• BMB Reports
• /
• v.28 no.5
• /
• pp.443-450
• /
• 1995

Cloned staphylococcal peptidoglycan hydrolase was used in determining the physiological characteristics of peptidoglycan hydrolase. This enzyme hydrolyzed the bacterial cell walls and released the N-terminal alanine, but not the reducing groups. This cloned gene product was localized in the cytoplasm of transformed Escherichia coli. Activity gels indicated the enzyme had an Mr of about 54,000, which was consistent with the deduced Mr from sequencing of the cloned gene. The activity bound to CM-cellulose but not DEAE-cellulose resin, indicating it as a basic protein. Enhanced enzyme activity in a low concentration of cations, and inhibited enzyme activity in a solution with dissolved phospholipids, suggested that the activity and the availability of this basic protein may be regulated between negatively charged and positively charged cellular molecules. The activity against boiled crude cell wall was much greater than against purifed cell wall, suggesting protein associated with crude cell wall may aid in the binding of the peptidoglycan hydrolase The cloned peptidoglycan hydrolase showed positive activity on whole cells of some lysostaphin-resistant coagulase-negative staphylococci. The cloned enzyme may be an alternative for lysostaphin for lysis of staphylococci.

• Archives of Pharmacal Research
• /
• v.22 no.5
• /
• pp.515-519
• /
• 1999

The biologically active peptidoglycan was purified form the alkali fraction of the fruiting bodies of Ganoderma lucidum and the composition of the peptidoglycan was investigated by conventional analyses. The alkali-extracted peptidoglycan showed differences in chemical compositions from the water-extracted. The alkali-extracted peptidoglycan contained 6.9% protein and 75.9% carbohydrates composed mainly of $\beta$-glucose, mannose, and $\alpha$-glucose. The molecular weight range of the peptidoglycan was determined as 2,000 kDa-17 kDa. The peptidoglycan is considered to be a hybrid molecule of polysaccaride chains covalently bound as a side chain to the polypeptide core.

• Korean Journal of Microbiology
• /
• v.41 no.4
• /
• pp.255-261
• /
• 2005

A 6.7kb DNA fragment containing the sprT gene encoding Streptomyces griseus trypsin (SGT) was cloned from Streptomyces griseus ATCC 10137, and the complete nucleotide sequence was determined. Nucleotide sequence and deduced amino acid or the EcoRI-HindIII fragment revealed the presence or the six complete ORFs containing the sprT gene and one incomplete ORF, which were named ORF1, SGT, ORF2, ORF3, ORF4, ORF5, and ORF6, respectively. ORF1 has homology with the oxidoreductases from several organisms. ORF2 and ORF3 show similarity with unknown proteins and transcription regulator that belongs to the ArsR family, respectively. ORF4 and ORF5 show homology with the peptidoglycan bound protein with LPXTG motif from Listeria monocytogenes and the membrane protein with transmembrane helix from several organisms, respectively. The last ORF, ORF6, shows homology with the lipoprotein from Streptomyces avermitilis.