The Tetramer Structure of the Glycoside Hydrolase Family 27 α-Galactosidase I from<i>Umbelopsis vinacea</i>

Fujimoto, Zui; Kaneko, Satoshi; Kim, Wook-Dong; Park, Gwi-Gun; Momma, Mitsuru; Kobayashi, Hideyuki

doi:10.1271/bbb.90604

Cited by 14 publications

(14 citation statements)

References 23 publications

(27 reference statements)

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“…It was demonstrated that extracellular α-galactosidases produced by Thermomyces lanuginosus, Debaryomyces hansenii, and Pleorotus florida are monomeric proteins with 57, 60, and 99 kDa, respectively [25][26][27]. On the other hand, α-galactosidases produced by Penicillium sp., Umbelopsis vinacea and A. niger were described as tetrameric proteins, composed by four identical subunits with 82, 54, and 94 kDa, respectively [20,28,29]. The E1, E2, and E3 α-galactosidase forms achieved maximal substrate hydrolysis at temperatures of 60, 55 and 50°C, respectively (Fig.…”

Section: Resultsmentioning

confidence: 99%

Purification and Characterization of Aspergillus terreus α-Galactosidases and Their Use for Hydrolysis of Soymilk Oligosaccharides

Ferreira

Reis

Guimarães

et al. 2011

Appl Biochem Biotechnol

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α-Galactosidases has the potential to hydrolyze α-1-6 linkages in raffinose family oligosaccharides (RFO). Aspergillus terreus cells cultivated on wheat bran produced three extracellular forms of α-galactosidases (E1, E2, and E3). E1 and E2 α-galactosidases presented maximal activities at pH 5, while E3 α-galactosidase was more active at pH 5.5. The E1 and E2 enzymes showed stability for 6 h at pH 4-7. Maximal activities were determined at 60, 55, and 50 °C, for E1, E2, and E3 α-galactosidase, respectively. E2 α-galactosidase retained 90% of its initial activity after 70 h at 50 °C. The enzymes hydrolyzed ρNPGal, melibiose, raffinose and stachyose, and E1 and E2 enzymes were able to hydrolyze guar gum and locust bean gum substrates. E1 and E3 α-galactosidases were completely inhibited by Hg²⁺, Ag⁺, and Cu²⁺. The treatment of RFO present in soy milk with the enzymes showed that E1 α-galactosidase reduced the stachyose content to zero after 12 h of reaction, while E2 promoted total hydrolysis of raffinose. The complete removal of the oligosaccharides in soy milk could be reached by synergistic action of both enzymes.

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Section: Resultsmentioning

confidence: 99%

Purification and Characterization of Aspergillus terreus α-Galactosidases and Their Use for Hydrolysis of Soymilk Oligosaccharides

Ferreira

Reis

Guimarães

et al. 2011

Appl Biochem Biotechnol

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“…Available crystal structures from α-Gals of GH27 are monomers of 40-60 kDa (Hypocrea jecorina 18 and Oryza sativa 19 ), a human enzyme is a dimer 9 and two fungal enzymes are tetramers (Umbelopsis vinacea 20 and Saccharomyces cerevisiae 21 ). By contrast, α-Gals from GH36 of 85 kDa are predominantly tetramers in solution, 4,5,[22][23][24][25] although different oligomeric arrangements are reported for a few enzymes.…”

Section: Introductionmentioning

confidence: 99%

Crystal Structure of α-Galactosidase from Lactobacillus acidophilus NCFM: Insight into Tetramer Formation and Substrate Binding

Fredslund

Hachem

Larsen

et al. 2011

Journal of Molecular Biology

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“…The GH27 family has been extensively studied, and numerous ␣-galactosidase structures from different species (bacteria and eukaryotes) have been determined (7)(8)(9)(10)(11)(12)(13). These structures are composed of two domains: the catalytic domain with a conserved (␤/␣) 8 barrel topology and similar active sites and the C-terminal domain.…”

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confidence: 99%

The Molecular Mechanism of Thermostable α-Galactosidases AgaA and AgaB Explained by X-ray Crystallography and Mutational Studies

Merceron

Foucault

Haser

et al. 2012

Journal of Biological Chemistry

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Background:The thermostable ␣-galactosidases AgaA and AgaB are of industrial interest and have different catalytic properties despite having a high sequence identity. Results: The crystal structures helped to explain the specificities of these two isoenzymes. Conclusion: The A355E substitution modulates the induced fit mechanism. Significance: Transglycosylation is increased by a single substitution that is located away from the active site.

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The Tetramer Structure of the Glycoside Hydrolase Family 27 α-Galactosidase I fromUmbelopsis vinacea

Cited by 14 publications

References 23 publications

Purification and Characterization of Aspergillus terreus α-Galactosidases and Their Use for Hydrolysis of Soymilk Oligosaccharides

Purification and Characterization of Aspergillus terreus α-Galactosidases and Their Use for Hydrolysis of Soymilk Oligosaccharides

Crystal Structure of α-Galactosidase from Lactobacillus acidophilus NCFM: Insight into Tetramer Formation and Substrate Binding

The Molecular Mechanism of Thermostable α-Galactosidases AgaA and AgaB Explained by X-ray Crystallography and Mutational Studies

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