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PMID: 6998964 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Two different species of murein transglycosylase in Escherichia coli.

Journal of bacteriology ·Vol. 144 ·No. 1 ·1980-10-00 ·Pages 45-52

Mett H, Keck W, Funk A, Schwarz U

Abstract

We demonstrated that Escherichia coli murein transglycosylase exists in two forms. After mechanical disruption of the cells, one form was found in the soluble fraction and the other, in the cell envelope. The two enzymes differed with respect to molecular weight, isoelectric point, solubility in aqueous buffers, and to some extent in their requirements for maximal catalytic activity. The molecular weight of the membrane-bound transglycosylase (35,000) was half that of the soluble enzyme. Whether the high-molecular-weight soluble protein is a precursor of the membrane-bound enzyme species remains to be elucidated.

MeSH Terms
Cell Membrane/enzymology Escherichia coli/enzymology Glycosyltransferases Isoelectric Point Kinetics Molecular Weight Peptidoglycan Transferases/isolation & purification,metabolism
Chemicals
Peptidoglycan Transferases Glycosyltransferases murein transglycosylase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Mett H
Keck W
Funk A
Schwarz U
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23 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.144.1.45-52.1980
Published
1980-10-00
Pages
45-52
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC294584
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.144.1.45-52.1980 PMC Full Text View journal details
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