A three dimensional model of the digestion of peptidoglycan by lysozyme.

Biophysics of structure and mechanism ·Vol. 4 ·No. 1 ·1977-12-27 ·Pages 1-14

Formanek H

Abstract

The digestion of single peptidoglycan chains of the recently proposed conformation (Formanek et al., 1974) can be described with the same enzymatic mechanism as proposed by Phillips for a hexasaccharide consisting of alternating N-acetylglucosamine, N-acetylmuramic acid residues (Phillips, 1966). It is shown by model building, that in a peptidoglycan lysozyme complex the peptide chains do not exhibit any sterical hindrance. The digestion of the peptidoglycan sacculus by lysozyme may occur at latice defects of its paracrystalline structure. A slit of about 30 A length and 10--15 A width between peptidoglycan micells may be sufficient for the attachment of lysozyme.

MeSH Terms

Acetylglucosamine Chitin Glycopeptides/metabolism Models, Molecular Molecular Conformation Muramic Acids Muramidase/metabolism Peptidoglycan/metabolism Protein Conformation

Chemicals

Glycopeptides Muramic Acids Peptidoglycan Chitin Muramidase Acetylglucosamine

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Formanek H

References (17)

17 references, click to expand

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Article Info

Journal

Biophysics of structure and mechanism

Abbr.

Biophys Struct Mech

ISSN

0340-1057

DOI

10.1007/BF00538836

Published

1977-12-27

Pages

1-14

Language

English

Region

Germany

NLM ID

7502020

Subset

External Links

PubMed source DOI: 10.1007/BF00538836

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A three dimensional model of the digestion of peptidoglycan by lysozyme.

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