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PMID: 3109395 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Purification and properties of a germination-specific cortex-lytic enzyme from spores of Bacillus megaterium KM.

The Biochemical journal ·Vol. 242 ·No. 2 ·1987-03-01 ·Pages 573-9

Foster SJ, Johnstone K

Abstract

Two peptidoglycan-lytic enzyme activities were isolated from spores of Bacillus megaterium KM. Surface-bound lytic enzyme was extracted from dormant spores and hydrolysed a variety of peptidoglycan substrates including isolated spore cortex, but did not cause refractility changes in permeabilized spores. Germination-specific lytic enzyme activity appeared early in germination and had minimal activity on isolated peptidoglycan substrates, but caused refractility changes in permeabilized spores of several Bacillus isolated peptidoglycan substrates, but caused refractility changes in permeabilized spores of several Bacillus species. The germination-specific lytic enzyme was shown to be a heat-sensitive 29 kDa protein with maximal activity at pH 6.5. It catalysed post-commitment muramic acid delta-lactam synthesis and displayed an inhibitor profile similar to that for post-commitment A600 loss. The relationship of the germination-specific enzyme to a recently proposed model of spore germination is discussed.

MeSH Terms
Bacillus megaterium/enzymology,physiology Bacterial Proteins Chromatography, Gel Electrophoresis, Polyacrylamide Gel Hydrogen-Ion Concentration Hydrolases/antagonists & inhibitors,isolation & purification,metabolism Permeability Spores, Bacterial/enzymology,physiology Substrate Specificity Temperature Trypsin/pharmacology
Chemicals
Bacterial Proteins Hydrolases peptidoglycan-lytic enzyme, Bacillus megaterium Trypsin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Foster S J
Johnstone K
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30 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2420573
Published
1987-03-01
Pages
573-9
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1147743
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2420573 PMC Full Text View journal details
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