Purification and Properties of a Novel Enzyme, Maltooligosyl Trehalose Synthase, from<i>Arthrobacter</i>sp. Q36

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

doi:10.1271/bbb.59.2210

Cited by 94 publications

(71 citation statements)

References 5 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1c). It was shown (Nishimoto et al, 1996;Nakada et al, 1995) that, although close in their intramolecular transglycosylation activity, TreY and TreS cannot substitute for each other in vivo because of the differences in their substrate specificities.…”

Section: Introductionmentioning

confidence: 99%

Genetic dissection of trehalose biosynthesis in Corynebacterium glutamicum: inactivation of trehalose production leads to impaired growth and an altered cell wall lipid composition

et al. 2003

View full text Add to dashboard Cite

The analysis of the available Corynebacterium genome sequence data led to the proposal of the presence of all three known pathways for trehalose biosynthesis in bacteria, i.e. trehalose synthesis from UDP-glucose and glucose 6-phosphate (OtsA-OtsB pathway), from malto-oligosaccharides or α-1,4-glucans (TreY-TreZ pathway), or from maltose (TreS pathway). Inactivation of only one of the three pathways by chromosomal deletion did not have a severe impact on C. glutamicum growth, while the simultaneous inactivation of the OtsA-OtsB and TreY-TreZ pathway or of all three pathways resulted in the inability of the corresponding mutants to synthesize trehalose and to grow efficiently on various sugar substrates in minimal media. This growth defect was largely reversed by the addition of trehalose to the culture broth. In addition, a possible pathway for glycogen synthesis from ADP-glucose involving glycogen synthase (GlgA) was discovered. C. glutamicum was found to accumulate significant amounts of glycogen when grown under conditions of sugar excess. Insertional inactivation of the chromosomal glgA gene led to the failure of C. glutamicum cells to accumulate glycogen and to the abolition of trehalose production in a ΔotsAB background, demonstrating that trehalose production via the TreY-TreZ pathway is dependent on a functional glycogen biosynthetic route. The trehalose-non-producing mutant with inactivated OtsA-OtsB and TreY-TreZ pathways displayed an altered cell wall lipid composition when grown in minimal broth in the absence of trehalose. Under these conditions, the mutant lacked both major trehalose-containing glycolipids, i.e. trehalose monocorynomycolate and trehalose dicorynomycolate, in its cell wall lipid fraction. The results suggest that a dramatically altered cell wall lipid bilayer of trehalose-less C. glutamicum mutants may be responsible for the observed growth deficiency of such strains in minimal medium. The results of the genetic and physiological dissection of trehalose biosynthesis in C. glutamicum reported here may be of general relevance for the whole phylogenetic group of mycolic-acid-containing coryneform bacteria.

show abstract

Section: Introductionmentioning

confidence: 99%

Genetic dissection of trehalose biosynthesis in Corynebacterium glutamicum: inactivation of trehalose production leads to impaired growth and an altered cell wall lipid composition

et al. 2003

View full text Add to dashboard Cite

show abstract

“…Five different pathways for the synthesis of trehalose have been examined (2,27), the most common of which involves a trehalose-6-phosphate synthase (Tps) that converts nucleoside diphosphate (NDP)-glucose and glucose-6-phosphate (Glc6P) into trehalose-6-phosphate (T6P) that is then dephosphorylated to trehalose by a trehalose-6-phosphate phosphatase (Tpp) (34). Other pathways for trehalose biosynthesis involve trehalose synthase (TreS) and the maltooligosyltrehalose synthase/hydrolase (TreY/TreZ) system, which catalyze the conversion of maltose and maltooligosaccharides into trehalose, respectively (24). Additionally, the TreS from Mycobacterium smegmatis can also convert glycogen into trehalose via maltose (26).…”

mentioning

confidence: 99%

A Unique Combination of Genetic Systems for the Synthesis of Trehalose in Rubrobacter xylanophilus : Properties of a Rare Actinobacterial TreT

et al. 2008

View full text Add to dashboard Cite

Trehalose is the primary organic solute inRubrobacter xylanophilus under all conditions tested, including those for optimal growth. We detected genes of four different pathways for trehalose synthesis in the genome of this organism, namely, the trehalose-6-phosphate synthase (Tps)/trehalose-6-phosphate phosphatase (Tpp), TreS, TreY/TreZ, and TreT pathways. Moreover, R. xylanophilus is the only known member of the phylum Actinobacteria to harbor TreT. The Tps sequence is typically bacterial, but the Tpp sequence is closely related to eukaryotic counterparts. Both the Tps/Tpp and the TreT pathways were active in vivo, while the TreS and the TreY/TreZ pathways were not active under the growth conditions tested and appear not to contribute to the levels of trehalose observed. The genes from the active pathways were functionally expressed in Escherichia coli, and Tps was found to be highly specific for GDP-glucose, a rare feature among these enzymes. The trehalose-6-phosphate formed was specifically dephosphorylated to trehalose by Tpp. The recombinant TreT synthesized trehalose from different nucleoside diphosphate-glucose donors and glucose, but the activity in R. xylanophilus cell extracts was specific for ADP-glucose. The TreT could also catalyze trehalose hydrolysis in the presence of ADP, but with a very high K m . Here, we functionally characterize two systems for the synthesis of trehalose in R. xylanophilus, a representative of an ancient lineage of the actinobacteria, and discuss a possible scenario for the exceptional occurrence of treT in this extremophilic bacterium.

show abstract

“…DEAE-Toyopearl 650S and Toyopearl HW-55S were purchased from Tosoh Co., Ltd. Glucosyl trehalose, maltosyl trehalose, maltotriosyl trehalose, maltotetraosyl trehalose, and maltopentaosyl trehalose were prepared in our laboratory using MTSase according to the method described in our accompanying paper. 10) Maltopentaose was prepared in our laboratory. The other sugars and polysaccharides were purchased from commercial sources.…”

Section: Methodsmentioning

confidence: 99%

“…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%

See 1 more Smart Citation

Purification and Characterization of a Novel Enzyme, Maltooligosyl Trehalose Trehalohydrolase, fromArthrobactersp. Q36

Nakada¹,

Maruta²,

Mitsuzumi³

et al. 1995

Bioscience, Biotechnology, and Biochemistry

Self Cite

View full text Add to dashboard Cite

Purification and Properties of a Novel Enzyme, Maltooligosyl Trehalose Synthase, fromArthrobactersp. Q36

Cited by 94 publications

References 5 publications

Genetic dissection of trehalose biosynthesis in Corynebacterium glutamicum: inactivation of trehalose production leads to impaired growth and an altered cell wall lipid composition

Genetic dissection of trehalose biosynthesis in Corynebacterium glutamicum: inactivation of trehalose production leads to impaired growth and an altered cell wall lipid composition

A Unique Combination of Genetic Systems for the Synthesis of Trehalose in Rubrobacter xylanophilus : Properties of a Rare Actinobacterial TreT

Purification and Characterization of a Novel Enzyme, Maltooligosyl Trehalose Trehalohydrolase, fromArthrobactersp. Q36

Contact Info

Product

Resources

About