Undecaprenyl phosphate metabolism in Gram-negative and Gram-positive bacteria

Abstract

Undecaprenyl phosphate (UP) is essential for the biosynthesis of bacterial extracellular polysaccharides. UP is produced by the dephosphorylation of undecaprenyl diphosphate (UPP) via de novo synthetic and recycling pathways. Gram-positive bacteria contain remarkable amounts of undecaprenol (UOH), which is phosphorylated to UP, although UOH has not been found in Gram-negative bacteria. Here, current knowledge about UPP phosphatase and UOH kinase is reviewed. Dephosphorylation of UPP is catalyzed by a BacA homologue and a type-2 phosphatidic acid phosphatase (PAP2) homologue. The presence of one of these UPP phosphatases is essential for bacterial growth. The catalytic center of both types of enzyme is located outside the cytoplasmic membrane. In Gram-positive bacteria, an enzyme homologous to DgkA, which is the diacylglycerol kinase of Escherichia coli, catalyzes UOH phosphorylation. The possible role of UOH and the significance of systematic construction of Staphylococcus aureus mutants to determine UP metabolism are discussed.

Antibacterial Activity of Red Dragon Fruit Leaves Extract and White Dragon Fruit Leaves Extract Against Meningitis Bacterial

“…The cell structure of Gram positive bacteria is simpler, that is single layered with a low lipid content making it easier for bioactive ingredients to enter the cell. Gram negative bacterial cell wall structure is more complex, namely three layers consisting of an outer layer of lipoprotein, a middle layer of lipopolysacrida which acts as a barrier to the entry of antibacterial bioactive material, and an inner layer of peptidoglycan in high lipid content 23 . The higher the concentration of red dragon fruit leaves extract and white dragon fruit leaves extract shows the higher the antibacterial activity.…”

Undecaprenol kinase: Function, mechanism and substrate specificity of a potential antibiotic target

“…[4,39] pyrophosphate and eight isopentenyl pyrophosphate units, catalysed by undecaprenyl pyrophosphate synthase (UppS). [25,38] C55P is then generated through undecaprenyl pyrophosphate phosphatase (UppP)-catalysed dephosphorylation of C55PP. Alternatively, in glyco-polymer/protein syntheses, C55PP is a by-product left in the outer leaflet of the cytoplasmic membrane.…”

“…[9] Teichoic acid biosynthesis also utilises C55P as a transmembrane shuttle to transport carbohydrate, carbohydrate-peptide and glycerol phosphate building blocks across the cytoplasmic membrane and is essential in both Gram-positive and Gram-negative bacteria. [21,22][ [23][24][25] As well as being involved in peptidoglycan biosynthesis, it is also required for the synthesis of lipopolysaccharide (LPS). [26,27] LPS are large molecular protrusions which are anchored in and extend from the outer leaflet of the outer membrane.…”

Construction of Staphylococcus aureus Mutant Deficient in the Undecaprenol Kinase Gene, dgkA, and Elucidation of the Role of Undecaprenol Kinase in the Metabolism of Undecaprenyl Phosphate

“…Then, the sugar unit is incorporated into the growing polysaccharide chain by the action of the specific polymerase, and undecaprenyl diphosphate (UPP) is released at the outer side of the cytoplasmic membrane [3]. UP is produced in both de novo synthesis and recycling pathways by dephosphorylation of UPP [2,[4][5][6]. In the de novo synthesis pathway, UPP is synthesized by sequential condensations of isopentenyl diphosphate to farnesyl diphosphate by the action of UPP synthase [7][8][9] at the inner side of the cytoplasmic membrane.…”

“…The DgkA protein in Bacillus subtilis [19] and Streptococcus mutans [20], which is homologous to diacylglycerol kinase in Escherichia coli [21], catalyzes the phosphorylation of UOH. It is possible that phosphorylation of UOH is a third pathway to produce UP at least in Grampositive bacteria [2,[4][5][6]. To investigate the role of a DgkA homolog in UP metabolism in Staphylococcus aureus, we cloned the dgkA homolog of S. aureus, and constructed the deletion mutant.…”