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Defining the structural requirements for ribose 5-phosphate-binding and intersubunit cross-talk of the malarial pyridoxal 5-phosphate synthase

Most organisms synthesise the B(6) vitamer pyridoxal 5-phosphate (PLP) via the glutamine amidotransferase PLP synthase, a large enzyme complex of 12 Pdx1 synthase subunits with up to 12 Pdx2 glutaminase subunits attached. Deletion analysis revealed that the C-terminus has four distinct functionaliti...

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Hauptverfasser: Derrer, Bianca (VerfasserIn) , Windeisen, Volker (VerfasserIn) , Guédez Rodríguez, Gabriela Liuvanova (VerfasserIn) , Seidler, Joerg (VerfasserIn) , Gengenbacher, Martin (VerfasserIn) , Lehmann, Wolf D. (VerfasserIn) , Rippe, Karsten (VerfasserIn) , Sinning, Irmgard (VerfasserIn) , Tews, Ivo (VerfasserIn) , Kappes, Barbara (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 17 September 2010
In: FEBS letters
Year: 2010, Jahrgang: 584, Heft: 19, Pages: 4169-4174
ISSN:1873-3468
DOI:10.1016/j.febslet.2010.09.013
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.febslet.2010.09.013
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Verfasserangaben:Bianca Derrer, Volker Windeisen, Gabriela Guédez Rodríguez, Joerg Seidler, Martin Gengenbacher, Wolf D. Lehmann, Karsten Rippe, Irmgard Sinning, Ivo Tews, Barbara Kappes
Beschreibung
Zusammenfassung:Most organisms synthesise the B(6) vitamer pyridoxal 5-phosphate (PLP) via the glutamine amidotransferase PLP synthase, a large enzyme complex of 12 Pdx1 synthase subunits with up to 12 Pdx2 glutaminase subunits attached. Deletion analysis revealed that the C-terminus has four distinct functionalities: assembly of the Pdx1 monomers, binding of the pentose substrate (ribose 5-phosphate), formation of the reaction intermediate I(320), and finally PLP synthesis. Deletions of distinct C-terminal regions distinguish between these individual functions. PLP formation is the only function that is conferred to the enzyme by the C-terminus acting in trans, explaining the cooperative nature of the complex.
Beschreibung:Gesehen am 25.01.2024
Beschreibung:Online Resource
ISSN:1873-3468
DOI:10.1016/j.febslet.2010.09.013

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