The role of two families of bacterial enzymes in putrescine synthesis from agmatine via agmatine deiminase Authors José M. Landete Mario E. Arena Isabel Pardo Maria C. Manca de Nadra Sergi Ferrer Keywords: agmatine, putrescine, agmatine deiminase, N-carbamoylputrescine amidohydrolase, putrescine carbamoyll-transferas Abstract Putrescine, one of the main biogenic amines associated to microbial food spoilage, can be formed by bacteriafrom arginine via ornithine decarboxylase (ODC), or from agmatine via agmatine deiminase (AgDI). This study aims to correlate putrescine production from agmatine to the pathway involving N-carbamoylputrescine formation via AdDI (the aguAproduct) and N-carbamoylputrescine amidohydrolase (the aguB product), or putrescine carbamoyltransferase (the ptcA product) in bacteria. PCR methods were developed to detect the two genes involved in putrescine production from agmatine.Putrescine production from agmatine could be linked to the aguA and ptcA genes in Lactobacillus hilgardii X1B,Enterococcus faecalis ATCC 11700, and Bacillus cereus ATCC 14579. By contrast Lactobacillus sakei 23K was unable toproduce putrescine, and although a fragment of DNA corresponding to the gene aguA was amplified, no amplification wasobserved for the ptcA gene. Pseudomonasaeruginosa PAO1 produces putrescine and is reported to harbour aguA and aguBgenes, responsible for agmatine deiminase and N-carbamoylputrescine amidohydrolase activities. The enzyme from P. aeruginosa PAO1 that converts N-carbamoylputrescine to putrescine (the aguB product) is different from other microorganismsstudied (the ptcA product). Therefore, the aguB gene from P. aeruginosa PAO1 could not be amplified with ptcA specificprimers. The aguB and ptcA genes have frequently been erroneously annotated in the past, as in fact these two enzymes areneither homologous nor analogous. Furthermore, the aguA, aguB and ptcA sequences available from GenBank were subjected to phylogenetic analysis, revealing that gram-positive bacteria harboured ptcA, whereas gram-negative bacteria harbouraguB. This paper also discusses the role of the agmatine deiminase system (AgDS) in acid stress resistance. Downloads PDF Published 2011-09-21 Issue Vol. 13 No. 4 (2010) Section Review Articles License Submission of a manuscript to International Microbiology implies: that the work described has not been published before, including publication in the World Wide Web (except in the form of an Abstract or as part of a published lecture, review, or thesis); that it is not under consideration for publication elsewhere; that all the coauthors have agreed to its publication. The corresponding author signs for and accepts responsability for releasing this material and will act on behalf of any and all coauthors regarding the editorial review and publication process.If an article is accepted for publication in International Microbiology, the authors (or other copyright holder) must transfer to the journal the right–not exclusive–to reproduce and distribute the article including reprints, translations, photographic reproductions, microform, electronic form (offline, online) or any other reproductions of similar nature. Nevertheless, all article in International Microbiology will be available on the Internet to any reader at no cost. The journal allows users to freely download, copy, print, distribute, search, and link to the full text of any article, provided the authorship and source of the published article is cited. The copyright owner's consent does not include copying for new works, or resale. In these cases, the specific written permission of International Microbiology must first be obtained.Authors are requested to create a link to the published article on the journal's website. The link must be accompanied by the following text: "The original publication is available on LINK at <http://www.im.microbios.org>. Please use the appropiate URL for the article in LINK. Articles disseminated via LINK are indexed, abstracted, and referenced by many abstracting and information services, bibliographic networks, subscription agencies, library networks, and consortia.