1887

Abstract

A high -asparaginase (-asparagine amidohydrolase; EC 3.5.1.1) activity was found under conditions of lysine overproduction in cultures of . -Asparaginase was purified 98-fold by protamine sulphate precipitation, DEAE-Sephacel anion exchange, ammonium sulphate precipitation and Sephacryl S-200 gel filtration. The asparaginase protein was subjected to PAGE under non-denaturing conditions, identified by an reaction and eluted from the gel in an active form. The estimated from gel filtration and SDS-PAGE was 80000. The -asparaginase activity was inhibited by the -asparagine analogue 5-diazo-4-oxo--norvaline. Neither -asparagine nor -glutamine was a substrate for the enzyme. -Asparaginase was produced constitutively; its role may be that of an overflow enzyme, converting excess asparagine into aspartic acid, the direct precursor of lysine and threonine.

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1990-03-01
2021-07-26
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