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Role of aspartic acid residues D87 and D89 in APS kinase domain of human 3 '-phosphoadenosine 5 '-phosphosulfate synthase 1 and 2b: A commonality with phosphatases/kinases

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11320%2F21%3A10438876" target="_blank" >RIV/00216208:11320/21:10438876 - isvavai.cz</a>

  • Result on the web

    <a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=h6T4udGaIG" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=h6T4udGaIG</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.bbrep.2021.101155" target="_blank" >10.1016/j.bbrep.2021.101155</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Role of aspartic acid residues D87 and D89 in APS kinase domain of human 3 '-phosphoadenosine 5 '-phosphosulfate synthase 1 and 2b: A commonality with phosphatases/kinases

  • Original language description

    3&apos;-phosphoadenosine 5&apos;-phosphosulfate (PAPS) is synthesized in two steps by PAPS synthase (PAPSS). PAPSS is comprised of ATP sulfurylase (ATPS) and APS kinase (APSK) domain activities. ATPS combines inorganic sulfate with a-phosphoryl of ATP to form adenosine 5&apos;-phosphosulfate (APS) and PPi. In the second step APS is phosphorylated at 3&apos;-OH using another mole of ATP to form PAPS and ADP catalyzed by APSK. The transfer of gamma-phosphoryl from ATP onto 3&apos;-OH requires Mg-2(+) and purported to involve residues D(87)GD(89)N. We report that mutation of either aspartic residue to alanine completely abolishes APSK activity in PAPS formation. PAPSS is an, unique enzyme that binds to four different nucleotides: ATP and APS on both ATPS and APSK domains and ADP and PAPS exclusively on the APSK domain. The thermodynamic binding and the catalytic interplay must be very tightly controlled to form the end-product PAPS in the forward direction. Though APS binds to ATPS and APSK, in ATPS domain, the APS is a product and for APSK it is a substrate. DGDN motif is absent in ATPS and present in APSK. Mutation of D-87 and D-89 did not hamper ATPS activity however abolished APSK activity severely. Thus, D(87)GD(89)N region is required for stabilization of Mg2+-ATP, in the process of splitting the 7-phosphoryl from ATP and transfer of 7-phosphoryl onto 3&apos;-OH of APS to form PAPS a process that cannot be achieved by ATPS domain. In addition, gamma P-32-ATP, trapped phosphoryl enzyme intermediate more with PAPSS2 than with PAPSS1. This suggests inherent active site residues could control novel catalytic differences. Molecular docking studies of hPAPSS1 with ATP + Mg2+ and APS of wild type and mutants supports the experimental results.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10301 - Atomic, molecular and chemical physics (physics of atoms and molecules including collision, interaction with radiation, magnetic resonances, Mössbauer effect)

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2021

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Biochemistry and Biophysics Reports [online]

  • ISSN

    2405-5808

  • e-ISSN

  • Volume of the periodical

    28

  • Issue of the periodical within the volume

    5

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    9

  • Pages from-to

    101155

  • UT code for WoS article

    000732710600008

  • EID of the result in the Scopus database

    2-s2.0-85122798048