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Substrate kinetics ...
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Decker, DanielUmeå universitet,Institutionen för fysiologisk botanik,Umeå Plant Science Centre (UPSC)
(author)
Substrate kinetics and substrate effects on the quaternary structure of barley UDP-glucose pyrophosphorylase
- Article/chapterEnglish2012
Publisher, publication year, extent ...
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Elsevier BV,2012
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printrdacarrier
Numbers
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LIBRIS-ID:oai:DiVA.org:umu-58610
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https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-58610URI
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https://doi.org/10.1016/j.phytochem.2012.04.002DOI
Supplementary language notes
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Language:English
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Summary in:English
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Classification
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Subject category:ref swepub-contenttype
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Subject category:art swepub-publicationtype
Notes
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UDP-Glc pyrophosphorylase (UGPase) is an essential enzyme responsible for production of UDP-Glc, which is used in hundreds of glycosylation reactions involving addition of Glc to a variety of compounds. In this study, barley UGPase was characterized with respect to effects of its substrates on activity and quaternary structure of the protein. Its K(m) values with Glc-1-P and UTP were 0.33 and 0.25 mM, respectively. Besides using Glc-1-P as a substrate, the enzyme had also considerable activity with Gal-1-P; however, the K(m) for Gal-1-P was very high (>10 mM), rendering this reaction unlikely under physiological conditions. UGPase had a relatively broad pH optimum of 6.5-8.5, regardless of the direction of reaction. The enzyme equilibrium constant was 0.4, suggesting slight preference for the Glc-1-P synthesis direction of the reaction. The quaternary structure of the enzyme, studied by Gas-phase Electrophoretic Mobility Macromolecule Analysis (GEMMA), was affected by addition of either single or both substrates in either direction of the reaction, resulting in a shift from UGPase dimers toward monomers, the active form of the enzyme. The substrate-induced changes in quaternary structure of the enzyme may have a regulatory role to assure maximal activity. Kinetics and factors affecting the oligomerization status of UGPase are discussed.
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Added entries (persons, corporate bodies, meetings, titles ...)
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Meng, MengUmeå universitet,Institutionen för fysiologisk botanik,Umeå Plant Science Centre (UPSC)(Swepub:umu)meme0001
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Gornicka, AgnieszkaUmeå universitet,Institutionen för fysiologisk botanik,Umeå Plant Science Centre (UPSC)
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Hofer, AndersUmeå universitet,Institutionen för medicinsk kemi och biofysik(Swepub:umu)anho0002
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Wilczynska, MalgorzataUmeå universitet,Institutionen för medicinsk kemi och biofysik(Swepub:umu)mawi0006
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Kleczkowski, Leszek AUmeå universitet,Institutionen för fysiologisk botanik,Umeå Plant Science Centre (UPSC)(Swepub:umu)lekl0001
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Umeå universitetInstitutionen för fysiologisk botanik
(creator_code:org_t)
Related titles
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In:Phytochemistry: Elsevier BV79, s. 39-450031-94221873-3700
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