1. The linkage of sugar phosphate polymer to peptidoglycan in walls of Micrococcus sp. 2102
- Author
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J Heptinstall, A.R. Archibald, John Coley, James Baddiley, and P J Ward
- Subjects
Chemical Phenomena ,Polymers ,Stereochemistry ,Trimer ,Peptidoglycan ,Biochemistry ,Micrococcus ,Residue (chemistry) ,chemistry.chemical_compound ,Cell Wall ,Glycerol ,Organic chemistry ,Sugar ,Molecular Biology ,chemistry.chemical_classification ,Sugar phosphates ,Chemistry ,Hydrolysis ,Periodate ,Cell Biology ,Phosphate ,Glycerophosphates ,Sugar Phosphates ,Protein Binding ,Research Article - Abstract
1. Protein-free walls of Micrococcus sp. 2102 contain peptidoglycan, poly-(N-acetylglucosamine 1-phosphate) and small amounts of glycerol phosphate. 2. After destruction of the poly-(N-acetylglucosamine 1-phosphate) with periodate, the glycerol phosphate remains attached to the wall, but can be removed by controlled alkaline hydrolysis. The homogeneous product comprises a chain of three glycerol phosphates and an additional phosphate residue. 3. The poly-(N-acetylglucosamine 1-phosphate) is attached through its terminal phosphate to one end of the tri(glycerol phosphate). 4. The other end of the glycerol phosphate trimer is attached through its terminal phosphate to the 3-or 4-position of an N-acetylglucosamine. It is concluded that the sequence of residues in the sugar 1-phosphate polymer-peptidoglycan complex is: (N-acetylglucosamine 1-phosphate)24-(glycerol phosphate)3-N-acetylglucosamine 1-phosphate-muramic acid (in peptidoglycan). Thus in this organism the phosphorylated wall polymer is attached to the peptidoglycan of the wall through a linkage unit comprising a chain of three glycerol phosphate residues and an N-acetylglucosamine 1-phosphate, similar to or identical with the linkage unit in Staphylococcus aureus H.
- Published
- 1978
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