Dephosphorylation of C<sub>55</sub>‐isoprenyl‐monophosphate by non‐specific phosphatases

Bohnenberger, Elisabeth; Sandermann, Heinrich

doi:10.1016/0014-5793(76)80875-7

Cited by 7 publications

(5 citation statements)

References 25 publications

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“…Only one report on the characterization of a C 55 ‐P phosphatase had been published to date (Willoughby et al , 1972) but a potential involvement of nonspecific phosphatases that could explain the generation of the large pool of C 55 ‐OH was also suggested (Bohnenberger & Sandermann, 1976). The C 55 ‐P phosphatase activity detected in particulate fractions from S. aureus did not require any cation, was optimal at pH 5, and had an apparent K m for C 55 ‐P of 1.5 μM (Willoughby et al , 1972).…”

Section: Undecaprenyl Phosphate Metabolismmentioning

confidence: 99%

The biosynthesis of peptidoglycan lipid-linked intermediates

et al. 2008

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The biosynthesis of bacterial cell wall peptidoglycan is a complex process involving many different steps taking place in the cytoplasm (synthesis of the nucleotide precursors) and on the inner and outer sides of the cytoplasmic membrane (assembly and polymerization of the disaccharide-peptide monomer unit, respectively). This review summarizes the current knowledge on the membrane steps leading to the formation of the lipid II intermediate, i.e. the substrate of the polymerization reactions. It makes the point on past and recent data that have significantly contributed to the understanding of the biosynthesis of undecaprenyl phosphate, the carrier lipid required for the anchoring of the peptidoglycan hydrophilic units in the membrane, and to the characterization of the MraY and MurG enzymes which catalyze the successive transfers of the N-acetylmuramoyl-peptide and N-acetylglucosamine moieties onto the carrier lipid, respectively. Enzyme inhibitors and antibacterial compounds interfering with these essential metabolic steps and interesting targets are presented.

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Section: Undecaprenyl Phosphate Metabolismmentioning

confidence: 99%

The biosynthesis of peptidoglycan lipid-linked intermediates

et al. 2008

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“…The source of free undecaprenol is not well understood. Perhaps it is generated by phosphatase/pyrophosphatase cleavage of undecaprenyl phosphate and/or pyrophosphate (see (9)) or perhaps it is directly generated as the byproduct of one or more yet-to-be-discovered biosynthetic pathways. In any case it has been known for many years that Gram-positive bacteria contain a UDPK activity (27–29,38,81).…”

Section: Proteomics and Microbial Physiologymentioning

confidence: 99%

Prokaryotic Diacylglycerol Kinase and Undecaprenol Kinase

Horn¹,

Sanders

2012

Annu. Rev. Biophys.

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Prokaryotic diacylglycerol kinase (DAGK) and undecaprenol kinase (UDPK) are the lone members of a family of multispan membrane enzymes that are very small, lack relationships to any other family of proteins—including water soluble kinases, and that exhibit an unusual structure and active site architecture. Escherichia coli DAGK plays an important role in recycling diacylglycerol produced as a byproduct of biosynthesis of molecules located in the periplasmic space. UDPK seems to play an analogous role in Gram-positive bacteria, where its importance is evident by the fact that UDPK is essential for biofilm formation by the oral pathogen Streptococcus mutans. DAGK has also long served as a model system for studies of membrane protein biocatalysis, folding, stability, and structure. This review explores our current understanding of the microbial physiology, enzymology, structural biology, and folding of the prokaryotic diacylglycerol kinase family, which is based on over 40 years of studies.

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“…Protein was determined by a modified Lowry procedure [6]. Radioactivity was determined by liquid scintillation counting [13,14].…”

Section: Methodsmentioning

confidence: 99%

Diglyceride Kinase from Escherichia coli

Bohnenberger

Sandermann

1979

European Journal of Biochemistry

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The diglyceride kinase activity of membranes from Escherichia coli was extracted into acidic butan-1-01. The enzyme was purified in organic solvent by precipitation at -20 "C, chromatography on DEAE-cellulose and repeated chromatography on Sephadex LH-60. The final 1460-fold purified enzyme preparation gave a single protein band upon isoelectric focusing in the presence of Triton X-100 (PI, 4.0) and upon polyacrylamide-gel electrophoresis in the presence of sodium dodecylsulphate. The latter method as well as gel chromatography on Sephadex LH-60 indicated a molecular weight of about 15 400.The purified enzyme was devoid of lipid, and it required re-addition of lipid for activity. sn-1,2-Dipalmitate and ceramide were phosphorylated, whereas the Css-isoprenoid alcohol, ficaprenol, did not serve as a substrate under the same conditions. Conversely, the butanol-soluble Cssisoprenoid-alcohol kinase from Staphylococcus aureus did not phosphorylate sn-l,2-dipalmitate.

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Dephosphorylation of C₅₅‐isoprenyl‐monophosphate by non‐specific phosphatases

Cited by 7 publications

References 25 publications

The biosynthesis of peptidoglycan lipid-linked intermediates

The biosynthesis of peptidoglycan lipid-linked intermediates

Prokaryotic Diacylglycerol Kinase and Undecaprenol Kinase

Diglyceride Kinase from Escherichia coli

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Dephosphorylation of C55‐isoprenyl‐monophosphate by non‐specific phosphatases

Cited by 7 publications

References 25 publications

The biosynthesis of peptidoglycan lipid-linked intermediates

The biosynthesis of peptidoglycan lipid-linked intermediates

Prokaryotic Diacylglycerol Kinase and Undecaprenol Kinase

Diglyceride Kinase from Escherichia coli

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Product

Resources

About

Dephosphorylation of C₅₅‐isoprenyl‐monophosphate by non‐specific phosphatases