Peptidoglycan in the context of "Gram-negative bacterium"

Play Trivia Questions online!

or

Skip to study material about Peptidoglycan in the context of "Gram-negative bacterium"

Ad spacer

>>>PUT SHARE BUTTONS HERE<<<
In this Dossier

Peptidoglycan in the context of Cell wall

A cell wall is a structural layer that surrounds some cell types, found immediately outside the cell membrane. It can be tough, flexible, and sometimes rigid. Primarily, it provides the cell with structural support, shape, protection, and functions as a selective barrier. Another vital role of the cell wall is to help the cell withstand osmotic pressure and mechanical stress. While absent in many eukaryotes, including animals, cell walls are prevalent in other organisms such as fungi, algae and plants, and are commonly found in most prokaryotes, with the exception of mollicute bacteria.

The composition of cell walls varies across taxonomic groups, species, cell type, and the cell cycle. In land plants, the primary cell wall comprises polysaccharides like cellulose, hemicelluloses, and pectin. Often, other polymers such as lignin, suberin or cutin are anchored to or embedded in plant cell walls. Algae exhibit cell walls composed of glycoproteins and polysaccharides, such as carrageenan and agar, distinct from those in land plants. Bacterial cell walls contain peptidoglycan, while archaeal cell walls vary in composition, potentially consisting of glycoprotein S-layers, pseudopeptidoglycan, or polysaccharides. Fungi possess cell walls constructed from the polymer chitin, specifically N-acetylglucosamine. Diatoms have a unique cell wall composed of biogenic silica.

↑ Return to Menu

Peptidoglycan in the context of Gram-negative bacteria

Gram-negative bacteria are bacteria that, unlike Gram-positive bacteria, do not retain the crystal violet stain used in the Gram staining method of bacterial differentiation. Their defining characteristic is that their cell envelope consists of a thin peptidoglycan cell wall sandwiched between an inner (cytoplasmic) membrane and an outer membrane. These bacteria are found in all environments that support life on Earth.

Within this category, notable species include the model organism Escherichia coli, along with various pathogenic bacteria, such as Pseudomonas aeruginosa, Chlamydia trachomatis, and Yersinia pestis. They pose significant challenges in the medical field due to their outer membrane, which acts as a protective barrier against numerous antibiotics (including penicillin), detergents that would normally damage the inner cell membrane, and the antimicrobial enzyme lysozyme produced by animals as part of their innate immune system. Furthermore, the outer leaflet of this membrane contains a complex lipopolysaccharide (LPS) whose lipid A component can trigger a toxic reaction when the bacteria are lysed by immune cells. This reaction may lead to septic shock, resulting in low blood pressure, respiratory failure, reduced oxygen delivery, and lactic acidosis.

↑ Return to Menu

Peptidoglycan in the context of Otto Kandler

Otto Kandler (23 October 1920 in Deggendorf – 29 August 2017 in Munich, Bavaria) was a German botanist and microbiologist. Until his retirement in 1986 he was professor of botany at the Ludwig Maximilian University of Munich.

His most important research topics were photosynthesis, plant carbohydrate metabolism, analysis of the structure of bacterial cell walls (murein/peptidoglycan), the systematics of Lactobacillus, and the chemotaxonomy of plants and microorganisms.He presented the first experimental evidence for the existence of photophosphorylation in vivo. His discovery of the basic differences between the cell walls of bacteria and archaea (up to 1990 called "archaebacteria") convinced him that archaea represent an autonomous group of organisms distinct from bacteria. This was the basis for his cooperation with Carl Woese and made him the founder of research on the Archaea in Germany. In 1990, together with Woese, he proposed the three domains of life: Bacteria, Archaea, Eucarya. Finally, on the basis of his lifelong interest in the early evolution and diversification of life on this planet, Kandler presented his pre-cell theory, suggesting that the three domains of life did not emerge from an ancestral cell, e.g. the last universal common ancestor (LUCA), but from a population of pre-cells.

↑ Return to Menu

Peptidoglycan in the context of Alphaproteobacteria

Alphaproteobacteria or α-proteobacteria, also called α-Purple bacteria in earlier literature, is a class of bacteria in the phylum Pseudomonadota (also called "Proteobacteria"). The Magnetococcales and Mariprofundales are considered basal or sister to the Alphaproteobacteria. The Alphaproteobacteria are highly diverse and possess few commonalities, but nevertheless share a common ancestor. Like all proteobacteria, its members are gram-negative, although some of its intracellular parasitic members lack peptidoglycan and are consequently gram variable.

↑ Return to Menu

Peptidoglycan in the context of Gram-positive bacteria

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.

The Gram stain is used by microbiologists to place bacteria into two main categories, Gram-positive (+) and Gram-negative (−). Gram-positive bacteria have a thick layer of peptidoglycan within the cell wall, and Gram-negative bacteria have a thin layer of peptidoglycan.

↑ Return to Menu

Peptidoglycan in the context of Active site

In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of amino acid residues that form temporary bonds with the substrate, the binding site, and residues that catalyse a reaction of that substrate, the catalytic site. Although the active site occupies only ~10–20% of the volume of an enzyme, it is the most important part as it directly catalyzes the chemical reaction. It usually consists of three to four amino acids, while other amino acids within the protein are required to maintain the tertiary structure of the enzymes.

Each active site is evolved to be optimised to bind a particular substrate and catalyse a particular reaction, resulting in high specificity. This specificity is determined by the arrangement of amino acids within the active site and the structure of the substrates. Sometimes enzymes also need to bind with some cofactors to fulfil their function. The active site is usually a groove or pocket of the enzyme which can be located in a deep tunnel within the enzyme, or between the interfaces of multimeric enzymes. An active site can catalyse a reaction repeatedly as residues are not altered at the end of the reaction (they may change during the reaction, but are regenerated by the end). This process is achieved by lowering the activation energy of the reaction, so more substrates have enough energy to undergo reaction.

↑ Return to Menu

Peptidoglycan in the context of Alanine

Alanine (symbol Ala or A), or α-alanine, is an α-amino acid that is used in the biosynthesis of proteins. It contains an amine group and a carboxylic acid group, both attached to the central carbon atom which also carries a methyl group side chain. Consequently it is classified as a non-polar, aliphatic α-amino acid. Under biological conditions, it exists in its zwitterionic form with its amine group protonated (as −NH+3) and its carboxyl group deprotonated (as −CO2). It is non-essential to humans as it can be synthesized metabolically and does not need to be present in the diet. It is encoded by all codons starting with GC (GCU, GCC, GCA, and GCG).

The L-isomer of alanine (left-handed) is the one that is incorporated into proteins. L-alanine is second only to L-leucine in rate of occurrence, accounting for 7.8% of the primary structure in a sample of 1,150 proteins. The right-handed form, D-alanine, occurs in peptides in some bacterial cell walls (in peptidoglycan) and in some peptide antibiotics, and occurs in the tissues of many crustaceans and molluscs as an osmolyte.

↑ Return to Menu

Peptidoglycan in the context of N-Acetylglucosamine

N-Acetylglucosamine (GlcNAc) is an amide derivative of the monosaccharide glucose. It is a secondary amide between glucosamine and acetic acid. It is significant in several biological systems.

It is part of a biopolymer in the bacterial cell wall, which is built from alternating units of GlcNAc and N-acetylmuramic acid (MurNAc), cross-linked with oligopeptides at the lactic acid residue of MurNAc. This layered structure is called peptidoglycan (formerly called murein).

↑ Return to Menu

Peptidoglycan in the context of Mollicutes

Mollicutes is a class of bacteria distinguished by the absence of a cell wall and its peptidoglycan. The word Mollicutes is derived from Latin mollis 'soft, pliable' and cutis 'skin'. Individuals are very small, typically only 0.2–0.3 μm (200–300 nm) in size and have a very small genome size. They vary in form, although most have sterols that make the cell membrane somewhat more rigid. Many move about by gliding, but members of the genus Spiroplasma are helical and move by twisting. The best-known genus in the Mollicutes is Mycoplasma, though it has been split in 2018 into several genera. Colonies show the typical "fried-egg" appearance.

Mollicutes can be parasitic or saprotrophic. They can be parasites of various animals and plants, living on or in the host's cells. Many cause diseases in humans, attaching to cells in the respiratory or urogenital tracts, particularly species of Mycoplasma and Ureaplasma. Phytoplasma and Spiroplasma are plant pathogens associated with insect vectors.

↑ Return to Menu