The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent FAD pyrophosphatase with a potential role in flavin homeostasis

Ranjit K. Deka; Chad A Brautigam; Wei Z. Liu; Diana R Tomchick; Michael V Norgard

doi:10.1074/jbc.M113.449975

The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent FAD pyrophosphatase with a potential role in flavin homeostasis

Ranjit K. Deka, Chad A Brautigam, Wei Z. Liu, Diana R Tomchick, Michael V Norgard

Research output: Contribution to journal › Article › peer-review

23 Scopus citations

Abstract

Background: The TP0796 lipoprotein of Treponema pallidum belongs to the poorly characterized ApbE superfamily. Results: TP0796 hydrolyzed FAD into FMN and AMP, consistent with the general enzymatic mechanism of an FAD pyrophosphatase. Conclusion: This novel metal-dependent enzyme probably plays an essential role in flavin homeostasis in T. pallidum. Significance: This is the first description of a metal-dependent FAD pyrophosphatase in bacteria.

Original language	English (US)
Pages (from-to)	11106-11121
Number of pages	16
Journal	Journal of Biological Chemistry
Volume	288
Issue number	16
DOIs	https://doi.org/10.1074/jbc.M113.449975
State	Published - Apr 19 2013

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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title = "The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent FAD pyrophosphatase with a potential role in flavin homeostasis",

abstract = "Background: The TP0796 lipoprotein of Treponema pallidum belongs to the poorly characterized ApbE superfamily. Results: TP0796 hydrolyzed FAD into FMN and AMP, consistent with the general enzymatic mechanism of an FAD pyrophosphatase. Conclusion: This novel metal-dependent enzyme probably plays an essential role in flavin homeostasis in T. pallidum. Significance: This is the first description of a metal-dependent FAD pyrophosphatase in bacteria.",

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AU - Deka, Ranjit K.

AU - Brautigam, Chad A

AU - Liu, Wei Z.

AU - Tomchick, Diana R

AU - Norgard, Michael V

PY - 2013/4/19

Y1 - 2013/4/19

N2 - Background: The TP0796 lipoprotein of Treponema pallidum belongs to the poorly characterized ApbE superfamily. Results: TP0796 hydrolyzed FAD into FMN and AMP, consistent with the general enzymatic mechanism of an FAD pyrophosphatase. Conclusion: This novel metal-dependent enzyme probably plays an essential role in flavin homeostasis in T. pallidum. Significance: This is the first description of a metal-dependent FAD pyrophosphatase in bacteria.

AB - Background: The TP0796 lipoprotein of Treponema pallidum belongs to the poorly characterized ApbE superfamily. Results: TP0796 hydrolyzed FAD into FMN and AMP, consistent with the general enzymatic mechanism of an FAD pyrophosphatase. Conclusion: This novel metal-dependent enzyme probably plays an essential role in flavin homeostasis in T. pallidum. Significance: This is the first description of a metal-dependent FAD pyrophosphatase in bacteria.

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The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent FAD pyrophosphatase with a potential role in flavin homeostasis

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