Exploitation of a library of α‐galactosidases for the synthesis of building blocks for glycopolymers

Casali, Monica; Tarantini, Letizia; Riva, Sergio; Huňková, Zdenka; Weignerová, Lenka; Křen, Vladimı́r

doi:10.1002/bit.10101

Cited by 13 publications

(6 citation statements)

References 19 publications

(13 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Fungal α-galactosidases were also reported for the synthesis of α-galactosides of different alcohols using reverse hydrolysis and transglycosylation reactions [44] and for the study of regioselectivity using p-nitrophenyl galactopyranoside as donor and acceptor. α-1-2, α-1-3 and α-1-6 dimers of the substrate were isolated and characterized in the latter case [45].…”

Section: Glycosyl Hydrolases α-Galactosidasesmentioning

confidence: 99%

Glycosyl Hydrolases and Glycosyltransferases in the Synthesis of Oligosaccharides

Trincone¹,

Giordano

2006

COC

View full text Add to dashboard Cite

Glycobiology and related disciplines have received an enormous interest in recent years as they shed new light on the functional roles of carbohydrates in biological events leading to the understanding of mechanisms of important pathologies and to the development of new therapeutics. Although carbohydrate can be isolated from natural sources, the synthetic strategy plays its own role allowing access to larger quantities of structurally defined material and entry to analogs of naturally occurring structures. Nowadays, the bottleneck in this field is represented by some limitations of the potential of carbohydrate containing molecules because their complex structures make classical chemical synthesis very difficult.The synthesis of oligosaccharides have to face with three main snags: (i) reactivity of the leaving group on the monosaccharide acting as donor; (ii) regioselectivity towards a single hydroxyl group on the acceptor molecule; (iii) stereoselectivity in forming pure anomers of the new glycosidic product. The protecting-group manipulations that are needed for the stereocontrol of the products are demanding procedures thus yields and selectivity are lowered hindering the efficient production of oligosaccharides needed for biological testing.A particular benefit of the renewed interest for sugar chemistry has been the attention of scientific community to the biological methodologies in the production of oligosaccharides, an area which emerged in recent decades.In the carbohydrate field different enzymes were used for diverse purposes but enzymatic strategies for high-yield and stereospecific construction of glycosidic bonds are based on the action of two types of enzymes: glycosyl hydrolases (endo-and exo-glycosidases) and glycosyltransferases. Glycosyl hydrolases in the cells are responsible for the cleavage of glycosidic linkages; the exo-glycosidase are involved for glycan processing during in vivo glycoprotein synthesis. The glycosyltransferases are instead responsible in vivo for the synthesis of most cell-surface glycoconjugates.This review deals with the application of different types of glycosyl hydrolases. Elegant examples concerning the use of genetically modified representatives of glycosyl hydrolases (glycosynthases and thioglycoligases) will be also reported; some recent advances on the use of glycosyltransferases are also included.In compiling this review we were aware of the huge amount of excellent material published in the recent years on this topic, thus we will limit the covering of literature to the last decade. Attention will be devoted to the regioselectivity towards pyranosidic templates and to the yield of reactions. The molecular diversity obtained by the use of enzymes from different biological sources and the biological importance of the compounds synthesized will be focused as well.This review will put in evidence that glycosyl hydrolases and glycosyltransferases for the synthesis of the glycosidic linkages will play a relevant role in the next future as on the bench bio-catalysts ...

show abstract

Section: Glycosyl Hydrolases α-Galactosidasesmentioning

confidence: 99%

Glycosyl Hydrolases and Glycosyltransferases in the Synthesis of Oligosaccharides

Trincone¹,

Giordano

2006

COC

View full text Add to dashboard Cite

show abstract

“…HRESIMS: (m/z) calcd for C 8 H 15 O 8 NNa + (M + Na) + 276.0695; found 276.0694. Compound 3d has been reported 47. Partial characterization was by 13 C NMR spectroscopy (reported only seven peaks) in DMSO-d 6 .1,3-Dichloropropan-2-yl 2,3,4,6-tetra-O-acetyl-α-D-galactopyranoside (4e).…”

mentioning

confidence: 99%

1,2-cis Alkyl glycosides: straightforward glycosylation from unprotected 1-thioglycosyl donors

2014

View full text Add to dashboard Cite

A 1,2-cis-alkyl glycosidation protocol that makes use of unprotected phenyl 1-thioglycosyl donors is reported. Glycosylation of various functionalized alcohols was accomplished in moderate to high yield and selectivity to give the 1,2-cis-glycosides. In order to quickly develop optimum glycosylation conditions, an FIA (flow injection analysis)-ESI-TOF-MS method was developed that enabled rapid and quantitative evaluation of yield on small scale. This methodology, coupled with NMR spectroscopy, allowed for rapid evaluation of the overall reactions.

show abstract

“…Other fungal enzymes such as α-D-galactosidases isolated from Aspergillus terreus CCM55, Aspergillus commune CCM 2969, Penicillium vinaceum CCM 2384 or Penicillium brasilianum 2155 were used (entry 7 Table 3) both in transglycosylation or reverse hydrolysis for the formation of three α-galactosides of allyl-, 2-nitroethyl-or (2',2',2'-trifluoroacetamido)-ethyl-aglycones (Casali et al, 2002). The same group of authors studied the dependence of fungal activity on the presence of organic cosolvents (entry 10 Table 3) for the synthesis of acylated glycosides in a publication reporting the preparation of 4-nitrophenyl α-Dgalactopyranosyl-(1,3)-6-O-acetyl-α-D-galactopyranoside catalyzed by α-D-galactosidase from Talaromyces flavus (Simerska et al, 2003).…”

Section: Synthesismentioning

confidence: 99%

Hooked on α-d-galactosidases: from biomedicine to enzymatic synthesis

Bakunina

Balabanova

Pennacchio

et al. 2015

Critical Reviews in Biotechnology

View full text Add to dashboard Cite

α-d-Galactosidases (EC 3.2.1.22) are enzymes employed in a number of useful bio-based applications. We have depicted a comprehensive general survey of α-d-galactosidases from different origin with special emphasis on marine example(s). The structures of natural α-galactosyl containing compounds are described. In addition to 3D structures and mechanisms of action of α-d-galactosidases, different sources, natural function and genetic regulation are also covered. Finally, hydrolytic and synthetic exploitations as free or immobilized biocatalysts are reviewed. Interest in the synthetic aspects during the next years is anticipated for access to important small molecules by green technology with an emphasis on alternative selectivity of this class of enzymes from different sources.

show abstract

Exploitation of a library of α‐galactosidases for the synthesis of building blocks for glycopolymers

Cited by 13 publications

References 19 publications

Glycosyl Hydrolases and Glycosyltransferases in the Synthesis of Oligosaccharides

Glycosyl Hydrolases and Glycosyltransferases in the Synthesis of Oligosaccharides

1,2-cis Alkyl glycosides: straightforward glycosylation from unprotected 1-thioglycosyl donors

Hooked on α-d-galactosidases: from biomedicine to enzymatic synthesis

Contact Info

Product

Resources

About