56-65-5Relevant articles and documents
Analytical Techniques for the Determination of Chemical Exchange Rate Constants with Application to the Creatine Kinase Reaction
Sorce, Dennis J.,Sciacca, Robert R.,Keller, Andrew M.
, p. 230 - 241 (1990)
A method for determining biochemical exchange rates for analysis of inversion recovery experiments is described.As used in the current application, the technique involves fitting multiexponential equations to the magnetization recovery curves for PCr and ATP.From the parameters of the exponential fits expressions for the forward and reverse rate constants are derived.Results obtained with this technique were compared with inversion transfer and with previously published results using saturation transfer.The addition of a third exchanging species was also investigated and found to have no significant effect on the calculated values for the forward and reverse rate constants.In addition, the feasibility of using an abbreviated 6-point sampling strategy was evaluated; values for the rate constants were similar to those obtained using all 21 data points.The results of this study indicate that chemical exchange rate constants can be determined using inversion recovery techniques which avoid many of the difficulties associated with selective excitation methods.
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Miller,Burgess
, p. 2054,2055 (1978)
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Newton,Perry
, p. 49 (1957)
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Canellakis et al.
, (1962)
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Formation of ATP by photochemical excitation of benzoquinones in dimethylacetamide solution
Lee, Hung-Wen,Huang, Kunpo
, p. 961 - 963 (2002)
A new method of adenosine triphosphate production is described which involves photo-excitation of p-benzoquinones under the presence of adenosine diphosphate and inorganic phosphate in N,N-dimethylacetamide solution. A possible mechanism for the reaction is presented.
Physiological and biochemical characterization of three nucleoside diphosphate kinase isozymes from rice (Oryza sativa L.)
Kihara, Akihiko,Saburi, Wataru,Wakuta, Shinji,Kim, Myung-Hee,Hamada, Shigeki,Ito, Hiroyuki,Imai, Ryozo,Matsui, Hirokazu
, p. 1740 - 1745 (2011)
Nucleoside diphosphate kinase (NDPK) is a ubiquitous enzyme that catalyzes the transfer of the γ-phosphoryl group from a nucleoside triphosphate to a nucleoside diphosphate. In this study, we examined the subcellular localization, tissue-specific gene expression, and enzymatic characteristics of three rice NDPK isozymes (OsNDPK1-OsNDPK3). Sequence comparison of the three OsNDPKs suggested differential subcellular localization. Transient expression of green fluorescence protein-fused proteins in onion cells indicated that OsNDPK2 and OsNDPK3 are localized to plastid and mitochondria respectively, while OsNDPK1 is localized to the cytosol. Expression analysis indicated that all the OsNDPKs are expressed in the leaf, leaf sheath, and immature seeds, except for OsNDPK1, in the leaf sheath. Recombinant OsNDPK2 and OsNDPK3 showed lower optimum pH and higher stability under acidic pH than OsNDPK1. In ATP formation, all the OsNDPKs displayed lower Km values for the second substrate, ADP, than for the first substrate, NTP, and showed lowest and highest K m values for GTP and CTP respectively.
N-acetyl-homocysteinthiolacton as a means of an oxidative synthesis of adenosine diphosphate and adenosine triphosphate from adenosine monophosphate and orthophosphate
Wieland,B?uerlein
, p. 3869 - 3876 (1967)
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Supramolecular catalysis of adenosine triphosphate synthesis in aqueous solution mediated by a macrocyclic polyamine and divalent metal cations
Hosseini,Lehn
, p. 451 - 453 (1991)
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Supramolecularly Assembled Nanocomposites as Biomimetic Chloroplasts for Enhancement of Photophosphorylation
Li, Yue,Feng, Xiyun,Wang, Anhe,Yang, Yang,Fei, Jinbo,Sun, Bingbing,Jia, Yi,Li, Junbai
, p. 796 - 800 (2019)
Prototypes of natural biosystems provide opportunities for artificial biomimetic systems to break the limits of natural reactions and achieve output control. However, mimicking unique natural structures and ingenious functions remains a challenge. Now, multiple biochemical reactions were integrated into artificially designed compartments via molecular assembly. First, multicompartmental silica nanoparticles with hierarchical structures that mimic the chloroplasts were obtained by a templated synthesis. Then, photoacid generators and ATPase-liposomes were assembled inside and outside of silica compartments, respectively. Upon light illumination, protons produced by a photoacid generator in the confined space can drive the liposome-embedded enzyme ATPase towards ATP synthesis, which mimics the photophosphorylation process in vitro. The method enables fabrication of bioinspired nanoreactors for photobiocatalysis and provides insight for understanding sophisticated biochemical reactions.
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Khorana
, p. 3517,3521 (1954)
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Fe(III)-ion-Catalysed Non-enzymatic Transformation of ADP into ATP
Kitani, Akira,Tsunetsugu, Shu-ichi,Sasaki, Kazuo
, p. 329 - 331 (1991)
Non-enzymatic phosphorylation of ADP to ATP has been found to occur readily when Fe(III) ion is present in aqueous solutions of ADP and acetyl phosphate.As long as the reaction temperature is low enough (25 deg C or less), the phosphorylation of ADP to ATP proceeds to about 20percent conversion with 100percent selectivity.At higher temperatures, the yield decreases owing to the hydrolysis of acetyl phosphate.Among several phosphoryl donors studied, acetyl phosphate was found to be the best phosphorylating reagent.Creatine phosphate also produced ATP but the efficiency was very low.The phosphorylation of AMP was unsuccessful, even with acetyl phosphate.
Boric Acid-Fueled ATP Synthesis by FoF1 ATP Synthase Reconstituted in a Supramolecular Architecture
Xu, Xia,Fei, Jinbo,Xu, Youqian,Li, Guangle,Dong, Weiguang,Xue, Huimin,Li, Junbai
, p. 7617 - 7620 (2021)
Significant strides toward producing biochemical fuels have been achieved by mimicking natural oxidative and photosynthetic phosphorylation. Here, different from these strategies, we explore boric acid as a fuel for tuneable synthesis of energy-storing molecules in a cell-like supramolecular architecture. Specifically, a proton locked in boric acid is released in a modulated fashion by the choice of polyols. As a consequence, controlled proton gradients across the lipid membrane are established to drive ATP synthase embedded in the biomimetic architecture, which facilitates tuneable ATP production. This strategy paves a unique route to achieve highly efficient bioenergy conversion, holding broad applications in synthesis and devices that require biochemical fuels.
The mechanism of ion translocation in mitochondria. 3. Coupling of K+ efflux with ATP synthesis.
Rossi,Azzone
, p. 319 - 327 (1970)
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Stereospecificity, substrate, and inhibitory properties of nucleoside diphosphate analogs for creatine and pyruvate kinases
Wennefors, Charlotta K.,Dobrikov, Mikhail I.,Xu, Zhihong,Li, Ping,Shaw, Barbara Ramsay
, p. 169 - 177 (2008)
Antiviral α-P-borano substituted NTPs are promising chain terminators targeting HIV reverse transcriptase (RT). Activation of antiviral nucleoside diphosphates (NDPs) to NTPs may be carried out by pyruvate kinase (PK) and creatine kinase (CK). Herein, are presented the effects of nucleobase, ribose, and α-phosphate substitutions on substrate specificities of CK and PK. Both enzymes showed two binding modes and negative cooperativity with respect to substrate binding. The stereospecificity and inhibition of ADP phosphorylation by α-P-borano substituted NDP (NDPαB) stereoisomers were also investigated. The Sp-ADPαB isomer was a 70-fold better substrate for CK than the Rp isomer, whereas PK preferred the Rp isomer of NDPαBs. For CK, the Sp-ADPαB isomer was a competitive inhibitor; for PK, the Rp-ADPαB isomer was a poor competitive inhibitor and the Sp-ADPαB isomer was a poor non-competitive inhibitor. Taken together, these data suggest that, although the Rp-NDPαB isomer would be minimally phosphorylated by CK or PK, it should not inhibit either enzyme.
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Ansberga et al.
, (1976)
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ATP regeneration by a single polyphosphate kinase powers multigram-scale aldehyde synthesisin vitro
Tavanti, Michele,Hosford, Joseph,Lloyd, Richard C.,Brown, Murray J. B.
supporting information, p. 828 - 837 (2021/02/09)
ATP recycling systems are required to avoid the addition of stoichiometric quantities of cofactor and facilitate industrial implementation of ATP-dependent enzymes. One factor that limits the biocatalytic application of these enzymes is the lack of a scalable AMP to ATP regeneration system. Whole-cells or a combination of purified enzymes are often exploited for ATP regeneration from AMP, whereas cell free systems comprising a single crude enzyme preparation would be preferred. To establish such a system, we focussed on polyphosphate kinases (PPKs) to find a single enzyme that could be used to power ATP-consuming reactions. Screening of some previously reported PPKs revealed limitations of these biocatalysts for scale-up purposes. As such, a panel of novel putative PPK2-III enzymes was constructed and compared to characterised enzymes belonging to the same class. Multidimensional small-scale screening revealed that PPK12 (from an unclassifiedErysipelotrichaceaebacterium) displays enhanced expression levels, ATP formation rates, polyphosphate tolerance and stability under a variety of harsh conditions. The carboxylic acid reductase (CAR) catalysed reduction of carboxylates to aldehydes was chosen as a model reaction to test the applicability of PPK12 as a bifunctional biocatalyst for ATP regeneration from AMP. The implementation of the identified ATP-recycling enzyme provided the first example of cell free multigram-scale aldehyde synthesis employing enzymes and a single PPK2-III, paving the way for affordable scalable ATP regeneration technologies.