1887

Abstract

is known to break down arginine by the arginine deiminase pathway. An additional pathway has now been found whereby arginine is converted to putres-cine with agmatine and -carbamoylputrescine as intermediates. The following enzyme activities belonging to this pathway were detected in crude extracts: arginine decarboxylase (EC 4.1.1.19), which catalyses the release of CO from arginine to give agmatine; agmatine deiminase (EC 3.5.3.12), which degrades agmatine to -carbamoylputrescine; and -carbamoylputrescine amidinohydrolase (EC 3.5.3.-), which then removes the ureido group of carbamoylputrescine. In crude extracts, arginine decarboxylase activity was stimulated by pyridoxal phosphate, Mg and by the products of the catabolic pathway, putrescine and spermidine.

Growth of on arginine as the sole carbon and nitrogen source markedly increased the activity of arginine decarboxylase. Agmatine and -carbamoylputrescine induced the synthesis of agmatine deiminase and -carbamoylputrescine hydrolase. Addition of succinate or citrate to medium containing arginine or agmatine led to repression of the agmatine deiminase and -carbamoylputrescine hydrolase was further increased when was grown in media with agmatine plus glutamine or agmatine plus succinate and ammonia. This suggests that the expression of the agmatine pathway may be regulated by carbon catabolite repression as well as nitrogen catabolite repression.

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1980-02-01
2021-05-12
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