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 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.
Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia.
I M
IM
Tsfasman
B V
BV
Sitkin
V Ya
VY
Lysanskaya
O A
OA
Stepnaya
I S
IS
Kulaev
D000581:Amidohydrolases / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D002473:Cell Wall / Q000201:enzymology*; D003600:Cytosol / Q000201:enzymology; D010450:Endopeptidases / Q000378:metabolism; D006596:Hexosaminidases / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D053528:Lysobacter / Q000201:enzymology*; D009113:Muramidase / Q000378:metabolism; D013379:Substrate Specificity; D013696:Temperature
D001426:Bacterial Proteins; D006596:Hexosaminidases; D009113:Muramidase; D010450:Endopeptidases; D000581:Amidohydrolases; C019665:amidase