Premium
Evolution of a novel lysine decarboxylase in siderophore biosynthesis
Author(s) -
Burrell Matthew,
Hanfrey Colin C.,
Kinch Lisa N.,
Elliott Katherine A.,
Michael Anthony J.
Publication year - 2012
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2012.08208.x
Subject(s) - cadaverine , siderophore , biology , lysine decarboxylase , streptomyces coelicolor , biochemistry , biosynthesis , gene cluster , putrescine , gene , enzyme , mutant
Summary Structural backbones of iron‐scavenging siderophore molecules include polyamines 1,3‐diaminopropane and 1,5‐diaminopentane (cadaverine). For the cadaverine‐based desferroxiamine E siderophore in S treptomyces coelicolor , the corresponding biosynthetic gene cluster contains an ORF encoded by desA that was suspected of producing the cadaverine (decarboxylated lysine) backbone. However, desA encodes an l ‐2,4‐diaminobutyrate decarboxylase ( DABA DC ) homologue and not any known form of lysine decarboxylase ( LDC ). The only known function of DABA DC is, together with l ‐2,4‐aminobutyrate aminotransferase ( DABA AT ), to synthesize 1,3‐diaminopropane. We show here that S . coelicolor desA encodes a novel LDC and we hypothesized that DABA DC homologues present in siderophore biosynthetic clusters in the absence of DABA AT ORFs would be novel LDCs . We confirmed this by correctly predicting the LDC activity of a DABA DC homologue from a Y ersinia pestis siderophore biosynthetic pathway. The corollary was confirmed for a DABA DC homologue, adjacent to a DABA AT ORF in a siderophore pathway in the cyanobacterium A nabaena variabilis , which was shown to be a bona fide DABA DC . These findings enable prediction of whether a siderophore pathway will utilize 1,3‐diaminopropane or cadaverine, and suggest that the majority of bacteria use DABA AT and DABA DC for siderophore, rather than norspermidine/polyamine biosynthesis.