Role of L-proline in the biosynthesis of prodigiosin.
Nonproliferating cells of Serratia marcescens, wild-type strain Nima, synthesized the pigment, prodigiosin, when saline suspensions were incubated with aeration at 27 degrees C in the presence of proline or alanine. Mutants PutS1 and PutS2 derived from strain Nima formed prodigiosin from alanine, but not from proline, unless alanine also was added. Strain Nima utilized proline as a sole source of carbon and of nitrogen for growth, whereas Put mutants did not. Investigation of enzymes degrading proline showed that the wild-type strain contained proline oxidase, which was absent in Put mutants. The wild type, as well as the mutants, utilized alanine as the sole source of carbon and nitrogen for growth. Although nonproliferating cells of Put mutants failed to synthesize prodigiosin from proline, addition of L-[U-14C]proline to suspensions metabolizing and synthesizing the pigment because of addition of alanine resulted in the incorporation of radioactive label into prodigiosin, as well as into cellular protein. Since Put mutants could not catabolize proline, the incorporation of [14C]proline into the prodigiosin molecule indicated that proline was incorporated directly into the pigment.
D000409:Alanine / Q000378:metabolism; D001426:Bacterial Proteins / Q000096:biosynthesis; D008769:Methylnitronitrosoguanidine; D009154:Mutation; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism; D011353:Prodigiosin / Q000378:metabolism*; D011392:Proline / Q000378:metabolism*; D012706:Serratia marcescens / Q000201:enzymology / Q000378:metabolism*; D013237:Stereoisomerism; D013696:Temperature
D001426:Bacterial Proteins; D008769:Methylnitronitrosoguanidine; D011392:Proline; D000587:Oxidoreductases Acting on CH-NH Group Donors; D000409:Alanine; D011353:Prodigiosin