Molecular Mechanism in<i>α</i>-Glucosidase and Glucoamylase

Chiba, Seiya

doi:10.1271/bbb.61.1233

Cited by 361 publications

(259 citation statements)

References 12 publications

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“…1,2) In the high concentrations of substrate, the enzyme also catalyzes the transferring reaction to form oligosaccharides. -Glucosidase is widely distributed in microorganisms, plants, mammals, and insects.…”

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Purification and Characterization of α-Glucosidase I from Japanese Honeybee (Apis cerana japonica) and Molecular Cloning of Its cDNA

Wongchawalit

Yamamoto

Nakai

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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α-Glucosidase (JHGase I) was purified from a Japanese subspecies of eastern honeybee (Apis cerana japonica) as an electrophoretically homogeneous protein. Enzyme activity of the crude extract was mainly separated into two fractions (component I and II) by salting-out chromatography. JHGase I was isolated from component I by further purification procedure using CM-Toyopearl 650M and Sephacryl S-100. JHGase I was a monomeric glycoprotein (containing 15% carbohydrate), of which the molecular weight was 82,000. Enzyme displayed the highest activity at pH 5.0, and was stable up to 40 °C and in a pH-range of 4.5–10.5. JHGase I showed unusual kinetic features: the negative cooperative behavior on the intrinsic reaction on cleavage of sucrose, maltose, and p-nitrophenyl α-glucoside, and the positive cooperative behavior on turanose. We isolated cDNA (1,930 bp) of JHGase I, of which the deduced amino-acid sequence (577 residues) confirmed that JHGase I was a member of α-amylase family enzymes. Western honeybees (Apis mellifera) had three α-glucosidase isoenzymes (WHGase I, II, and III), in which JHGase I was considered to correspond to WHGase I

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“…Type I -glucosidase is a member of GH 13, and type II and type III enzymes are members of GH 31. 2,4) We purified three -glucosidases from western honeybee (Apis mellifera L.), WHGase I, II, and III. 5,6) Three -glucosidases were different in molecular size, pH-stability, temperature-stability, substrate specificity, and localization in organ.…”

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confidence: 99%

Purification and Characterization of α-Glucosidase I from Japanese Honeybee (Apis cerana japonica) and Molecular Cloning of Its cDNA

Wongchawalit

Yamamoto

Nakai

et al. 2006

Bioscience, Biotechnology, and Biochemistry

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“…Starch is a storage glucan comprising -1,4-linked D-glucose main chains and maltooligosaccharides and starch producing glucose, i.e., the former enzyme produces 63 -glucose and the latter produces -glucose (Chiba, 1997). In mammals, dietary starch 64 is degraded to maltooligosaccharides and limited dextrin by salivary and pancreatic 65 -amylases.…”

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confidence: 99%

“…suggest that HdAgl possesses transglycosylation activity that is known as a 251 characteristic property for retaining enzymes (Chiba, 1997).…”

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Characterization of an α-glucosidase, HdAgl, from the digestive fluid of Haliotis discus hannai

Satoh

Inoue

Ojima

2013

Comparative Biochemistry and Physiology Part B: Biochemistry an

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25Previously, we isolated two -amylase isozymes, HdAmy58 and HdAmy82, from 26 the digestive fluid of the Pacific abalone Haliotis discus hannai (Kumagai et al, 2013, 27 Comp. Biochem. Physiol., B 164,[80][81][82][83][84][85][86][87][88]. These enzymes degraded starch producing 28 maltooligosaccharides but not glucose. However, the digestive fluid itself could produce 29 glucose from starch, indicating that the digestive fluid contains -glucosidase-like 30 enzymes together with the -amylases. Thus, in the present study, we isolated this 31 -glucosidase-like enzyme from the digestive fluid and characterized it to some extent. 32Isolation of this enzyme was carried out by ammonium sulfate fractionation followed by

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“…␣-Glucosidases are mainly classified in glycoside hydrolase family (GH) 3 13 or 31 (1,2). GH 13 ␣-glucosidases (13AGs) (1,(3)(4)(5)(6)(7) have four conserved regions of ␣-amylase family enzymes (8).…”

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A Novel Metabolic Pathway for Glucose Production Mediated by α-Glucosidase-catalyzed Conversion of 1,5-Anhydrofructose

Kim

Saburi

Yu³

et al. 2012

Journal of Biological Chemistry

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Background: ␣-Glucosidase-catalyzed hydration on 1,5-anhydrofructose has not been clarified. Results: ␣-Glucosidases of glycoside hydrolase families 13 and 31 synthesize ␣-configurated product from 1,5-anhydrofructose. Combined reaction of glucan lyase and ␣-glucosidase enhances glucose production from starch. Conclusion: ␣-Glucosidases catalyze trans-addition on 1,5-anhydrofructose. Significance: Novel ␣-glucosidase-associated metabolic pathway of glucose formation from 1,5-anhydrofructose suggests a salvage process of unutilized 1,5-anhydrofructose to glucose in nature.

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Molecular Mechanism inα-Glucosidase and Glucoamylase

Cited by 361 publications

References 12 publications

Purification and Characterization of α-Glucosidase I from Japanese Honeybee (Apis cerana japonica) and Molecular Cloning of Its cDNA

Purification and Characterization of α-Glucosidase I from Japanese Honeybee (Apis cerana japonica) and Molecular Cloning of Its cDNA

Characterization of an α-glucosidase, HdAgl, from the digestive fluid of Haliotis discus hannai

A Novel Metabolic Pathway for Glucose Production Mediated by α-Glucosidase-catalyzed Conversion of 1,5-Anhydrofructose

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