Formation of Trehalose from Maltooligosaccharides by a Novel Enzymatic System

Maruta, Kazuhiko; Nakada, Tetsuya; Kubota, Michio; Chaen, Hiroto; Sugimoto, Toshiyuki; Kurimoto, Masashi; Tsujisaka, Yoshio

doi:10.1271/bbb.59.1829

Cited by 126 publications

(78 citation statements)

References 7 publications

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“…The activities of the TreY-TreZ pathway were investigated as described by Maruta et al (1995). Trehalose phosphorylase was examined as described by Maréchal & Belocopitow (1972).…”

Section: Methodsmentioning

confidence: 99%

Biochemical and genetic characterization of the pathways for trehalose metabolism in Propionibacterium freudenreichii, and their role in stress response

2007

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Propionibacterium freudenreichii accumulates high levels of trehalose, especially in response to stress. The pathways for trehalose metabolism were characterized, and their roles in response to osmotic, oxidative and acid stress were studied. Two pathways were identified: the trehalose-6-phosphate synthase/phosphatase (OtsA-OtsB) pathway, and the trehalose synthase (TreS) pathway. The former was used for trehalose synthesis, whereas the latter is proposed to operate in trehalose degradation. The activities of OtsA, OtsB and TreS were detected in cell extracts; the corresponding genes were identified, and the recombinant proteins were characterized in detail. In crude extracts of P. freudenreichii, OtsA was specific for ADP-glucose, in contrast to the pure recombinant OtsA, which used UDP-, GDP-and TDP-glucose, in addition to ADP-glucose. Moreover, the substrate specificity of OtsA in cell extracts was lost during purification, and the recombinant OtsA became specific to ADP-glucose upon incubation with a dialysed cell extract. The level of OtsA was enhanced (approximately twofold) by osmotic, oxidative and acid stress, whereas the level of TreS remained constant, or it decreased, under identical stress conditions. Therefore, the OtsA-OtsB pathway plays an important role in the synthesis of trehalose in response to stress. It is most likely that trehalose degradation proceeds via TreS to yield maltose, which is subsequently catabolized via amylomaltase activity. Hydrolytic activities that are potentially involved in trehalose degradation (trehalase, trehalose phosphorylase, trehalose-6-phosphate phosphorylase and trehalose-6-phosphate hydrolase) were not present. The role of trehalose as a common response to three distinct stresses is discussed.

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“…The activities of the TreY-TreZ pathway were investigated as described by Maruta et al (1995). Trehalose phosphorylase was examined as described by Maréchal & Belocopitow (1972).…”

Section: Methodsmentioning

confidence: 99%

Biochemical and genetic characterization of the pathways for trehalose metabolism in Propionibacterium freudenreichii, and their role in stress response

2007

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Section: Trey-trez Pathwaymentioning

confidence: 99%

“…(Maruta et al, 1995) and it is also a two-step pathway, in which maltodextrines are converted to trehalose. In the first step, maltooligosyltrehalose synthase (TreY) catalyzes the convertion of maltopentaose into maltooligosyl trehalose by intramolecular transglycosylation, and in the second step, maltooligosyltrehalose trehalohydrolase (TreZ) hydrolizes the maltooligosyl trehalose, releasing free trehalose (Maruta et al, 1995). This pathway is also found in other bacterial species such as Rhizobium (Maruta et al, 1996a), Bradyrhizobium japonicum (Sugawara et al, 2010) and Corynebacterium (Tzvetkov et al, 2003), but is missing in other major bacterial groups including E. coli and Bacillus subtilis.…”

Section: Trey-trez Pathwaymentioning

confidence: 99%

Trehalose and Abiotic Stress in Biological Systems

Iordăchescu¹,

Imai²

2011

Abiotic Stress in Plants - Mechanisms and Adaptations

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“…trehalose +maltooligosaccharide (2) MTHase These enzymes are especially useful for industrial production of trehalose because of the efficient conversion of ry,,-1,4 glucans into trehalose by simultaneous reactions. 9 ) In the accompanying paper, 10) we reported the purification and characterization of MTSase catalyzing the first reaction described above. In this paper, we describe the purification and some properties of MTHase, which catalyzes the second reaction.…”

Section: Mtsasementioning

confidence: 99%