Structural elements in dextran glucosidase responsible for high specificity to long chain substrate

Saburi, Wataru; Mori, Haruhide; Saito, Saori; Okuyama, Masayuki; Kimura, Atsuo

doi:10.1016/j.bbapap.2006.01.012

Cited by 54 publications

(69 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…1D). DG can act on AF but not a soluble starch, whereas the other ␣-glucosidases used will be able to release glucose from soluble starch (3,4). Therefore, the formation of glucose will provide the evidence that the GL released AF from soluble starch.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

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

Self Cite

View full text Add to dashboard Cite

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.

show abstract

Section: Resultsmentioning

confidence: 99%

“…GH 13 ␣-glucosidases (13AGs) (1,(3)(4)(5)(6)(7) have four conserved regions of ␣-amylase family enzymes (8). Their three-dimensional structures have been resolved (3,5).…”

mentioning

confidence: 99%

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

Self Cite

View full text Add to dashboard Cite

show abstract

“…In the standard enzyme assay, the activity toward 2 mM p-nitrophenyl ␣-d-glucopyranoside (pNPG, Nacalai Tesque, Kyoto, Japan) was measured as described previously (1). Thermal and pH stabilities and optimum pH were evaluated according to our previous study (1).…”

Section: Enzyme Assaymentioning

confidence: 99%

“…Thermal and pH stabilities and optimum pH were evaluated according to our previous study (1). Steady state kinetic parameters for pNPG, phenyl ␣-glucopyranoside (PG) (synthesized by Trevelyan's method (20)), and p-nitrophenyl ␣-isomaltoside (pNPIG2) (prepared by our previous method (1)) were determined according to the procedures described previously (21).…”

Section: Enzyme Assaymentioning

confidence: 99%

“…Amplified PCR fragments were cloned into pET-23d (Novagen, Darmstadt, Germany) as described previously (1). The resulting expression plasmids were introduced into Escherichia coli BL21 (DE3) CodonPlus RIL (Stratagene; La Jolla, CA), and the mutant enzymes were prepared as reported else- where (1). Induction of protein production was carried out at 15°C for 18 h to improve the production level of the recombinant protein.…”

Section: Preparation Of C129s/c532s (2cs) D194a/c129s/c532s (D194c-2mentioning

confidence: 99%

See 1 more Smart Citation

Replacement of the Catalytic Nucleophile Aspartyl Residue of Dextran Glucosidase by Cysteine Sulfinate Enhances Transglycosylation Activity

Saburi

Kobayashi

Mori

et al. 2013

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Dextran glucosidase from Streptococcus mutans (SmDG) catalyzes the hydrolysis of an α-1,6-glucosidic linkage at the nonreducing end of isomaltooligosaccharides and dextran. This enzyme has an Asp-194 catalytic nucleophile and two catalytically unrelated Cys residues, Cys-129 and Cys-532. Cys-free SmDG was constructed by replacement with Ser (C129S/C532S (2CS), the activity of which was the same as that of the wild type, SmDG). The nucleophile mutant of 2CS was generated by substitution of Asp-194 with Cys (D194C-2CS). The hydrolytic activity of D194C-2CS was 8.1 × 10⁻⁴ % of 2CS. KI-associated oxidation of D194C-2CS increased the activity up to 0.27% of 2CS, which was 330 times higher than D194C-2CS. Peptide-mapping mass analysis of the oxidized D194C-2CS (Ox-D194C-2CS) revealed that Cys-194 was converted into cysteine sulfinate. Ox-D194C-2CS and 2CS shared the same properties (optimum pH, pI, and substrate specificity), whereas Ox-D194C-2CS had much higher transglucosylation activity than 2CS. This is the first study indicating that a more acidic nucleophile (-SOO−) enhances transglycosylation. The introduction of cysteine sulfinate as a catalytic nucleophile could be a novel approach to enhance transglycosylation

show abstract

Structure and function of α-glucan debranching enzymes

Møller

Henriksen

Svensson

2016

Cell. Mol. Life Sci.

View full text Add to dashboard Cite

α-Glucan debranching enzymes hydrolyse α-1,6-linkages in starch/glycogen, thereby, playing a central role in energy metabolism in all living organisms. They belong to glycoside hydrolase families GH13 and GH57 and several of these enzymes are industrially important. Nine GH13 subfamilies include α-glucan debranching enzymes; isoamylase and glycogen debranching enzymes (GH13_11); pullulanase type I/limit dextrinase (GH13_12-14); pullulan hydrolase (GH13_20); bifunctional glycogen debranching enzyme (GH13_25); oligo-1 and glucan-1,6-α-glucosidases (GH13_31); pullulanase type II (GH13_39); and α-amylase domains (GH13_41) in two-domain amylase-pullulanases. GH57 harbours type II pullulanases. Specificity differences, domain organisation, carbohydrate binding modules, sequence motifs, three-dimensional structures and specificity determinants are discussed. The phylogenetic analysis indicated that GH13_39 enzymes could represent a "missing link" between the strictly α-1,6-specific debranching enzymes and the enzymes with dual specificity and α-1,4-linkage preference.

show abstract

Structural elements in dextran glucosidase responsible for high specificity to long chain substrate

Cited by 54 publications

References 35 publications

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

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

Replacement of the Catalytic Nucleophile Aspartyl Residue of Dextran Glucosidase by Cysteine Sulfinate Enhances Transglycosylation Activity

Structure and function of α-glucan debranching enzymes

Contact Info

Product

Resources

About