Substrate specificity and some physicochemical properties of autolytic enzymes of the bacterium Lysobacter sp. XL 1

The substrate specificity of autolytic enzymes of the bacterium Lysobacter sp. XL 1 has been established. The periplasmic enzyme A8, the cytosolic enzyme A1, and the enzyme A10 solubilized from the cell walls and membranes with Triton X-100 exhibit glucosaminidase activity; the cytosolic enzyme A4 a...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2007-07, Vol.72 (7), p.760-765
Main Authors: Tsfasman, I M, Sitkin, B V, Lysanskaya, V Ya, Stepnaya, O A, Kulaev, I S
Format: Article
Language:English
Subjects:
Amidohydrolases - metabolism
Bacterial Proteins - metabolism
Cell Wall - enzymology
Cytosol - enzymology
Endopeptidases - metabolism
Enzymes
Hexosaminidases - metabolism
Hydrogen-Ion Concentration
Lysobacter - enzymology
Muramidase - metabolism
Peptidoglycans
Physicochemical properties
Properties
Substrate Specificity
Temperature
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Summary:The substrate specificity of autolytic enzymes of the bacterium Lysobacter sp. XL 1 has been established. The periplasmic enzyme A8, the cytosolic enzyme A1, and the enzyme A10 solubilized from the cell walls and membranes with Triton X-100 exhibit glucosaminidase activity; the cytosolic enzyme A4 and the enzyme A9 solubilized from the cell walls and membranes with LiCl exhibit the muramidase activity. The cytosolic enzymes A3 and A6 have N-acetylmuramoyl-L-alanine amidase activity, and the enzyme A5 exhibits the diaminopimelinoyl-alanine endopeptidase activity. Some physicochemical properties of the most active autolytic cytosolic enzymes of Lysobacter sp. XL 1 (endopeptidases A5 and A7 and N-acetylmuramoyl-L-alanine amidase A6) were studied. The enzymes exhibit maximal activity over a wide range of buffer concentrations in weakly alkaline medium and moderate temperatures. The investigated enzymes are comparatively thermolabile proteins.
ISSN:0006-2979
1608-3040
0320-9725
DOI:10.1134/S0006297907070103