Recent Advances in the Chemoenzymatic Synthesis of Carbohydrates and Carbohydrate Mimetics

Gijsen, Harrie J. M.; Qiao, Lei; Fitz, Wolfgang; Wong, Chi‐Huey

doi:10.1021/cr950031q

Cited by 415 publications

(168 citation statements)

References 362 publications

Supporting

Mentioning

164

Contrasting

Unclassified

Order By: Relevance

“…Thus, NeuNAc aldolase has been used to synthesize a variety of NeuNAc derivatives or analogs by enzymatic method. [19][20][21][22][23][24][25][26][27] To find out the optical substrates for the bioengineering of NeuNAc on tumor cells, and other cells as well, by utilizing the permissibility of NeuNAc aldolase, it is necessary to understand the reactions of various N-acyl-D-mannosamines with the enzyme. For this purpose, the accessibility of a number of N-acyl derivatives of D-mannosamine to NeuNAc aldolase was investigated.…”

Section: Introductionmentioning

confidence: 99%

Accessibility of N-acyl-d-mannosamines to N-acetyl-d-neuraminic acid aldolase

Pan

Ayani

Nadas

et al. 2004

Carbohydrate Research

View full text Add to dashboard Cite

N-Acetyl-D-neuraminic acid (NeuNAc) aldolase is an important enzyme for the metabolic engineering of cell surface NeuNAc using chemically modified D-mannosamines. To explore the optimal substrates for this application, eight N-acyl derivatives of D-mannosamine were prepared, and their accessibility to NeuNAc aldolase was investigated quantitatively. The N-propionyl-, Nbutanoyl-, N-iso-butanoyl-, N-pivaloyl-and N-phenylacetyl-D-mannosamines proved to be as good substrates as, or even better than, the natural N-acetyl-D-mannosamine, while the Ntrifluoropropionyl and benzoyl derivatives were poor. It was proposed that the electronic effects might have a significant influence on the enzymatic aldol condensation reaction of D-mannosamine derivatives, with electron-deficient acyl groups having a negative impact. The results suggest that N-propionyl-, N-butanoyl-, N-iso-butanoyl-and N-phenylacetyl-D-mannosamines may be employed to bioengineer NeuNAc on cells.

show abstract

Section: Introductionmentioning

confidence: 99%

Accessibility of N-acyl-d-mannosamines to N-acetyl-d-neuraminic acid aldolase

Pan

Ayani

Nadas

et al. 2004

Carbohydrate Research

View full text Add to dashboard Cite

show abstract

“…Chemical synthesis of carbohydrates is an inefficient and labor-intensive process (Ichikawa et al, 1992). Therefore, these enzymes may be unique and powerful tools as catalysts for regio-and stereospecific synthesis of oligosaccharides (Ichikawa et al, 1992;Gijsen et al, 1996). Glycosyltransferases, especially their large-scale expression, have become one of the prime targets in the pharmaceutical industry (Karlsson, 1991).…”

Section: Introductionmentioning

confidence: 99%

Expression and Characterization of β-1,4-Galactosyltransferase from Neisseria meningitidis and Neisseria gonorrhoeae

Park¹,

Lee²,

Il³

et al. 2002

BMB Reports

View full text Add to dashboard Cite

The lgtB genes that encode β-1,4-galactosyltransferases from Neisseria meningitidis ATCC 13102 and gonorrhoeae ATCC 31151 were isolated by a polymerase chain reaction using the pfu DNA polymerase. They were expressed under the control of lac and T7 promoters in Escherichia coli M15 and BL21 (DE3). Although the genes were efficiently expressed in E. coli M15 at 37 o C (33 kDa), most of the β-1,4-galactosyltransferases that were produced were insoluble and proteolysed into enzymatically inactive polypeptides that lacked C-terminal residues (29.5 kDa and 28 kDa) during the purification steps. When the temperature of the cell growth was lowered to 25 o C, however, the solubility of the β-1,4-galactosyltransferases increased substantially. A stable N-terminal his-tagged recombinant enzyme preparation could be achieved with E. coli BL21 (DE3) that expressed lgtB. Therefore, the cloned β-1,4-galactosyltransferases were expressed under the control of the T7 promoter in E. coli BL21 (DE3), mostly to the soluble form at 25 o C. The proteins were easily purified to homogeneity by column chromatography using Ni-NTA resin, and were found to be active. The galactosyltransferases exhibited pH optimum at 6.5-7.0, and had an essential requirement for the Mn +2 ions for its action. The Mg +2 and Ca +2 ions showed about half of the galactosyltransferase activities with the Mn +2 ion. In the presence of the Fe +2 ion, partial activation was observed with the β-1,4-galactosyltransferase from N. meningitidis (64% of the enzyme activity with the Mn +2 ion), but not from N. gonorrhoeae. ions, the Mn +2 ion could not activate the enzyme activities. Also, the β-1,4-galactosyltransferase activity was 1.5-fold stimulated with the non-ionic detergent Triton X-100 (0.1-5%).

show abstract

“…Consequently, they are carriers of large amounts of biological information that originates from the specificity of glycosyltransferases. In addition to their biosynthetic roles, some glycosyltransferases also function directly in cellular interactions and regulation (4,5). The limited information currently available regarding the structural basis of molecular recognition and catalysis by these important enzymes precludes a clear understanding of the molecular basis of their various biological functions.…”

mentioning

confidence: 99%

Structure of UDP Complex of UDP-galactose:β-Galactoside-α-1,3-galactosyltransferase at 1.53-Å Resolution Reveals a Conformational Change in the Catalytically Important C Terminus

Boix

Swaminathan

Zhang

et al. 2001

Journal of Biological Chemistry

View full text Add to dashboard Cite

Specific hetero-oligosaccharides on glycoproteins and glycolipids play important roles in cell-cell and cell-matrix interactions, affect the stability and structure of proteins, and modulate cellular interactions with viruses, toxins, and other proteins; they are also epitopes that are recognized by the immune system (1). The range and types of carbohydrate structures present on a cell vary in different tissues and species as a reflection of the specificity of glycosyltransferases, enzymes that catalyze the transfer of a specific monosaccharide from an activated derivative (such as UDP-galactose) into a defined linkage with a specific acceptor (2, 3). The carbohydrate chains of glycoconjugates have an enormous potential for variation because of the range of different sugars and the large number of alternative glycosidic linkages. Consequently, they are carriers of large amounts of biological information that originates from the specificity of glycosyltransferases. In addition to their biosynthetic roles, some glycosyltransferases also function directly in cellular interactions and regulation (4, 5). The limited information currently available regarding the structural basis of molecular recognition and catalysis by these important enzymes precludes a clear understanding of the molecular basis of their various biological functions. High resolution structural data are also needed to inform the design of inhibitors and to facilitate the engineering of new catalysts for the enzymatic synthesis of natural and novel glycoconjugates for therapeutic uses (4, 6, 7).

show abstract

Recent Advances in the Chemoenzymatic Synthesis of Carbohydrates and Carbohydrate Mimetics

Cited by 415 publications

References 362 publications

Accessibility of N-acyl-d-mannosamines to N-acetyl-d-neuraminic acid aldolase

Accessibility of N-acyl-d-mannosamines to N-acetyl-d-neuraminic acid aldolase

Expression and Characterization of β-1,4-Galactosyltransferase from Neisseria meningitidis and Neisseria gonorrhoeae

Structure of UDP Complex of UDP-galactose:β-Galactoside-α-1,3-galactosyltransferase at 1.53-Å Resolution Reveals a Conformational Change in the Catalytically Important C Terminus

Contact Info

Product

Resources

About