905904-58-7Relevant articles and documents
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.
Intrinsic Apyrase-Like Activity of Cerium-Based Metal–Organic Frameworks (MOFs): Dephosphorylation of Adenosine Tri- and Diphosphate
Gu, Jinlou,Li, Chunzhong,Li, Ke,Yang, Jian
supporting information, p. 22952 - 22956 (2020/10/23)
Apyrase is an important family of extracellular enzymes that catalyse the hydrolysis of high-energy phosphate bonds (HEPBs) in ATP and ADP, thereby modulating many physiological processes and driving life activities. Herein, we report an unexpected discovery that cerium-based metal–organic frameworks (Ce-MOFs) of UiO-66(Ce) have intrinsic apyrase-like activity for ATP/ADP-related physiological processes. The abundant CeIII/CeIV couple sites of Ce-MOFs endow them with the ability to selectively catalyse the hydrolysis of HEPBs of ATP and ADP under physiological conditions. Compared to natural enzymes, they could resist extreme pH and temperature, and present a broad range of working conditions. Based on this finding, a significant inhibitory effect on ADP-induced platelet aggregation was observed upon exposing the platelet-rich plasma (PRP) to the biomimetic UiO-66(Ce) films, prefiguring their wide application potentials in medicine and biotechnology.
RECOMBINANT SMNPP5 AND METHODS OF USE
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Paragraph 00196, (2019/10/04)
Described herein are methods and compositions for reducing coagulation, e.g., in a subject having a coagulation disease or disorder. Aspects of the invention relate to administering to a subject a recombinant SmNPP-5 protein or pharmaceutical composition described herein. Other aspects of the invention relate to methods for producing a recombinant SmNPP-5 protein.