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

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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 languageEnglish (US)
Pages (from-to)11106-11121
Number of pages16
JournalJournal of Biological Chemistry
Volume288
Issue number16
DOIs
StatePublished - Apr 19 2013

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FAD pyrophosphatase
Bimetals
Treponema pallidum
Lipoproteins
Homeostasis
Metals
Flavin Mononucleotide
Flavin-Adenine Dinucleotide
Adenosine Monophosphate
Bacteria
Enzymes
4,6-dinitro-o-cresol

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

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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.",
author = "Deka, {Ranjit K.} and Brautigam, {Chad A} and Liu, {Wei Z.} and Tomchick, {Diana R} and Norgard, {Michael V}",
year = "2013",
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doi = "10.1074/jbc.M113.449975",
language = "English (US)",
volume = "288",
pages = "11106--11121",
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publisher = "American Society for Biochemistry and Molecular Biology Inc.",
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T1 - The TP0796 lipoprotein of Treponema pallidum is a bimetal-dependent FAD pyrophosphatase with a potential role in flavin homeostasis

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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U2 - 10.1074/jbc.M113.449975

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JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

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