Enzymatic Synthesis of Acarviosyl-maltooligosaccharides Using Disproportionating Enzyme 1

Tagami, Takayoshi; Tanaka, Yoshiyuki; Mori, Haruhide; Okuyama, Masayuki; Kimura, Atsuo

doi:10.1271/bbb.120732

Cited by 11 publications

(5 citation statements)

References 34 publications

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“…Mori et al. observed that isomerization ( cis / trans =1 : 2) of the double bond occurs in the alkynylation of acetylene to cis allyl bromide, [7] whereas our reaction proceeded without isomerization. Enyne 2Na was obtained from olefin 1N .…”

Section: Resultscontrasting

confidence: 50%

Regioselective Alkynylation of Allylic Phosphates with Alkynyl Copper Reagents

Mamada

Ogawa

2023

Eur J Org Chem

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We developed an alkynylation of allylic phosphates with acetylenes in the presence of copper and magnesium salts. The reaction proceeded regioselectively to afford the corresponding 1,4‐enynes. Furthermore, the functional group tolerance of this reaction was established. As an application, the 1,4‐enyne intermediate involved in the synthesis of 13R,19S,20S‐trihydroxydocosapentaenoic acid could be efficiently synthesized.

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Section: Resultscontrasting

confidence: 50%

Regioselective Alkynylation of Allylic Phosphates with Alkynyl Copper Reagents

Mamada

Ogawa

2023

Eur J Org Chem

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“…Plant disproportionating enzymes have also been used to transfer glucans from cheap donor molecules onto acceptor molecules ( e.g. to generate fluorinated oligosaccharides ( 18 ) and to generate novel acarviostatin-like molecules ( 19 )). Amylomaltase can also be used to modify starches in order to make thermoreversible gels ( 20 ) and alternatives to gelatin and to replace fats in yogurt ( 21 ).…”

Section: Introductionmentioning

confidence: 99%

Structural Dissection of the Maltodextrin Disproportionation Cycle of the Arabidopsis Plastidial Disproportionating Enzyme 1 (DPE1)

O’Neill

Stevenson

Tantanarat

et al. 2015

Journal of Biological Chemistry

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Background: Arabidopsis maltodextrin disproportionating enzyme 1 (AtDPE1) plays a key role in chloroplast starch degradation.Results: Six AtDPE1 structures define the active site and reveal mechanistically relevant conformations of both the enzyme and substrate.Conclusion: Substrates are captured through loop rearrangements; the subtle deployment of active site residues controls catalysis.Significance: A molecular level understanding of the complete disproportionation cycle of AtDPE1 is presented.

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“…It was proposed that DPE1 plays an important role in the conversion of transitory starch into sucrose in leaves at night [15,16]. In vitro DPE1 from adzuki bean cotyledons can catalyze intermolecular transglycosylation to produce acarviosyl-maltooligosaccharides from acarbose [17] and purified DPE1 from Arabidopsis leaf has been used to produce maltodextrin from maltotriose [6].…”

mentioning

confidence: 99%

Expression and characterization of 4-α-glucanotransferase genes from Manihot esculenta Crantz and Arabidopsis thaliana and their use for the production of cycloamyloses

Tantanarat

O’Neill

Rejzek

et al. 2014

Process Biochemistry

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4-α-Glucanotransferase or disproportionating enzyme (D-enzyme, DPE) catalyzes the α-1,4 glycosyl transfer between oligosaccharides. Type I D-enzyme (DPE1) can transfer maltosyl unit from one 1,4-α-D-glucan to an acceptor mono-or oligo-saccharide, which reflects the physiological role of DPE1 in plant starch metabolism. In this study, the genes encoding DPE1 from Arabidopsis thaliana (AtDPE1) and Manihot esculenta Crantz cultivar KU50 (MeDPE1) were cloned and expressed in Escherichia coli and purified to homogeneity. MeDPE1 encoded 585 amino acid residues, including a 56 residue signal peptide, while AtDPE1 encoded 576 amino acid residues with a 45 residue signal peptide. The molecular mass of both mature enzymes, estimated from deduced amino acid sequence, were the same at 59.4 kDa, with a pI of 5.13. The predicted structures of both enzymes showed the conserved 250's loop and three catalytic amino acid residues, characteristics of disproportionating enzymes in the GH77 glycoside hydrolase family. Biochemical characterization showed that both purified recombinant enzymes were homodimers in solution, with similar optimum pH and temperature for disproportionating activity at pH 6-8 and 37 °C. Using potato amylose as a substrate, AtDPE1 can produce cycloamyloses in the range 16-50 glucose residues, while products from the action of MeDPE1 on the same substrate were in a wider range of 16 to DP>60. These recombinant enzymes are useful tools for elucidation of their functional roles in starch metabolism and for applications in the starch industry.

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Enzymatic Synthesis of Acarviosyl-maltooligosaccharides Using Disproportionating Enzyme 1

Cited by 11 publications

References 34 publications

Regioselective Alkynylation of Allylic Phosphates with Alkynyl Copper Reagents

Regioselective Alkynylation of Allylic Phosphates with Alkynyl Copper Reagents

Structural Dissection of the Maltodextrin Disproportionation Cycle of the Arabidopsis Plastidial Disproportionating Enzyme 1 (DPE1)

Expression and characterization of 4-α-glucanotransferase genes from Manihot esculenta Crantz and Arabidopsis thaliana and their use for the production of cycloamyloses

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