Strategy in manipulating transglycosylation activity of glycosyl hydrolase for oligosaccharide production.

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Strategy in manipulating transglycosylation activity of glycosyl hydrolase for oligosaccharide production.

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年學術文章

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Strategy in manipulating trans ...... or oligosaccharide production.

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Strategy in manipulating trans ...... or oligosaccharide production.

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Strategy in manipulating trans ...... or oligosaccharide production.

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P1476

Strategy in manipulating trans ...... for oligosaccharide production

@en

P2093

Nor Muhammad Mahadi

http://www.w3.org/2001/XMLSchema#string

Rosli Md Illias

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P2860

Hydrogen bonding and catalysis: a novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase

Structures of maltohexaose and maltoheptaose bound at the donor sites of cyclodextrin glycosyltransferase give insight into the mechanisms of transglycosylation activity and cyclodextrin size specificity

Role of Phe286 in the recognition mechanism of cyclomaltooligosaccharides (cyclodextrins) by Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structures of the mutant TVAIIs, F286A and F286Y, and kinetic analyses of the Phe286-replaced

Xylan binding subsite mapping in the xylanase from Penicillium simplicissimum using xylooligosaccharides as cryo-protectant

Conversion of cyclodextrin glycosyltransferase into a starch hydrolase by directed evolution: the role of alanine 230 in acceptor subsite +1

Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 1 with malto-oligosaccharides demonstrate the role of domain N acting as a starch-binding domain

Strategies for modulating the pH-dependent activity of a family 11 glycoside hydrolase

A Trapped Covalent Intermediate of a Glycoside Hydrolase on the Pathway to Transglycosylation. Insights from Experiments and Quantum Mechanics/Molecular Mechanics Simulations

Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 angstrom resolution. Implications for product specificity

Structure of the Aspergillus oryzae alpha-amylase complexed with the inhibitor acarbose at 2.0 A resolution

P304

272-293

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P31

scholarly article

P356

10.1080/07388551.2017.1339664

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Nor Hasmaliana Abdul Manas

P577

2017-07-06T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

28683572

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P921

oligosaccharide