α-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. III. Substrate specificity, mode of action, and cleavage mechanism

Yu, Shukun; Ahmad, Tania; Kenne, Lennart; Pedersén, Marianne

doi:10.1016/0304-4165(94)00202-9

Cited by 59 publications

(42 citation statements)

References 12 publications

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“…third -1,4-glucanolytic system of starch and glycogen 101) has been found in fungi 102) and red algae, [103][104][105] and the lyase was first purified from red seaweed. Afterwards the enzymes have been found to be widespread in the biological world.…”

Section: Reaction Mechanism Of Exo--14-glucan Lyasementioning

confidence: 99%

A Historical Perspective for the Catalytic Reaction Mechanism of Glycosidase; So As to Bring about Breakthrough in Confusing Situation

Chiba

2012

Bioscience, Biotechnology, and Biochemistry

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Various catalytic reaction models have been proposed as the reaction mechanisms of glycosidases, but a reasonable and unitary model capable of interpreting both ''inverting'' and ''retaining'' glycosidase reactions remains to be established. As for the models proposed to date, the nucleophilic displacement mechanism and the oxocarbenium ion intermediate mechanism are widely known, but recently the former is widely accepted, and so the general tendency of world opinion appears to favor it. This reaction model, however, is considered to comprise some inconsistencies that cannot be neglected from the viewpoint of reactivity in organic chemistry. While the nucleophilic displacement mechanism is often applied to reactions of glycosidases, it appears unlikely that such reactions actually occur. This review argues that the oxocarbenium ion intermediate reaction mechanism is more rational than the nucleophilic displacement reaction mechanism, as the action mode of glycosidases and related enzymes.

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Section: Reaction Mechanism Of Exo--14-glucan Lyasementioning

confidence: 99%

A Historical Perspective for the Catalytic Reaction Mechanism of Glycosidase; So As to Bring about Breakthrough in Confusing Situation

Chiba

2012

Bioscience, Biotechnology, and Biochemistry

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“…2). Purification of the recombinant glucan lyases was performed by anion exchange chromatography using Q-Sepharose FF with 20 mM Bis-Tris, pH 6.7, as buffer A, and buffer A containing 1.0 M NaCl as buffer B (17,18). Further purification was achieved by a second anion exchange chromatography step using a Mono Q column and elution with a gradient of 0.28 -0.32 M NaCl in 20 mM Bis-Tris, pH 6.7.…”

Section: Expression and Purification Of ␣-14-glucan Lyase-thementioning

confidence: 99%

Crystal Structure of α-1,4-Glucan Lyase, a Unique Glycoside Hydrolase Family Member with a Novel Catalytic Mechanism

Rozeboom

Yu²,

Madrid³

et al. 2013

Journal of Biological Chemistry

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Background: ␣-1,4-Glucan lyase (GLase) is a glycoside hydrolase family member that degrades starch via an elimination reaction. Results: Crystal structures of GLase with covalently bound inhibitors show that the catalytic nucleophile can abstract the proton. Conclusion:The nucleophile has a dual function, acting successively as nucleophile and base. Significance: A single substitution converts a glycoside hydrolase into a lyase.

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“…AF with 99% purity was produced from soluble starch by GL (20). GlcAL was prepared from the 3,4,6-tri-O-acetyl form (Sigma-Aldrich) (17).…”

Section: Methodsmentioning

confidence: 99%

“…Due to a tautomerization in the aqueous solution, AF forms enol-, keto-, and hydrated-type structures (Fig. 1C) (19,20). Although the hydrated AF is the major form in water, a 1,2-enol AF mimics the oxocarbenium ion transition state more than GlcAL does (22).…”

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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

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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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α-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. III. Substrate specificity, mode of action, and cleavage mechanism

Cited by 59 publications

References 12 publications

A Historical Perspective for the Catalytic Reaction Mechanism of Glycosidase; So As to Bring about Breakthrough in Confusing Situation

A Historical Perspective for the Catalytic Reaction Mechanism of Glycosidase; So As to Bring about Breakthrough in Confusing Situation

Crystal Structure of α-1,4-Glucan Lyase, a Unique Glycoside Hydrolase Family Member with a Novel Catalytic Mechanism

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

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