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PMID: 7789526 Published · ppublish English Journal Article

Cloning and controlled overexpression of the gene encoding the 35 kDa soluble lytic transglycosylase from Escherichia coli.

FEBS letters ·Vol. 366 ·No. 2-3 ·1995-06-12 ·Pages 115-8

Dijkstra AJ, Hermann F, Keck W

Abstract

The lytic transglycosylases of Escherichia coli are involved in peptidoglycan metabolism and resemble the lysozymes not only in activity, but in the case of the 70 kDa soluble lytic transglycosylase (Slt70), also structurally. Here we report the cloning of the gene that encodes the 35 kDa soluble lytic transglycosylase (Slt35) of E. coli. Based on the sequence of the full-length gene, Slt35 is very likely to be a proteolytically truncated form of a slightly larger protein. The homology between Slt35 and Slt70, albeit poor, indicates that the active site architecture of both proteins may be alike. Using the T-7 promoter system, Slt35 was overproduced in large quantities and purified to homogeneity for crystallographic purposes.

MeSH Terms
Amino Acid Sequence Bacterial Proteins/biosynthesis,genetics Base Sequence Binding Sites Cloning, Molecular Escherichia coli/enzymology,genetics Gene Expression Genes, Bacterial Glycosyltransferases/biosynthesis,genetics Molecular Sequence Data Recombinant Fusion Proteins/biosynthesis,genetics Sequence Alignment
Chemicals
Bacterial Proteins Recombinant Fusion Proteins Glycosyltransferases murein transglycosylase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Dijkstra A J
Pharma Research Department, Hoffmann-La Roche Ltd., Basel, Switzerland.
Hermann F
Keck W
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1995-06-12
Pages
115-8
Language
English
Region
England
NLM ID
0155157
Subset
IM
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