Publications by authors named "Hari Parapatla"
Article Synopsis
- The study confirmed that organophosphate hydrolase (OPH) from Sphingobium fuliginis is crucial for iron uptake by interacting directly with ferric-enterobactin.
- Alterations to the active site of OPH did not hinder its ability to bind ferric-enterobactin, indicating a separate binding site for this interaction.
- The presence of OPH in an engineered E. coli system enhanced iron uptake, while its absence or use of inactive variants resulted in decreased iron acquisition, highlighting OPH's essential role in the iron transport process.
Organophosphate hydrolase (OPH) is a membrane-associated lipoprotein. It translocates across the inner membrane via the twin-arginine transport pathway and remains anchored to the periplasmic face of the inner membrane through a diacylglycerol moiety linked to the invariant cysteine residue found at the junction of a SpaseII cleavage site. Due to the existence of a transmembrane helix at the C-terminus of the mature OPH, an inner-membrane topology was predicted suggesting the C-terminus of OPH is cytoplasmic.
View Article and Find Full Text PDFGenome-Guided Insights Reveal Organophosphate-Degrading Brevundimonas diminuta as Sphingopyxis wildii and Define Its Versatile Metabolic Capabilities and Environmental Adaptations.
Genome Biol Evol
January 2017
The complete genome sequence of Brevundimonas diminuta represented a chromosome (∼4.15 Mb) and two plasmids (pCMS1 and pCMS2) with sizes of 65,908 and 30,654 bp, respectively. The sequence of the genome showed no significant similarity with the known bacterial genome sequences, instead showed weak similarity with the members of different genera of family, Sphingomonadaceae.
View Article and Find Full Text PDFArticle Synopsis
- Organophosphate hydrolase (OPH) breaks down organophosphate bonds in insecticides and nerve agents and is transported to the inner membrane of Brevundimonas diminuta via the twin-arginine transport (Tat) pathway.
- The OPH signal peptide features a key cysteine at the cleavage site and a conserved lipobox motif; inhibiting signal peptidase II with globomycin leads to a buildup of non-processed OPH in the cytoplasm.
- OPH is confirmed as a lipoprotein through cysteine to serine substitution, which allows it to enter the periplasm and interact with proteins such as TolC and PstS, aiding phosphate transport from organophosphates, highlighting the