Annotation inferences using phylogenetic trees
Identification and Characterization of Heptaprenylglyceryl Phosphate Processing Enzymes in Bacillus subtilis.
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The yvoF deletion identifies the native ether-lipid acetylation step; recombinant YvoF is acetyl-CoA dependent and overlaps only partly with MAT substrate scope.
"The acetyl-CoA-dependent enzyme YvoF is a close relative of maltose O-acetyltransferase (MAT)."
Lipoprotein N-terminal modification in Bacillus: a new paradigm for extracellular acetylation and species-dependent Toll-like receptor 2 immunomodulation.
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YvoF supplies the acetylated lipid donor for the reconstituted LhaT pathway; the in vitro carrier is a C20 analogue of native C35 HepG.
"We substituted the commercially available geranylgeranyl pyrophosphate (GGPP) (four isoprenyl repeats) for the native heptaprenyl pyrophosphate (seven isoprenyl repeats) carrier"
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Native deletion and complementation link yvoF to lipoprotein N-acetylation without making YvoF the enzyme that modifies the protein amino terminus.
"Back complementation of pcrB/ypjA/yvoF restored Ac-LP synthesis in all cases"
YvoF primary localization evidence
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Activity fractionation supports membrane association; the cytoplasmic face is a mechanistic assignment rather than a directly resolved topology measurement.
"No activity was left in the fraction of soluble proteins."