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Enzymic synthesis of monosaccharide-amino acid conjugates

Johansson, Elisabet ; Hedbys, Lars and Larsson, Per-Olof LU (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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author
; and
organization
publishing date
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
2025-10-14 11:25:10
@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}},
}