Bactoprenol

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Bactoprenol
Bactoprenol.svg
Names
IUPAC name
(6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-3,7,11,15,19,23,27,31,35,39,43-undecamethyltetratetraconta-6,10,14,18,22,26,30,34,38,42-decaen-1-ol
Other names
Dolichol-11
Identifiers
3D model (JSmol)
ChemSpider
PubChem CID
  • InChI=1S/C55H92O/c1-45(2)23-13-24-46(3)25-14-26-47(4)27-15-28-48(5)29-16-30-49(6)31-17-32-50(7)33-18-34-51(8)35-19-36-52(9)37-20-38-53(10)39-21-40-54(11)41-22-42-55(12)43-44-56/h23,25,27,29,31,33,35,37,39,41,55-56H,13-22,24,26,28,30,32,34,36,38,40,42-44H2,1-12H3/b46-25+,47-27+,48-29-,49-31-,50-33-,51-35-,52-37-,53-39-,54-41- Yes check.svgY
    Key: BNAIICFZMLQZKW-LSTWDCEHSA-N Yes check.svgY
  • InChI=1S/C55H92O/c1-45(2)23-13-24-46(3)25-14-26-47(4)27-15-28-48(5)29-16-30-49(6)31-17-32-50(7)33-18-34-51(8)35-19-36-52(9)37-20-38-53(10)39-21-40-54(11)41-22-42-55(12)43-44-56/h23,25,27,29,31,33,35,37,39,41,55-56H,13-22,24,26,28,30,32,34,36,38,40,42-44H2,1-12H3/b46-25+,47-27+,48-29-,49-31-,50-33-,51-35-,52-37-,53-39-,54-41-
    Key: BNAIICFZMLQZKW-LSTWDCEHSA-N
  • C/C(C)=C/CC/C(C)=C/CC/C(C)=C/CC/C(C)=C\CC/C(C)=C\CC/C(C)=C\CC/C(C)=C\CC/C(C)=C\CC/C(C)=C\CC/C(C)=C\CCC(C)CCO
Properties
C55H92O
Molar mass 769.318 g·mol−1
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Yes check.svgY  verify  (what is  Yes check.svgYX mark.svgN ?)

Bactoprenol also known as dolichol-11 and (isomerically vaguely) C55-isoprenyl alcohol (C55-OH) is a lipid first identified in certain species of lactobacili. [1] It is a hydrophobic alcohol that plays a key role in the growth of cell walls (peptidoglycan) in Gram-positive bacteria. [2]

Contents

The double bonds all have the Z configuration except for the three ω-terminal ones, which are biosynthetically derived from (E,E)-farnesyl diphosphate. [3]

Occurrence

Bactoprenol is a lipid synthesized from mevalonic acid and is the most abundant lipid found in certain species of lactobacilli. [1] Bactoprenol is found in both mesosomal and plasma membranes. [4] Mesosomal and plasma bactoprenol are synthesized independently from each other. [5]

Function

Bactoprenol is thought to play a key role in the formation of cell walls in gram-positive bacteria by cycling peptidoglycan monomers through the plasma membrane and inserting these monomers at points of growth in the bacterial cell wall. [6]

Antibiotic significance

Because bactoprenol is so important for cell growth, numerous antibiotic compounds function by disrupting the bactoprenol-mediated transportation pathway. [7] This strategy was first identified by studying the antibiotic mechanism of friulimicin B. [8] Since then, other antibiotics that make use of a similar mechanism have been identified, including nisin [9] and lantibiotics such as NAI-107. [10]

Related Research Articles

Gram-positive bacteria Bacteria that give a positive result in the Gram stain test

In bacteriology, gram-positive bacteria are bacteria that give a positive result in the Gram stain test, which is traditionally used to quickly classify bacteria into two broad categories according to their type of cell wall.

Peptidoglycan or murein is a polymer consisting of sugars and amino acids that forms a mesh-like peptidoglycan layer outside the plasma membrane of most bacteria, forming the cell wall. The sugar component consists of alternating residues of β-(1,4) linked N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM). Attached to the N-acetylmuramic acid is a peptide chain of three to five amino acids. The peptide chain can be cross-linked to the peptide chain of another strand forming the 3D mesh-like layer. Peptidoglycan serves a structural role in the bacterial cell wall, giving structural strength, as well as counteracting the osmotic pressure of the cytoplasm. Peptidoglycan is also involved in binary fission during bacterial cell reproduction.

Bacteriocins are proteinaceous or peptidic toxins produced by bacteria to inhibit the growth of similar or closely related bacterial strain(s). They are similar to yeast and paramecium killing factors, and are structurally, functionally, and ecologically diverse. Applications of bacteriocins are being tested to assess their application as narrow-spectrum antibiotics.

Lanthionine Chemical compound

Lanthionine is a nonproteinogenic amino acid with the chemical formula (HOOC-CH(NH2)-CH2-S-CH2-CH(NH2)-COOH). It is typically formed by a cysteine residue and a dehydrated serine residue. Despite its name, lanthionine does not contain the element lanthanum.

Nisin Chemical compound

Nisin is a polycyclic antibacterial peptide produced by the bacterium Lactococcus lactis that is used as a food preservative. It has 34 amino acid residues, including the uncommon amino acids lanthionine (Lan), methyllanthionine (MeLan), didehydroalanine (Dha), and didehydroaminobutyric acid (Dhb). These unusual amino acids are introduced by posttranslational modification of the precursor peptide. In these reactions a ribosomally synthesized 57-mer is converted to the final peptide. The unsaturated amino acids originate from serine and threonine, and the enzyme-catalysed addition of cysteine residues to the didehydro amino acids result in the multiple (5) thioether bridges.

Lantibiotics are a class of polycyclic peptide antibiotics that contain the characteristic thioether amino acids lanthionine or methyllanthionine, as well as the unsaturated amino acids dehydroalanine, and 2-aminoisobutyric acid. They belong to ribosomally synthesized and post-translationally modified peptides.

The cell envelope comprises the inner cell membrane and the cell wall of a bacterium. In gram-negative bacteria an outer membrane is also included. This envelope is not present in the Mollicutes where the cell wall is absent.

Antimicrobial peptides

Antimicrobial peptides (AMPs), also called host defence peptides (HDPs) are part of the innate immune response found among all classes of life. Fundamental differences exist between prokaryotic and eukaryotic cells that may represent targets for antimicrobial peptides. These peptides are potent, broad spectrum antibiotics which demonstrate potential as novel therapeutic agents. Antimicrobial peptides have been demonstrated to kill Gram negative and Gram positive bacteria, enveloped viruses, fungi and even transformed or cancerous cells. Unlike the majority of conventional antibiotics it appears that antimicrobial peptides frequently destabilize biological membranes, can form transmembrane channels, and may also have the ability to enhance immunity by functioning as immunomodulators.

Lactic acid bacteria Order of bacteria

Lactobacillales are an order of gram-positive, low-GC, acid-tolerant, generally nonsporulating, nonrespiring, either rod-shaped (bacilli) or spherical (cocci) bacteria that share common metabolic and physiological characteristics. These bacteria, usually found in decomposing plants and milk products, produce lactic acid as the major metabolic end product of carbohydrate fermentation, giving them the common name lactic acid bacteria (LAB).

Penicillin-binding proteins

Penicillin-binding proteins (PBPs) are a group of proteins that are characterized by their affinity for and binding of penicillin. They are a normal constituent of many bacteria; the name just reflects the way by which the protein was discovered. All β-lactam antibiotics bind to PBPs, which are essential for bacterial cell wall synthesis. PBPs are members of a subgroup of enzymes called transpeptidases. Specifically, PBPs are DD-transpeptidases.

Levilactobacillus brevis is a gram-positive, rod shaped species of lactic acid bacteria which is heterofermentative, creating CO2, lactic acid and acetic acid or ethanol during fermentation. L. brevis is the type species of the genus Levilactobacillus (previously L. brevis group), which comprises 24 species (http://www.lactobacillus.ualberta.ca/, http://www.lactobacillus.uantwerpen.be/). It can be found in many different environments, such as fermented foods, and as normal microbiota. L.brevis is found in food such as sauerkraut and pickles. It is also one of the most common causes of beer spoilage. Ingestion has been shown to improve human immune function, and it has been patented several times. Normal gut microbiota L.brevis is found in human intestines, vagina, and feces.

In enzymology, a phospho-N-acetylmuramoyl-pentapeptide-transferase is an enzyme that catalyzes the chemical reaction

Lipid II:glycine glycyltransferase (EC 2.3.2.16, N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:N6-glycine transferase, femX (gene)) is an enzyme with systematic name alanyl-D-alanine-diphospho-ditrans, octacis-undecaprenyl-N-acetylglucosamine:glycine N6-glycyltransferase. This enzyme catalyses the following chemical reaction

N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase (EC 2.3.2.18, femB (gene)) is an enzyme with systematic name N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-ditrans,octacis-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase. This enzyme catalyses the following chemical reaction

Teixobactin is a peptide-like secondary metabolite of some species of bacteria, that kills some gram-positive bacteria. It appears to belong to a new class of antibiotics, and harms bacteria by binding to lipid II and lipid III, important precursor molecules for forming the cell wall.

Eleftheria terrae is a recently discovered Gram-negative bacterium. E. terrae is a temporary name for the organism, as it was only discovered in 2014 and is still undergoing scientific study. It was found to produce a previously unknown antibiotic named teixobactin. The discovery of E. terrae could represent a new age of antibiotics, as teixobactin is the first new antibiotic discovered since the synthetic era of the 1980s. Prior research has indicated that other uncultivable bacteria like E. terrae have potential in the development of new antimicrobial agents.

Lipid II Chemical compound

Lipid II is a precursor molecule in the synthesis of the cell wall of bacteria. It is a peptidoglycan, which is amphipathic and named for its bactoprenol hydrocarbon chain, which acts as a lipid anchor, embedding itself in the bacterial cell membrane. Lipid II must translocate across the cell membrane to deliver and incorporate its disaccharide-pentapeptide "building block" into the peptidoglycan mesh. Lipid II is the target of several antibiotics.

The bacterial murein precursor exporter (MPE) family is a member of the cation diffusion facilitator (CDF) superfamily of membrane transporters. Members of the MPE family are found in a large variety of Gram-negative and Gram-positive bacteria and facilitate the translocation of lipid-linked murein precursors. A representative list of proteins belonging to the MPE family can be found in the Transporter Classification Database.

The multidrug/oligosaccharidyl-lipid/polysaccharide (MOP) flippase superfamily is a group of integral membrane protein families. The MOP flippase superfamily includes twelve distantly related families, six for which functional data are available:

  1. One ubiquitous family (MATE) specific for drugs - (TC# 2.A.66.1) The Multi Antimicrobial Extrusion (MATE) Family
  2. One (PST) specific for polysaccharides and/or their lipid-linked precursors in prokaryotes - (TC# 2.A.66.2) The Polysaccharide Transport (PST) Family
  3. One (OLF) specific for lipid-linked oligosaccharide precursors of glycoproteins in eukaryotes - (TC# 2.A.66.3) The Oligosaccharidyl-lipid Flippase (OLF) Family
  4. One (MVF) lipid-peptidoglycan precursor flippase involved in cell wall biosynthesis - (TC# 2.A.66.4) The Mouse Virulence Factor (MVF) Family
  5. One (AgnG) which includes a single functionally characterized member that extrudes the antibiotic, Agrocin 84 - (TC# 2.A.66.5) The Agrocin 84 Antibiotic Exporter (AgnG) Family
  6. And finally, one (Ank) that shuttles inorganic pyrophosphate (PPi) - (TC# 2.A.66.9) The Progressive Ankylosis (Ank) Family

Heike Brötz-Oesterhelt is a German microbiologist. She is a full professor and holds the Chair of the Department for Microbial Bioactive Compounds at the Interfaculty Institute for Microbiology and Infection Medicine, University of Tübingen, Germany.

References

  1. 1 2 Thorne KJ, Kodicek E (April 1966). "The structure of bactoprenol, a lipid formed by lactobacilli from mevalonic acid". The Biochemical Journal. 99 (1): 123–7. doi:10.1042/bj0990123. PMC   1264965 . PMID   5965329.
  2. ↑ Kaiser, Gary (September 2018). "BIOL 230 Lecture Guide - Synthesis of Peptidoglycan - Role of Bactoprenol". faculty.ccbcmd.edu. Retrieved 2018-12-20.
  3. ↑ Jaenicke L, Siegmund HU (November 1989). "Synthesis and characterization of dolichols and polyprenols of designed geometry and chain length". Chemistry and Physics of Lipids. 51 (3–4): 159–70. doi:10.1016/0009-3084(89)90003-0.
  4. ↑ Barker DC, Thorne KJ (November 1970). "Spheroplasts of Lactobacillus casei and the cellular distribution of bactoprenol". Journal of Cell Science. 7 (3): 755–85. doi:10.1242/jcs.7.3.755. PMID   4250091.
  5. ↑ Thorne KJ, Barker DC (April 1972). "The occurrence of bactoprenol in the mesosome and plasma membranes of Lactobacillus casei and Lactobacillus plantarum". Journal of General Microbiology. 70 (1): 87–98. doi: 10.1099/00221287-70-1-87 . PMID   4625239.
  6. ↑ Kaiser G (September 2018). "BIOL 230 Lecture Guide - Synthesis of Peptidoglycan - Role of Bactoprenol". faculty.ccbcmd.edu. Retrieved 2018-12-20.
  7. ↑ Schneider T, Sahl HG (February 2010). "Lipid II and other bactoprenol-bound cell wall precursors as drug targets". Current Opinion in Investigational Drugs. 11 (2): 157–64. PMID   20112165.
  8. ↑ Schneider T, Gries K, Josten M, Wiedemann I, Pelzer S, Labischinski H, Sahl HG (April 2009). "The lipopeptide antibiotic Friulimicin B inhibits cell wall biosynthesis through complex formation with bactoprenol phosphate". Antimicrobial Agents and Chemotherapy. 53 (4): 1610–8. doi:10.1128/AAC.01040-08. PMC   2663061 . PMID   19164139.
  9. ↑ Scherer K, Wiedemann I, Ciobanasu C, Sahl HG, Kubitscheck U (November 2013). "Aggregates of nisin with various bactoprenol-containing cell wall precursors differ in size and membrane permeation capacity". Biochimica et Biophysica Acta (BBA) - Biomembranes. 1828 (11): 2628–36. doi: 10.1016/j.bbamem.2013.07.014 . PMID   23872123.
  10. ↑ Münch D, Müller A, Schneider T, Kohl B, Wenzel M, Bandow JE, Maffioli S, Sosio M, Donadio S, Wimmer R, Sahl HG (April 2014). "The lantibiotic NAI-107 binds to bactoprenol-bound cell wall precursors and impairs membrane functions". The Journal of Biological Chemistry. 289 (17): 12063–76. doi:10.1074/jbc.M113.537449. PMC   4002112 . PMID   24627484.
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