Purification and Substrate Specificity of Brewer’s Yeast α-Glucosidase

Matsusaka, Kouetsu; Chiba, Seiya; Shimomura, Tokuji

doi:10.1080/00021369.1977.10862786

Cited by 14 publications

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“…The substrate specificity of a-glucosidase is known to differ greatly with the enzyme sources. 2) There have been few reports on a-glucosidases with such a substrate specificity, except for brewer's yeast 3 ) and Bacillus species 4 ,5) enzymes. The kinetic properties of honeybee a-glucosidase I has been studied in detail, and the enzyme was found to attack some substrates in unusual reactivity, which were different from Michaelis-Menten type kinetics.…”

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Substrate Specificity and Subsite Affinities of Honeybeeα-Glucosidase II

Takewaki

Kimura

Kubota

et al. 1993

Bioscience, Biotechnology, and Biochemistry

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The substrate specificity of honeybee IX-glucosidase II, a monomeric protein, was investigated in detail. The enzyme hydrolyzed phenyl IX-glucoside and p-nitrophenyl IX-glucoside more rapidly than maltooligosaccharides. Unusual kinetics were observed in hydrolysis of sucrose,. turanose, kojibiose, and soluble starch. The s versus v plots showed sigmoidal curves, and so the Lineweaver-Burk plots became concave, indicating positive kinetic cooperativity. The Hill coefficients for sucrose, turanose, kojibiose, and soluble starch were calculated to be 1.46, 1.34, 1.15, and 1.28, respectively. The Km values for these substrates were calculated as the concentration at one half of the maximum velocity. The ratios of the maximum velocities for maltose, malto-triose, -tetraose, -pentaose, -hexaose, -heptaose, maltodextrin (DP = 13), kojibiose, nigerose, isomaltose, sucrose, turanose, phenyl (X-glucoside, p-nitrophenyl a-glucoside, phenyl IX-maltoside, and soluble starch were estimated to be 100 substrates, 5.4, 4.0, 6.3, 11, 31, 50, 50, 7.6, 20, 5.6, 6.7, 7.7, 1.6, 1.8, 2.0, and 9.4mM, respectively. The enzyme was also active on (X-glucose-1-phosphate. Its maximum activity was 79.9% of that to maltose and the Km was 50mM. The substrate specificity of this enzyme was different from that of honeybee IX-glucosidase I. The two enzymes were found to be immunologically distinct proteins. Based on the rate parameters for maltooligosaccharides, the subsite affinities (A/s) in the active site of the enzyme were evaluated. Subsites 1, 2, and 3 having the positive Ai value (AH A 2 , and A3: 0.672, 4.61, and 0.483kcal/mol, respectively) were considered to be effective for binding of substrate to the active site.

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confidence: 99%

Substrate Specificity and Subsite Affinities of Honeybeeα-Glucosidase II

Takewaki

Kimura

Kubota

et al. 1993

Bioscience, Biotechnology, and Biochemistry

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“…Chiba 4 ) proposed to classify e<:-glucosidasc into the following three groups: (I) enzymes that hydrolyze heterogeneous substrates such as synthetic a-glucosides and sucrose 5 ); (II) enzymes that hydrolyze homogeneous malto-oligosaccharides preferentially but not synthetic ::x-glucosides or sucrose 6 9); and (III) enzymes that hydrolyze not only homogeneous malto-oligosaccharides but also ::x-glucans. [10][11][12][13][14][15][16][17][18] It has been reported that multiple molecular forms of ::x-glucosidase which have different substrate specificity were observed in geen gram, 19) sugar beet seed, 20) rice seeds, 21) banana pulp tissues,22) honey bee,7) and pig duodenum.…”

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Multiple Molecular Forms ofα-Glucosidase from Spinach Seeds,Spinacia oleraceaL.

Sugimoto

Furui

Suzuki

1995

Bioscience, Biotechnology, and Biochemistry

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“…Recently, Yu et al (33) found that fungus A. niger was able to use AF as the sole carbon source for growth, whereas Bakers' yeast could not grow in the presence of 0.47 M AF in medium. This observation is of interest because A. niger secretes large amounts of 31AG into medium (9), but ␣-glucosidase (13AG) of yeast stays inside of cells (34,35). In nature, microorganisms receive glucose from AF by secreting ␣-glucosidase, implying the presence of a salvage pathway of unutilized AF.…”

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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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Purification and Substrate Specificity of Brewer’s Yeast α-Glucosidase

Cited by 14 publications

References 0 publications

Substrate Specificity and Subsite Affinities of Honeybeeα-Glucosidase II

Substrate Specificity and Subsite Affinities of Honeybeeα-Glucosidase II

Multiple Molecular Forms ofα-Glucosidase from Spinach Seeds,Spinacia oleraceaL.

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

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