• Login
    View Item 
    •   Home
    • LECTURER SCIENTIFIC PUBLICATION (Publikasi Ilmiah)
    • LSP-Conference Proceeding
    • View Item
    •   Home
    • LECTURER SCIENTIFIC PUBLICATION (Publikasi Ilmiah)
    • LSP-Conference Proceeding
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Revealing the Important Role of Allosteric Property in Sucrose Phosphate Synthase from Sugarcane with N-terminal Domain Deletion

    Thumbnail
    View/Open
    F. MIPA_Prosiding_Bambang S_Revealing the important role of allosteric property.pdf (1.019Mb)
    Date
    2019-01-09
    Author
    Sawitri, Widhi Dyah
    Sugiharto, Bambang
    Metadata
    Show full item record
    Abstract
    Sucrose occupies many essential roles to control regulation of carbon partitioning in plants, including prokaryotic cells. Sucrose phosphate synthase (SPS; EC 2.4.1.14) is a key enzyme to catalyze the form of sucrose in primary sucrose synthesis pathway. Plants SPS has a molecular size around 120 kDa, which consists of N-terminal domain, C-terminal domain, and central domain. We produced the recombinant sugarcane SPS (SoSPS1) in Escherichia coli, however, the expression often appears to be a shorter form with retained enzyme activity. In our result, we reported that the shorter form is suggested to have a truncated N-terminal 20-kDa region. The truncated form of SoSPS1 (∆N-SPS) tends to enhance the specific activity 10-fold compared to full-length SoSPS1. The full-lenght SoSPS1 showed a remarkable allosteric activation by glucose-6-phosphate (G6P), while none of the N-terminal truncated form had such a characteristic. By kinetic analysis of full-length SoSPS1, a higher substrate affinity was shown in the presence of G6P. Conversely, the ∆N-SPS showed a similar substrate affinity whether G6P was added or not. Based on these results, we revealed that N-terminal region of SoSPS1 has essential role for allosteric regulation by G6P and may function like a suppressor domain for the enzyme activity.
    URI
    http://repository.unej.ac.id/handle/123456789/97044
    Collections
    • LSP-Conference Proceeding [1877]

    UPA-TIK Copyright © 2024  Library University of Jember
    Contact Us | Send Feedback

    Indonesia DSpace Group :

    University of Jember Repository
    IPB University Scientific Repository
    UIN Syarif Hidayatullah Institutional Repository
     

     

    Browse

    All of RepositoryCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects

    My Account

    LoginRegister

    UPA-TIK Copyright © 2024  Library University of Jember
    Contact Us | Send Feedback

    Indonesia DSpace Group :

    University of Jember Repository
    IPB University Scientific Repository
    UIN Syarif Hidayatullah Institutional Repository