[Formation of L-asparagine and L-glutamine deamidases by bacterial cultures].
Among studied 40 bacterial cultures, 17 strains catalysed hydroxylaminolysis of I.-asparagine and L-glutamine, and among these cultures seven strains belonged to the Pseudomonas genus. Extracts of the cells of Ps. boreopolis 526 (MGU), Ps. aurantiaca IBFM B-14, and Ps. septica IBFM B-40 had the maximum deamidase activity during the stage of decelerated growth. The activity of L-asparaginase 2 was practically the same upon various ways of disintegration of the cells of Ps. aurantiaca IBFM B-14: ballistic technique, ultrasound, extrusion form the solid state. Production of beta-aspartylhydroxamic acid by L-asparaginase 2 depended on the concentration of hydroxylamine and protein in the reaction mixture and on the duration of the reaction.
D000421:Alcaligenes / Q000201:enzymology; D001215:Asparaginase / Q000096:biosynthesis*; D001419:Bacteria / Q000201:enzymology*; D002861:Chromobacterium / Q000201:enzymology; D004754:Enterobacter / Q000201:enzymology; D004926:Escherichia coli / Q000201:enzymology; D005972:Glutaminase / Q000096:biosynthesis*; D007527:Isoenzymes / Q000096:biosynthesis*; D011513:Proteus mirabilis / Q000201:enzymology; D011514:Proteus vulgaris / Q000201:enzymology; D012706:Serratia marcescens / Q000201:enzymology
D007527:Isoenzymes; D001215:Asparaginase; D005972:Glutaminase
Obrazovanie dezamidaz L-asparagina i L-glutamina bakterial'nymi kul'turami