Defining the structural requirements for ribose 5-phosphate-binding and intersubunit cross-talk of the malarial pyridoxal 5-phosphate synthase
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 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.
vitamin B6, pyridoxal 5-phosphate (plp) synthase, malaria, Pdx1/Pdx2, protein protein interaction, ribose 5-phosphate-binding
4169-4174
Derrer, Bianca
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Windeisen, Volker
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Guédez Rodríguez, Gabriela
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Seidler, Joerg
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Gengenbacher, Martin
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Lehmann, Wolf D
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Rippe, Karsten
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Sinning, Irmgard
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Tews, Ivo
9117fc5e-d01c-4f8d-a734-5b14d3eee8dd
Kappes, Barbara
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8 October 2010
Derrer, Bianca
47afe991-41ef-4501-92c8-6a656cad95ec
Windeisen, Volker
904d85ea-64f9-4157-b273-031e5dbc0f76
Guédez Rodríguez, Gabriela
42efdb20-b768-437b-9230-4f5a5db166a3
Seidler, Joerg
f0af1e17-d197-4399-8235-2c2ec5202221
Gengenbacher, Martin
0d3f66c3-f327-488b-93ad-6070366e0f73
Lehmann, Wolf D
2d4b1918-3e0f-42d7-bb22-f3c7ff73504b
Rippe, Karsten
5dc8f1ed-943d-42d2-baa6-1e7f777f391e
Sinning, Irmgard
fbc3f199-8a3b-47a6-9ee7-00bfc472e079
Tews, Ivo
9117fc5e-d01c-4f8d-a734-5b14d3eee8dd
Kappes, Barbara
10edf779-dc81-4973-878b-d3177273f86a
Derrer, Bianca, Windeisen, Volker, Guédez Rodríguez, Gabriela, Seidler, Joerg, Gengenbacher, Martin, Lehmann, Wolf D, Rippe, Karsten, Sinning, Irmgard, Tews, Ivo and Kappes, Barbara
(2010)
Defining the structural requirements for ribose 5-phosphate-binding and intersubunit cross-talk of the malarial pyridoxal 5-phosphate synthase.
FEBS Letters, 584 (19), .
(doi:10.1016/j.febslet.2010.09.013).
(PMID:20837012)
Abstract
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.
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e-pub ahead of print date: 15 September 2010
Published date: 8 October 2010
Additional Information:
Funded by European Commission - FP6: Vitamin biosynthesis as a target for antimalarial therapy (VITBIOMAL) (12158)
Keywords:
vitamin B6, pyridoxal 5-phosphate (plp) synthase, malaria, Pdx1/Pdx2, protein protein interaction, ribose 5-phosphate-binding
Organisations:
Centre for Biological Sciences
Identifiers
Local EPrints ID: 200233
URI: http://eprints.soton.ac.uk/id/eprint/200233
ISSN: 0014-5793
PURE UUID: 13d1e70d-78cb-4ac7-a9a5-a6a28944d85e
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Date deposited: 24 Oct 2011 11:39
Last modified: 15 Mar 2024 03:36
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Author:
Bianca Derrer
Author:
Volker Windeisen
Author:
Gabriela Guédez Rodríguez
Author:
Joerg Seidler
Author:
Martin Gengenbacher
Author:
Wolf D Lehmann
Author:
Karsten Rippe
Author:
Irmgard Sinning
Author:
Barbara Kappes
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