Evolution of a novel lysine decarboxylase in siderophore biosynthesis

Matthew Burrell, Colin C. Hanfrey, Lisa N. Kinch, Katherine A. Elliott, Anthony J. Michael

Research output: Contribution to journalArticle

20 Citations (Scopus)

Abstract

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 Streptomyces 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 Yersinia 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 Anabaena 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.

Original languageEnglish (US)
Pages (from-to)485-499
Number of pages15
JournalMolecular Microbiology
Volume86
Issue number2
DOIs
StatePublished - Oct 2012

Fingerprint

lysine decarboxylase
Siderophores
Carboxy-Lyases
Cadaverine
Open Reading Frames
Polyamines
Anabaena variabilis
4-Aminobutyrate Transaminase
Streptomyces coelicolor
Yersinia pestis
Biosynthetic Pathways
Cyanobacteria
Multigene Family
Lysine
Iron

ASJC Scopus subject areas

  • Molecular Biology
  • Microbiology

Cite this

Evolution of a novel lysine decarboxylase in siderophore biosynthesis. / Burrell, Matthew; Hanfrey, Colin C.; Kinch, Lisa N.; Elliott, Katherine A.; Michael, Anthony J.

In: Molecular Microbiology, Vol. 86, No. 2, 10.2012, p. 485-499.

Research output: Contribution to journalArticle

Burrell, Matthew ; Hanfrey, Colin C. ; Kinch, Lisa N. ; Elliott, Katherine A. ; Michael, Anthony J. / Evolution of a novel lysine decarboxylase in siderophore biosynthesis. In: Molecular Microbiology. 2012 ; Vol. 86, No. 2. pp. 485-499.
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