ChemInform Abstract: Semisynthesis of a Homogeneous Glycoprotein Enzyme: Ribonuclease C. Part 2.

Piontek, Christian; Silva, Daniel Varón; Heinlein, Christian; Poehner, C.; Mezzato, Stefano; Ring, Petra; Martin, Andreas; Schmid, Franz X.; Unverzagt, Carlo

doi:10.1002/chin.200918200

Cited by 1 publication

(1 citation statement)

References 1 publication

Supporting

Mentioning

Contrasting

Order By: Relevance

“…[9] Access to single glycoforms of glycoproteins can be A C H T U N G T R E N N U N G achieved by total synthesis of both glycan and polypeptide components, and outstanding achievements in this area have recently been published. [10,11] However, such synthetic approaches are particularly arduous, and do not realistically represent a practical approach that could be applied to widespread and large-scale glycoprotein production. Approaches based on bioengineering of cell lines in order to optimise production of glycoproteins bearing particular oligosaccharide structures have also been reported, [12,13] and been exploited commercially, though such approaches have no guarantee of complete glycan homogeneity.…”

Section: Introductionmentioning

confidence: 99%

Endohexosaminidase‐Catalysed Glycosylation with Oxazoline Donors: Fine Tuning of Catalytic Efficiency and Reversibility

Rising

Heidecke

Moir

et al. 2008

Chemistry A European J

View full text Add to dashboard Cite

A complete series of oxazoline di-, tri-, tetra-, and hexasaccharides, corresponding to the core sections of N-linked glycoprotein high mannose glycans, together with the corresponding oligosaccharides containing a central glucose unit, were synthesised and tested as glycosyl donors for glycosylation of a GlcNAcAsn glycosyl amino acid catalysed by the endohexosaminidases M (Endo M), A (Endo A) and H (Endo H). Whilst Endo H did not catalyse any glycosylation reactions, both Endo M and Endo A efficiently catalysed glycosylations that were not limited to donors containing the Manbeta(1-->4)GlcNAc linkage. Precise structure activity relationships and time course studies have revealed fine-tuning of the efficiency of the synthetic processes which correlated both with the enzyme used and the precise oxazoline structure. Efficient irreversible glycosylation was achievable with both Endo M and Endo A, further demonstrating the use of structurally modified oxazoline donors as transition state mimics in order to promote enzyme-catalysed synthesis, whilst precluding product hydrolysis; enzymes in these cases display "glycoligase" activity.

show abstract

Section: Introductionmentioning

confidence: 99%

Endohexosaminidase‐Catalysed Glycosylation with Oxazoline Donors: Fine Tuning of Catalytic Efficiency and Reversibility

Rising

Heidecke

Moir

et al. 2008

Chemistry A European J

View full text Add to dashboard Cite

show abstract

ChemInform Abstract: Semisynthesis of a Homogeneous Glycoprotein Enzyme: Ribonuclease C. Part 2.

Abstract: Enzymes U 1100 Semisynthesis of a Homogeneous Glycoprotein Enzyme: Ribonuclease C. Part 2. -(PIONTEK, C.; SILVA, D. V.; HEINLEIN, C.; POEHNER, C.; MEZZATO, S.; RING, P.; MARTIN, A.; SCHMID, F. X.; UNVERZAGT*, C.; Angew.

Cited by 1 publication

References 1 publication

Endohexosaminidase‐Catalysed Glycosylation with Oxazoline Donors: Fine Tuning of Catalytic Efficiency and Reversibility

Endohexosaminidase‐Catalysed Glycosylation with Oxazoline Donors: Fine Tuning of Catalytic Efficiency and Reversibility

Contact Info

Product

Resources

About