dadamowiki

A wikipedia of Dr. D'Adamo's research



Difference (from prior minor revision)

Changed: 8c8

< Antibacterial drugs such as penicillin target the peptidoglycan layer by interfering with its formation, specifically the crosslinking enzyme transpeptidase. Mutations in the transpeptidase enzyme (also known as penicillin binding protein or PBP) which lead to reduced interactions between an antibiotic and the bacterial PBPs are a significant cause of emerging antibiotic resistance.

to

> Antibacterial drugs such as penicillin target the peptidoglycan layer by interfering with its formation, specifically the crosslinking enzyme transpeptidase. [[Mutation]]s in the transpeptidase enzyme (also known as penicillin binding protein or PBP) which lead to reduced interactions between an antibiotic and the bacterial PBPs are a significant cause of emerging antibiotic resistance.

Changed: 10c10

< The peptidoglycan layer in the bacterial cell wall is a crystal lattice structure formed from linear chains of two alternating amino sugars, namely N-acetyl glucosamine ([[GlcNAc]]) and [[N-acetyl muramic acid]] (MurNAc). Each MurNAc is attached to a short (4 to 5 residue) amino acid chain. Cross-linking between amino acids in different linear amino sugar chains by an enzyme known as transpeptidase result in a 3-dimensional structure that is strong and rigid. The specific amino acid sequence and molecular structure vary with the bacterial species.

to

> The peptidoglycan layer in the bacterial cell wall is a crystal lattice structure formed from linear chains of two alternating amino sugars, namely [[N-acetyl glucosamine]] (GlcNAc) and [[N-acetyl muramic acid]] (MurNAc). Each MurNAc is attached to a short (4 to 5 residue) amino acid chain. Cross-linking between amino acids in different linear amino sugar chains by an enzyme known as transpeptidase result in a 3-dimensional structure that is strong and rigid. The specific amino acid sequence and molecular structure vary with the bacterial species.


Immunology?

See Also

  • [Pattern recognition receptors]?

Description

Peptidoglycan, also known as murein, is a polymer consisting of sugars and amino acids that forms a homogeneous layer outside the plasma membrane of eubacteria. Archaea have a similar layer of pseudopeptidoglycan. Peptidoglycan serves a structural role in the bacterial cell wall, giving the wall shape and structural strength, as well as counteracting the osmotic pressure of the cytoplasm. Peptidoglycan is also involved in binary fission during bacterial cell reproduction.

The peptidoglycan layer is substantially thicker in Gram-positive bacteria (20 to 80 nm) than in Gram-negative bacteria (7 to 8 nm), with the attachment of the S-layer. Peptidoglycan forms around 90% of the dry weight of Gram-positive bacteria but only 10% of Gram-negative strains.

Antibiotic inhibition

Antibacterial drugs such as penicillin target the peptidoglycan layer by interfering with its formation, specifically the crosslinking enzyme transpeptidase. Mutation?s in the transpeptidase enzyme (also known as penicillin binding protein or PBP) which lead to reduced interactions between an antibiotic and the bacterial PBPs are a significant cause of emerging antibiotic resistance.

Structure

The peptidoglycan layer in the bacterial cell wall is a crystal lattice structure formed from linear chains of two alternating amino sugars, namely N-acetyl glucosamine (GlcNAc) and N-acetyl muramic acid (MurNAc). Each MurNAc is attached to a short (4 to 5 residue) amino acid chain. Cross-linking between amino acids in different linear amino sugar chains by an enzyme known as transpeptidase result in a 3-dimensional structure that is strong and rigid. The specific amino acid sequence and molecular structure vary with the bacterial species.

References

1. Madigan M; Martinko J (editors). (2005). Brock Biology of Microorganisms, 11th ed., Prentice Hall. ISBN 0131443291 (alternate, search).

2. a b Salton MRJ, Kim KS (1996). Structure. In: Baron's Medical Microbiology (Barron S et al, eds.), 4th ed., Univ of Texas Medical Branch. (via NCBI Bookshelf) ISBN 0-9631172-1-1 (alternate, search).

3. Spratt BG (1994). "Resistance to antibiotics mediated by target alterations". Science 264 (5157): 388-93. PMID 8153626.

4. Ryan KJ; Ray CG (editors) (2004). Sherris Medical Microbiology, 4th ed., McGraw Hill. ISBN 0838585299 (alternate, search).

Links

Attribution

SPOTLIGHT

COMPLETE BLOOD TYPE ENCYCLOPEDIA


The Complete Blood Type Encyclopedia is the essential desk reference for Dr. D'Adamo's work. This is the first book to draw on the thousands of medical studies proving the connection between blood type and disease.

Click to learn more

Click the Play button to hear to Dr. Peter J. D'Adamo discuss .



The statements made on our websites have not been evaluated by the FDA (U.S. Food & Drug Administration).
Our products and services are not intended to diagnose, cure or prevent any disease. If a condition persists, please contact your physician.
Copyright © 2015-2023, Hoop-A-Joop, LLC, Inc. All Rights Reserved.     Log In