Enzymic synthesis of monosaccharide-amino acid conjugates
(1991) In Enzyme and Microbial Technology 13(10). p.781-787- Abstract
- Enzymatic condensation between amino acids and monosaccharides was studied. A screening involving the OH-containing amino acids serine and threonine and the monosaccharide substrates for the enzymes α-N-acetylgalactosaminidase, α-galactosidase, α-mannosidase, β-xylosidase, and β-galactosidase was carried out. Enzymatic condensation was observed with α-mannosidase and α-N-acetylgalactosaminidase. Products were only detected under reversed hydrolysis conditions, not under transglycosylation conditions with activated substrates. Both l- and d-isomers of the amino acids were substrates for α-mannosidase and α-N-acetylgalactosaminidase. A closer investigation of the formation of α-d-Man-(1–3′)-l-Ser and α-d-GalNAc-(1–3′)-l-Ser was carried out... (More)
- Enzymatic condensation between amino acids and monosaccharides was studied. A screening involving the OH-containing amino acids serine and threonine and the monosaccharide substrates for the enzymes α-N-acetylgalactosaminidase, α-galactosidase, α-mannosidase, β-xylosidase, and β-galactosidase was carried out. Enzymatic condensation was observed with α-mannosidase and α-N-acetylgalactosaminidase. Products were only detected under reversed hydrolysis conditions, not under transglycosylation conditions with activated substrates. Both l- and d-isomers of the amino acids were substrates for α-mannosidase and α-N-acetylgalactosaminidase. A closer investigation of the formation of α-d-Man-(1–3′)-l-Ser and α-d-GalNAc-(1–3′)-l-Ser was carried out at 35°C and 55°C, at which temperature the reaction rates were greatly increased. (Less)
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https://lup.lub.lu.se/record/e1da7aac-ccf7-43f4-b3db-717a4234178d
- author
- Johansson, Elisabet ; Hedbys, Lars and Larsson, Per-Olof LU
- organization
- publishing date
- 1991
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Glycosidases, Reversed hydrolysis, Mannosidase, Acetylgalactosaminidase, Monosaccharide-amino acid conjugates
- in
- Enzyme and Microbial Technology
- volume
- 13
- issue
- 10
- pages
- 7 pages
- publisher
- Elsevier
- external identifiers
-
- scopus:0026245542
- ISSN
- 0141-0229
- DOI
- 10.1016/0141-0229(91)90060-N
- language
- English
- LU publication?
- yes
- id
- e1da7aac-ccf7-43f4-b3db-717a4234178d
- date added to LUP
- 2024-06-17 13:14:44
- date last changed
- 2024-10-05 04:03:23
@article{e1da7aac-ccf7-43f4-b3db-717a4234178d, abstract = {{Enzymatic condensation between amino acids and monosaccharides was studied. A screening involving the OH-containing amino acids serine and threonine and the monosaccharide substrates for the enzymes α-N-acetylgalactosaminidase, α-galactosidase, α-mannosidase, β-xylosidase, and β-galactosidase was carried out. Enzymatic condensation was observed with α-mannosidase and α-N-acetylgalactosaminidase. Products were only detected under reversed hydrolysis conditions, not under transglycosylation conditions with activated substrates. Both l- and d-isomers of the amino acids were substrates for α-mannosidase and α-N-acetylgalactosaminidase. A closer investigation of the formation of α-d-Man-(1–3′)-l-Ser and α-d-GalNAc-(1–3′)-l-Ser was carried out at 35°C and 55°C, at which temperature the reaction rates were greatly increased.}}, author = {{Johansson, Elisabet and Hedbys, Lars and Larsson, Per-Olof}}, issn = {{0141-0229}}, keywords = {{Glycosidases; Reversed hydrolysis; Mannosidase; Acetylgalactosaminidase; Monosaccharide-amino acid conjugates}}, language = {{eng}}, number = {{10}}, pages = {{781--787}}, publisher = {{Elsevier}}, series = {{Enzyme and Microbial Technology}}, title = {{Enzymic synthesis of monosaccharide-amino acid conjugates}}, url = {{http://dx.doi.org/10.1016/0141-0229(91)90060-N}}, doi = {{10.1016/0141-0229(91)90060-N}}, volume = {{13}}, year = {{1991}}, }