Sucrose-Utilizing Transglucosidases for Biocatalysis

André, Isabelle; Potocki-Véronèse, Gabrielle; Morel, Sandrine; Monsan, Pierre; Remaud‐Siméon, Magali

doi:10.1007/128_2010_52

Cited by 52 publications

(43 citation statements)

References 131 publications

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“…[6] They are produced by various strains and have been characterized from Alteromonas, Arthrobacter, Deinococcus, and Neisseria species. [7] They naturally catalyze the synthesis of a-1,4-glucans, together with some secondary reactions (sucrose isomerization and hydrolysis). Interestingly, amylosucrases have also been shown to glucosylate various non-natural hydroxylated acceptors such as flavonoids, hydroquinone, catechin, and carbohydrates.…”

Section: Introductionmentioning

confidence: 99%

Probing Substrate Promiscuity of Amylosucrase from Neisseria polysaccharea

Daudé¹,

Champion²,

Morel³

et al. 2013

ChemCatChem

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The amylosucrase from Neisseria polysaccharea (NpAS) naturally catalyzes the synthesis of a variety of products from sucrose and shows signs of plasticity of its active site. To explore further this promiscuity, the tolerance of amylosucrase towards different donor and acceptor substrates was investigated. The selection of alternate donor substrates was first made on the basis of preliminary molecular modeling studies. From 11 potential donors harboring selective derivatizations that were experimentally evaluated, only p‐nitrophenyl‐α‐D‐glucopyranoside was used by the wild‐type enzyme, and this underlines the high specificity of the −1 subsite of NpAS for glucosyl donor substrates. The acceptor substrate promiscuity was further explored by screening 20 hydroxylated molecules, including D‐ and L‐monosaccharides as well as polyols. With the exception of one compound, all were successfully glucosylated, and this showcases the tremendous plasticity of the +1 subsite of NpAS, which is responsible for acceptor recognition. The products obtained from the transglucosylation reactions of three selected acceptors were characterized, and they revealed original structures and enzyme enantiopreference, which were more particularly analyzed by in silico docking analyses.

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Section: Introductionmentioning

confidence: 99%

Probing Substrate Promiscuity of Amylosucrase from Neisseria polysaccharea

Daudé¹,

Champion²,

Morel³

et al. 2013

ChemCatChem

Self Cite

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“…By contrast, fructosyltransferases transfer the fructosyl moiety, resulting in the synthesis of fructooligosaccharides and/or fructan polymers, such as levan or inulin [65][66][67]. Current efforts for enzyme development focus on side-directed mutagenesis, directed evolution, and chimeric enzyme construction to modulate the different activities and improve product properties and yields [68].…”

Section: Polymerization (Oligomerization) By Transglycosylation With mentioning

confidence: 98%

When Enzymes Do It Better: Enzymatic Glycosylation Methods

Planas¹,

Faijes²,

Codera³

2015

Carbohydrate Chemistry: State of the Art and Challenges for Drug Development

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Glycoside Bond Formation by CAZymesCarbohydrates, in the forms of oligosaccharides, polysaccharides, and glycoconjugates (glycoproteins, glycolipids, glycosylated metabolites, etc) are key biomolecules in all living organisms. They play roles in a variety of biological functions as structural components of cell walls, reserves of stored energy, and mediators of cell-cell interactions, being central components in many important biological recognition processes, such as cell adhesion and signaling, cancer progression, host-pathogen interactions, and immune responses [1][2][3][4][5].Synthetic tools to access natural and non-natural glycosides and glycoconjugates have become a central issue in glycochemistry and glycobiology. Both for industrial applications in diverse fields, such as medicine, pharmacology, food, cosmetics, etc., as well as for biological research in functional glycomic studies, there is the need for efficient synthetic approaches for structurally defined oligosaccharides and glycoconjugates. In contrast to conventional chemical synthesis that requires complex and tedious protection/deprotection manipulations and activation strategies to achieve regio-and Carbohydrate Chemistry: State of the Art and Challenges for Drug Development Downloaded from www.worldscientific.com by UNIVERSITY OF PITTSBURGH on 10/02/15. For personal use only.

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“…GS from glycoside hydrolase family 70 (Gh70) produce dextransucrase (ec 2.1.4.5), mutansucrase (ec 2.1.4.5), alternansucrase (ec 2.1.4.140), and reuteransucrase (ec 2.1.4.5) (1,28).…”

Section: Introductionmentioning

confidence: 99%