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.
Tsfasman
I M
IM
Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia.
Sitkin
B V
BV
Lysanskaya
V Ya
VY
Stepnaya
O A
OA
Kulaev
I S
IS
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