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Novel inositol catabolic pathway in T hermotoga maritima

Irina A. Rodionova; Semen A. Leyn; Michael D. Burkart; Nathalie Boucher; Kenneth M. Noll; Andrei L. Osterman; Dmitry A. Rodionov
Environmental Microbiology · Vol. 15, Issue 8 · pp. 2254-2266 · 2013

Abstract

Summary myo ‐ inositol ( MI ) is a key sugar alcohol component of various metabolites, e.g. phosphatidylinositol‐based phospholipids that are abundant in animal and plant cells. The seven‐step pathway of MI degradation was previously characterized in various soil bacteria including B acillus subtilis . Through a combination of bioinformatics and experimental techniques we identified a novel variant of the MI catabolic pathway in the marine hyperthermophilic bacterium T hermotoga maritima . By using in vitro biochemical assays with purified recombinant proteins we characterized four inositol catabolic enzymes encoded in the TM 0412– TM 0416 chromosomal gene cluster. The novel catabolic pathway in T . maritima starts as the conventional route using the myo ‐inositol dehydrogenase IolG followed by three novel reactions. The first 2‐keto‐ myo ‐inositol intermediate is oxidized by another, previously unknown NAD ‐dependent dehydrogenase TM 0412 (named IolM ), and a yet unidentified product of this reaction is further hydrolysed by TM 0413 ( IolN ) to form 5‐keto‐ l ‐gluconate. The fourth step involves epimerization of 5‐keto‐ l ‐gluconate to d ‐tagaturonate by TM 0416 ( IolO ). T. maritima is unable to grow on myo ‐inositol as a single carbon source. The determined in vitro specificity of the InoEFGK ( TM 0418– TM 0421) transporter to myo ‐inositol‐phosphate suggests that the novel pathway in T hermotoga utilizes a phosphorylated derivative of inositol.

Bibliographic Information

JournalEnvironmental Microbiology
PublisherWiley
Publication Date2013-08-01
Publication Year2013
Volume15
Issue8
Pages2254-2266
Document TypeJournal Article
Print ISSN1462-2912
eISSN1462-2920
DOI10.1111/1462-2920.12096
SubjectMicrobial Ecology

Access Information

NARA Access Coverage1999-01-01~Current
Journal Homepagehttps://onlinelibrary.wiley.com/loi/14622920
Publisher PageOpen Publisher Page
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