These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Transglycosylation reaction of maltotriose-forming amylase from Streptomyces griseus.
    Author: Usui T, Murata T, Yabuuchi Y, Ogawa K.
    Journal: Carbohydr Res; 1993 Dec 16; 250(1):57-66. PubMed ID: 7511484.
    Abstract:
    A maltotriose-forming amylase from Streptomyces griseus produced predominantly p-nitrophenyl alpha-maltotetraoside through a transglycosylation reaction from maltotetraose as a donor and p-nitrophenyl alpha-D-glucopyranoside as an acceptor in an organic co-solvent. With p-nitrophenyl beta-D-glucopyranoside acceptor, the enzyme catalyzed the formation of an alpha-(1-->3)-linked tetrasaccharide (p-nitrophenyl 3(1)-O-alpha-maltotriosyl-beta-D-glucopyranoside) in a yield of 16%, based on the acceptor added with its isomer p-nitrophenyl beta-maltotetraoside. This was also the case for the formation of o-chloro-p-nitrophenyl 3(1)-O-alpha-maltotriosyl-beta-D-glucopyranoside with o-chloro-p-nitrophenyl beta-D-glucopyranoside acceptor. The results shows that the anomeric configuration of the aryl group in the glucosyl acceptors had an effect on the position of transglycosylation.
    [Abstract] [Full Text] [Related] [New Search]