A novel alpha-D-galactosynthase from Thermotoga maritima converts beta-D-galactopyranosyl azide to alpha-galacto-oligosaccharides. (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• A novel alpha-D-galactosynthase from Thermotoga maritima converts beta-D-galactopyranosyl azide to alpha-galacto-oligosaccharides. (Articolo in rivista) (literal)

Anno

• 2011-01-01T00:00:00+01:00 (literal)

Alternative label

• Cobucci-Ponzano B, Zorzetti C, Strazzulli A, Carillo S, Bedini E, Corsaro MM, Comfort DA, Kelly RM, Rossi M, Moracci M. (2011)
  A novel alpha-D-galactosynthase from Thermotoga maritima converts beta-D-galactopyranosyl azide to alpha-galacto-oligosaccharides.
  in Glycobiology (Oxf.)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Cobucci-Ponzano B, Zorzetti C, Strazzulli A, Carillo S, Bedini E, Corsaro MM, Comfort DA, Kelly RM, Rossi M, Moracci M. (literal)

Pagina inizio

• 448 (literal)

Pagina fine

• 456 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 21 (literal)

Rivista

• Glycobiology (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Titolo

• A novel alpha-D-galactosynthase from Thermotoga maritima converts beta-D-galactopyranosyl azide to alpha-galacto-oligosaccharides. (literal)

Abstract

• The large-scale production of oligosaccharides is a daunting task, hampering the study of the role of glycans in vivo and the testing of the efficacy of novel glycan-based drugs. Glycosynthases, mutated glycosidases that synthesize oligosaccharides in high yields, are becoming important chemo-enzymatic tools for the production of oligosaccharides. However, while ²-glycosynthase can be produced with a rather well established technology, examples of ±-glycosynthases are thus far limited only to enzymes from families GH29, GH31 and GH95. ±-L-Fucosynthases from GH29 use convenient glycosyl azide derivatives as a strategic alternative to glycosyl fluoride donors. However, the general applicability of this method to other ±-glycosynthases is not trivial and remains to be confirmed. Here, ²-D-galactopyranosyl azide was converted to ±-galacto-oligosaccharides with good yields and high regioselectivity, catalyzed by a novel ±-galactosynthase based on the GH36 ±-galactosidase from the hyperthermophilic bacterium Thermotoga maritima. These results open a new avenue to the practical synthesis of biologically interesting ±-galacto-oligosaccharides and demonstrate more widespread use of ²-glycosyl-azide as donors confirming their utility to expand the repertoire of glycosynthases. (literal)

Prodotto di

• DR. MORACCI: Studio del Rapporto Struttura-Funzione e progettazione di Enzimi e Proteine (SV.P14.004.001) (Modulo)
• PROF. M. ROSSI: Applicazioni innovative di enzimi e biotrasformazioni (SV.P14.002.001) (Modulo)
• Institute of protein biochemistry (IBP) (Istituto)

Autore CNR

• MARCO MORACCI (Unità di personale interno)
• ANDREA STRAZZULLI (Unità di personale esterno)
• Mosè Rossi (Unità di personale esterno)
• BEATRICE COBUCCI PONZANO (Persona)

Incoming links:

Autore CNR di

• MARCO MORACCI (Unità di personale interno)
• BEATRICE COBUCCI PONZANO (Persona)
• Mosè Rossi (Unità di personale esterno)
• ANDREA STRAZZULLI (Unità di personale esterno)

Prodotto

• Institute of protein biochemistry (IBP) (Istituto)
• PROF. M. ROSSI: Applicazioni innovative di enzimi e biotrasformazioni (SV.P14.002.001) (Modulo)
• DR. MORACCI: Studio del Rapporto Struttura-Funzione e progettazione di Enzimi e Proteine (SV.P14.004.001) (Modulo)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Glycobiology (Rivista)