Polyethylene glycol (PEG)–carboxylate–CoA synthetase is involved in PEG metabolism in Sphingopyxis macrogoltabida strain 103

Abstract

Sphingopyxis macrogoltabida strain 103 possesses polyethylene-glycol (PEG)-inducible pegBCDAE operon encoding the genes relevant to PEG degradation. PEG is converted to PEG-carboxylate by PegA (PEG dehydrogenase) and PegC (PEG-aldehyde dehydrogenase). In this study, the recombinant PegE (homologous to acyl-CoA synthetases) was characterized. PegE was an acyl-CoA synthetase active for PEG-carboxylate and fatty acids. Judging from the nature of this kind of protein (located on the cytoplasmic membrane as a translocator), PegE might be responsible for the translocation of PEG-carboxylate from the periplasm into the cytoplasm or for the detoxification of strong acidity of the substrate.

Effect of tributyrin supplementation in high‐soya bean meal diet on growth performance, body composition, intestine morphology and microbiota of juvenile yellow drum (Nibea albiflora)

“…Some metabolic‐associated genera were observed significantly increased by tributyrin supplementation in SBM‐based diet, including Hydrogenophaga , Rhodocyclaceae , Sphingopyxis , Hydrogenophaga , Methyloversatilis and Devosia . The increase in denitrifying species, such as Hydrogenophaga (Magic‐Knezev, Wullings, & Kooij, ; Tanamool, Imai, Danvirutai, & Kaewkannetra, ) , Rhodocyclaceae (Oren, ) and Methyloversatilis (Smalley et al, ) and bacteria degrading organic substances, such as Sphingopyxis (Tani, Somyoonsap, Minami, Kimbara, & Kawai, ), may contribute to degrading ingredients from SBM protein. Although these results provided basic knowledge on the impacts of dietary tributyrin supplementation alteration on the intestinal microbiota composition and diversity of juvenile yellow drum, putative involvement of bacteria in the metabolism and immunity merits further investigation.…”

“…Methyloversatilis (Smalley et al, 2015) and bacteria degrading organic substances, such as Sphingopyxis (Tani, Somyoonsap, Minami, Kimbara, & Kawai, 2008), may contribute to degrading ingredients from SBM protein. Although these results provided basic knowledge on the impacts of dietary tributyrin supplementation alteration on the intestinal microbiota composition and diversity of juvenile yellow drum, putative involvement of bacteria in the metabolism and immunity merits further investigation.…”

Novel Polyoxyethylene-Containing Glycolipids Are Synthesized inCorynebacterium matruchotiiandMycobacterium smegmatisCultured in the Presence of Tween 80

“…The acyl-CoA ligase ( pegE ) catalyzes the ligation of PEG-carboxylate (polyoxyethylenate) and CoA on the cytoplasmic membrane [32]. We have identified homologs of PEG dehydrogenase ( pegA ), PEG-aldehyde dehydrogenase ( pegC ), acyl-CoA ligase ( pegE ), and AraC-type transcription regulator ( pegR ) in corynebacteria and mycobacteria genomes by sequence homology searches ( in silico analysis).…”

The Biochemistry and Molecular Biology of Xenobiotic Polymer Degradation by Microorganisms

“…A gene coding acyl-CoA synthetase in the peg operon was expressed and the recombinant enzyme was found to react with PEG-carboxylate to form PEG-carboxylate-CoA. 28) Judging from the nature of this kind of protein (located on the cytoplasmic membrane as a translocator), the enzyme might be responsible for the translocation of PEG-carboxylate from the periplasm into the cytoplasm or for the detoxification of strong acidity of the substrate. Since glutathione S-transferase (a gene coding this enzyme is located in the downstream of the peg operon) is localized in the cytoplasm and suggested to buffer the toxicity of PEG-carboxylateCoA, 29) the role of acyl-CoA synthetase might be to buffer the toxicity of PEG-carboxylate (perhaps a low molecular size) together with glutathione S-transferase.…”

“…All the metabolic enzymes included in PEG degradation have been localized in the membrane and are thought to work in the periplasm, in accordance with the fact that PEG and its metabolites were detected in the periplasmic fraction (unpublished data), suggesting that PEG is taken up into the periplasm and metabolized there. We cloned the genes involved in PEG degradation, and found that the peg operon consisted of five genes and was expressed by PEG through induction of an araCtype regulator, [26][27][28] as shown in Fig. 2.…”