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

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

doi:10.1271/bbb.59.2215

Cited by 61 publications

(26 citation statements)

References 3 publications

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“…Although the synthesis utilizes a mixture of several enzymes, the two main enzymes that directly produce trehalose from starch are maltooligosyl-trehalose synthase (MTSase) and maltooligosyl-trehalose trehalohydrolase (MTHase). [140][141][142] These two enzymes were derived from a nonpathogenic soil microbe designated as Arthrobacter ramosus. 31,143 The key function of MTSase is to recognize the reducing end of the terminal D-glucose units of amylose molecules [141][142] and to convert the "-1,4-to "-1,1-glycosidic bond in an intramolecular transglycosylation reaction, creating an amylose molecule with a terminal trehalose unit.…”

Section: Methods Of Productionmentioning

confidence: 99%

Trehalose: Current Use and Future Applications

Ohtake

Wang²

2011

Journal of Pharmaceutical Sciences

402

261

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Section: Methods Of Productionmentioning

confidence: 99%

Trehalose: Current Use and Future Applications

Ohtake

Wang²

2011

Journal of Pharmaceutical Sciences

402

261

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“…However, enzymes that are able to generate a-1,1-linked glucosyl moieties by intramolecular glucosyl transfer, using a-1,4-glucans, malto-oligosaccharides or, in some cases, maltose itself as the substrate, have now been described in the archaebacteria Sulfolobus spp. (Lama et al 1990(Lama et al , 1991Kato et al 1996;Maruta et al 1996c;Nakada et al 1996aNakada et al , 1996bKobayashi et al 1996); in Thermus aquaticus (Nishimoto et al 1996a) and the actinomycetes Arthrobacter (Maruta et al 1995(Maruta et al , 1996aNakada et al 1995aNakada et al , 1995b and Pimelobacter (Nishimoto et al 1995; and in gram-negative organisms (Rhizobium spp.) (Maruta et al 1996b;Streeter and Bhagwat 1999).…”

Section: Duplicated Operons For Storage Carbohydrate Metabolismmentioning

confidence: 99%

Duplicated gene clusters suggest an interplay of glycogen and trehalose metabolism during sequential stages of aerial mycelium development in Streptomyces coelicolor A3(2)

Schneider¹,

Bruton²,

Chater³

2000

Mol Gen Genet

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DNA sequencing and operon disruption experiments indicate that the genes glgBI and glgBII, which code for the two developmentally specific glycogen branching enzymes of Streptomyces coelicolor A3(2) each form part of larger duplicated operons consisting of at least four genes in the order pep1-treS-pep2-glgB. The sequences of the TreS proteins are 73% identical (93% similar) to that of an enzyme that converts maltose into trehalose in Pinmelobacter, a distantly related actinomycete; and the Pep1 proteins show relatedness to the alpha-amylase superfamily. Disruptions of each operon have spatially specific effects on the nature of glycogen deposits, as assessed by electron microscopy. Upstream of the glgBI operon, and diverging from it, is a gene (glgP) that encodes a protein resembling glycogen phosphorylase from Thermatoga maritima and a homologue in Mycobacterium tuberculosis. These three proteins form a distinctive subgroup compared with glycogen phosphorylases from most other bacteria, which more closely resemble the enzymes from eukaryotes. Diverging from the glgBII operon, and separated from the pep1 gene by two very small ORFs, is a gene (glgX) encoding a probable glycogen debranching enzyme. It is suggested that most of these gene products participate in the developmentally modulated interconversion of immobile, inert glycogen reservoirs, and diffusible forms of carbon, both metabolically active (e.g. glucose-1-phosphate generated by glycogen phosphorylase) and metabolically inert but physiologically significant (trehalose).

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“…No enzyme that shows such a substrate specificity is known, except for maltooligosyl trehalose trehalohydrolase (EC 3.2.1.141). 26) Maltoheptaose, amylose and maltopentaosyl trehalose were completely hydrolyzed among the tested substrates. Table 4 shows the molar ratios of the oligosaccharides generated by the hydrolysis reaction.…”

Section: Orf-3mentioning

confidence: 92%

A Novel Glucanotransferase that Produces a Cyclomaltopentaose Cyclized by an .ALPHA.-1,6-Linkage

Watanabe¹,

Nishimoto²,

Chaen³

et al. 2007

J. Appl. Glycosci.

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Enzymatic syntheses of various nonreducing oligosaccharides from starch have been reported by many researchers. Nonreducing oligosaccharides are generally divided into two groups: linear and cyclic oligosaccharides. Trehalose (α D glucopyranosyl α D glucopyranoside) is a typical linear nonreducing oligosaccharide occurring in bacteria, yeasts, fungi, plants, and invertebrates. Mass production of trehalose from starch has been developed using two bacterial enzymes, maltooligosyltrehalose synthase (EC 5.4.99.15) and maltooligosyltrehalose trehalohydrolase (EC 3.2.1.141), 1 3) and now this saccharide is used in the fields of food, cosmetics, and pharmaceuticals. Cyclomaltohexaose (α cyclodextrin), one of the most well known cyclic oligosaccharides, is produced from linear α 1,4 glucans by the intramolecular α 1,4 transglycosylation reaction of a cyclomaltodextrin glucanotransferase (CGTase; EC 2.4.1.19).4) The cyclic oligosaccharide has a hydrophobic cavity in the center of the structure. Guest molecules of suitable size can enter the cavity, and the formation of the inclusion complex is used for stabilizing labile materials, 5) masking odors 6) and modifying viscosity. 7) Co te and co workers first reported that a cyclic tetrasaccharide consisting ofproduced from a dextran like polysaccharide, alternan, by its degrading enzyme.8 10) The cyclic oligosaccharide was designated cycloalternan (CA). Recently, we discovered two novel enzymes, 6 α glucosyltransferase and 3 α isomaltosyltransferase, in Bacillus globisporus, and succeeded in the mass production of this saccharide from starch by the joint reaction of the two enzymes.11 13) More recently, we found a new enzymatic system for synthesizing a cyclic maltosyl (1 6) 14,15) We consequently obtained two kinds of cyclic tetrasaccharides by discovering CMM. To distinguish the two kinds of cyclic tetrasaccharides, in this review we designate the cyclic nigerosyl (1 6 The amino-acid sequence deduced from igtZ exhibited no similarity to any proteins with known or unknown functions. IgtZ was expressed in Escherichia coli, and the enzyme (IgtZ) was purified. The enzyme acted on maltooligosaccharides that have a DP of 4 or more, amylose, and soluble starch to produce glucose and maltooligosaccharides up to DP5 by a hydrolysis reaction. The enzyme, which has a novel amino-acid sequence, should be assigned to α-amylase. It is notable that both IGTase and IgtZ have a tandem sequence similar to a carbohydrate-binding module belonging to family 25. These two enzymes jointly acted on raw starch, and efficiently generated ICG5.

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

Cited by 61 publications

References 3 publications

Trehalose: Current Use and Future Applications

Trehalose: Current Use and Future Applications

Duplicated gene clusters suggest an interplay of glycogen and trehalose metabolism during sequential stages of aerial mycelium development in Streptomyces coelicolor A3(2)

A Novel Glucanotransferase that Produces a Cyclomaltopentaose Cyclized by an .ALPHA.-1,6-Linkage

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