Please use this identifier to cite or link to this item: http://elib.uni-stuttgart.de/handle/11682/15515
Authors: Hildenbrand, Jennie C.
Sprenger, Georg A.
Teleki, Attila
Takors, Ralf
Jendrossek, Dieter
Title: Polyphosphate kinases phosphorylate thiamine phosphates
Issue Date: 2023
metadata.ubs.publikation.typ: Zeitschriftenartikel
metadata.ubs.publikation.seiten: 1-11
metadata.ubs.publikation.source: Microbial physiology 33 (2023), S. 1-11
URI: http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-ds-155150
http://elib.uni-stuttgart.de/handle/11682/15515
ISSN: 2673-1673
2673-1665
Abstract: Polyphosphate kinases (PPKs) catalyze the reversible transfer of the γ-phosphate moiety of ATP (or of another nucleoside triphosphate) to a growing chain of polyphosphate (polyP). In this study, we describe that PPKs of various sources are additionally able to phosphorylate thiamine diphosphate (ThP2) to produce thiamine triphosphate (ThP3) and even thiamine tetraphosphate in vitro using polyP as phosphate donor. Furthermore, all tested PPK2s, but not PPK1s, were able to phosphorylate thiamine monophosphate (ThP1) to ThP2 and ThP3 although at low efficiency. The predicted masses and identities of the mono- and oligo-phosphorylated thiamine metabolites were identified by high-performance liquid chromatography tandem mass spectrometry. Moreover, the biological activity of ThP2, that was synthesized by phosphorylation of ThP1 with polyP and PPK, as a cofactor of ThP2-dependent enzymes (here transketolase TktA from Escherichia coli ) was confirmed in a coupled enzyme assay. Our study shows that PPKs are promiscuous enzymes in vitro that could be involved in the formation of a variety of phosphorylated metabolites in vivo.
Appears in Collections:04 Fakultät Energie-, Verfahrens- und Biotechnik

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