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Substrate kinetics ...
Substrate kinetics and substrate effects on the quaternary structure of barley UDP-glucose pyrophosphorylase
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- Decker, Daniel (författare)
- Umeå universitet,Institutionen för fysiologisk botanik,Umeå Plant Science Centre (UPSC)
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- Meng, Meng (författare)
- Umeå universitet,Institutionen för fysiologisk botanik,Umeå Plant Science Centre (UPSC)
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- Gornicka, Agnieszka (författare)
- Umeå universitet,Institutionen för fysiologisk botanik,Umeå Plant Science Centre (UPSC)
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- Hofer, Anders (författare)
- Umeå universitet,Institutionen för medicinsk kemi och biofysik
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- Wilczynska, Malgorzata (författare)
- Umeå universitet,Institutionen för medicinsk kemi och biofysik
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- Kleczkowski, Leszek A (författare)
- Umeå universitet,Institutionen för fysiologisk botanik,Umeå Plant Science Centre (UPSC)
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(creator_code:org_t)
- Elsevier BV, 2012
- 2012
- Engelska.
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Ingår i: Phytochemistry. - : Elsevier BV. - 0031-9422 .- 1873-3700. ; 79, s. 39-45
- Relaterad länk:
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http://www.sciencedi...
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- Cell wall synthesis
- Oligomerization
- Protein structure
- Sucrose metabolism
- Sucrose synthase
- Sugar activation
- UDP-sugar synthesis
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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