural occurrence of 2′-adenylated NAD+ was also detected. In vitro assays demonstrated that besides ATP, GTP was a good substrate for the sponge OAS, especially for OAS from C. nucula. Pyrimidine nucleotides UTP and CTP were also used as substrates for oligomerization, giving 2′,5′-linked homo-oligomers. These data refer to the substrate specificity of sponge OASs that is remarkably different from that of vertebrate OASs. Further studies of OASs from sponges may help to elucidate evolutionary and functional aspects of OASs as proteins of the nucleotidyltransferase family.
Factors influencing the operational stability of NADPH-dependent alcohol dehydrogenase and an NADH-dependent variant thereof in gas/solid reactors
Kulishova, Liliya,Dimoula, Kerasina,Jordan, Max,Wirtz, Astrid,Hofmann, Diana,Santiago-Schuebel, Beatrix,Fitter, Joerg,Pohl, Martina,Spiess, Antje C.
experimental part, p. 271 - 283 (2011/02/22)
The continuous enzymatic gas/solid bio-reactor serves both for the production of volatile fine chemicals and flavors on an industrial scale and for thermodynamically controlled investigation of substrate and water effects on enzyme preparations for research purposes. Here, we comparatively investigated the molecular effects on the operational stability of NADPH-dependent Lactobacillus brevis alcohol dehydrogenase and an NADH-dependent variant thereof, LbADH G37D, in the gas/solid bioreactor. The reference reaction is the reduction of acetophenone to (R)-1-phenylethanol with concomitant oxidation of 2-propanol to acetone for the purpose of regeneration of the redox cofactor. It could be clearly shown that not the thermostability of the cofactor, but the thermostability of the proteins in the solid dry state govern the order of magnitude of the operational stability of both purified enzymes in the gas/solid reactor at low thermodynamic activity of water and substrate. However, at higher thermodynamic activity the operational stability in the gas/solid reactor is overlaid by stabilizing and destabilizing effects of the substrates that require further investigation. We demonstrated first evidence that the substrate affinity of the two variants in the gas/solid reactor is similar to the affinity in aqueous medium. We could also show that partial unfolding of the proteins with subsequent aggregation are the factors governing protein thermo-in-stability both in the dissolved and in the dry state. Thus, stability investigations of enzymes in the dry state are suggested to predict their basal level of operational stability in gas/solid reactions.