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Hydrolysis of γ-glutamyl linkages by Fusobacterium nucleatum.
- Source :
- Current Microbiology; Jan1990, Vol. 20 Issue 1, p5-11, 7p
- Publication Year :
- 1990
-
Abstract
- The cell extracts of two human oral strains (FN2 and FN3) of Fusobacterium nucleatum displayed exceptionally high γ-glutamylpeptidase activity as determined with N-γ- l-glutamyl-2-naphthylamine as substrate. This activity was so dominant that the hydrolysis of other N-aminoacyl-2-naphthylamines progressed at a rate <10% of the former. Two major enzymes (I and II) were partially purified from FN2. I had a molecular weight of 115,000 and did not hydrolyze γ-glutamylcysteinylglycine (glutathione). II had a molecular weight of 70,000 and rapidly liberated only glutamic acid from glutathione. Strain FN3 contained several enzymes hydrolyzing γ-glu-2NA. Direct anion exchange chromatography of FN3 cell extracts separated one enzyme that liberated both glutamic acid and glycine from glutathione, one that was inactive against glutathione (but hydrolyzed γ-glu-2NA), and one that liberated only glutamic acid. Although γ-glu-2NA was a good synthetic substrate, glutathione was hydrolyzed at least 500 times faster by an enzyme present in both strains. These results indicate that the presence of γ-glutamylpeptidase activity is very characteristic of these F. nucleatum strains. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 03438651
- Volume :
- 20
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- Current Microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 70632546
- Full Text :
- https://doi.org/10.1007/BF02094016