The purilication and certain propertics of L-asparagine dearnitlase of Bncilll~s coagz~la?ts a~~d Bacillz~s slearotker,i~opAil~ls are described. Masimum enzyme activity was obtained a t 55' C. ovct-a pII ranpc oi 7.5 to 8.5. The purifie,d dearnidase hyclrolyzec1 the L-isomer of a s p a r a g i~~c quantitatively to aspartlc acid and aminonia and did not attncli thc D-isonler. D--4sparagine inhibited the hydrolysis of the L-isomer. The Ii,,,, for the inhibition reaction was found to be 1.87X10-3 A&.. The cnzytne did not catalyze trarlsatnidation or hydrosyla~n i n c transfer rcactlolls. Enzyme activity \\-as inhibited by S-ethylmaleimide a11d p-chloro~nerc~~ribe~~zoate. The inhibition by these agcnts \\-as reversed by glutnthionc. I n the absence oi substrate the cle;unidase of both organis~ns was relati\~cly heat labile a t 55' C. 'I'he heat lability of this enzytne is discussed in relation to the heat stability of other enzyme systems of thcrmophilic microorganisms. il~uteriuls D-and L-Asparagine and the amino acids tested were obtained from the Nutritional Biochen~icals Corp. N-Ethylmaleimide and p-chioromercuribenzoate were purcl~ased froin the Manil Research Laboratories. Formamide, acetamide, propananlicle, n-butyramide, isobutyramide, valeramide, hexanlillanuscript
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