Incorporation of proline into prodigiosin by a Put mutant of Serratia marcesens.
A Put mutant of Serratia marcescens, deficient in proline oxidase and therefore unable to degrade proline, was used to assay for an enzymatic reaction responsible for incorporation of proline into prodigiosin. The reaction had a pH optimum of 7.5 and a Km of 1.1 X 10(-4) M at 27 C. At temperatures above 27 C, the velocity of the reaction decreased with increasing temperature and little activity was detected at 42 C. Activity of the enzyme was directly proportional to the quantity of pigment formed and was inhibited by thioproline, a substrate analog. These data suggested the presence of a unique and specific enzyme in the biosynthetic pathway for prodigiosin.
Incorporation of proline into prodigiosin by a Put mutant of Serratia marcesens. A Put mutant of Serratia marcescens, deficient in proline oxidase and therefore unable to degrade proline, was used to assay for an enzymatic reaction responsible for incorporation of proline into prodigiosin. The reaction had a pH optimum of 7.5 and a Km of 1.1 X 10(-4) M at 27 C. At temperatures above 27 C, the velocity of the reaction decreased with increasing temperature and little activity was detected at 42 C. Activity of the enzyme was directly proportional to the quantity of pigment formed and was inhibited by thioproline, a substrate analog. These data suggested the presence of a unique and specific enzyme in the biosynthetic pathway for prodigiosin.