Periplasmic binding proteins Bug69 and Bug27 from Bordetella pertussis are in vitro high‐affinity quinolinate binders with a potential role in NAD biosynthesis DOI Creative Commons
Leonardo Sorci, Gabriele Minazzato, Adolfo Amici

et al.

FEBS Open Bio, Journal Year: 2024, Volume and Issue: 14(10), P. 1718 - 1730

Published: Aug. 8, 2024

Bordetella 's genome contains a large family of periplasmic binding proteins (PBPs) known as Bugs, whose functions are mainly unassigned. Two members, Bug27 and Bug69, have previously been considered potential candidates for the uptake small pyridine precursors, possibly linked to NAD biosynthesis. Here, we show an in vitro affinity Bug69 quinolinate submicromolar range, with marked preference over other precursors. A combined sequence similarity network context analysis identifies cluster Bug69/27 homologs that genomically associated transcriptional regulator NadQ enzyme phosphoribosyltransferase (QaPRT, gene nadC ), suggesting functional linkage metabolism. Integrating molecular docking structure‐based multiple alignments confirms is preferred ligand Bug69.

Language: Английский

Metabolic engineering of Escherichia coli for upcycling of polyethylene terephthalate waste to vanillin DOI
Yang Li,

Xiaomin Zhao,

Siqi Chen

et al.

The Science of The Total Environment, Journal Year: 2024, Volume and Issue: 957, P. 177544 - 177544

Published: Nov. 19, 2024

Language: Английский

Citations

1
<i>Ideonella sakaiensis</i>によるポリエチレンテレフタレートを原料としたポリヒドロキシアルカン酸の発酵生産 DOI
Shosuke Yoshida

Sen i Gakkaishi, Journal Year: 2024, Volume and Issue: 80(4), P. P - 135

Published: Jan. 1, 2024

Citations

0
Periplasmic binding proteins Bug69 and Bug27 from Bordetella pertussis are in vitro high‐affinity quinolinate binders with a potential role in NAD biosynthesis DOI Creative Commons
Leonardo Sorci, Gabriele Minazzato, Adolfo Amici

et al.

FEBS Open Bio, Journal Year: 2024, Volume and Issue: 14(10), P. 1718 - 1730

Published: Aug. 8, 2024

Bordetella 's genome contains a large family of periplasmic binding proteins (PBPs) known as Bugs, whose functions are mainly unassigned. Two members, Bug27 and Bug69, have previously been considered potential candidates for the uptake small pyridine precursors, possibly linked to NAD biosynthesis. Here, we show an in vitro affinity Bug69 quinolinate submicromolar range, with marked preference over other precursors. A combined sequence similarity network context analysis identifies cluster Bug69/27 homologs that genomically associated transcriptional regulator NadQ enzyme phosphoribosyltransferase (QaPRT, gene nadC ), suggesting functional linkage metabolism. Integrating molecular docking structure‐based multiple alignments confirms is preferred ligand Bug69.

Language: Английский

Citations

0