| Literature DB >> 27316872 |
K Yamamoto1, K Yoshikawa1, S Okada1.
Abstract
The detailed action mechanism of dextrin dextranase (EC 2.4.1.2, DDase) from Acetobacter capsulatus ATCC 11894 was investigated. DDase catalyzed the transglucosylation action of the non-reducing terminal glucosyl residue of a donor substrate, and three transglucosylation modes were recognized; (1) transfer of an α-1,4 linked glucosyl residue forming an α-1,6 linkage, (2) transfer of an α-1,4 linked glucosyl residue forming an α-1,4 linkage, (3) transfer of an α-1,6 linked glucosyl residue forming an α-1,6 linkage. From these results, the action of DDase was considered to transfer α-1,4 or α-1,6 linked glucosyl residues at non-reducing termini of oligosaccharides to glucose molecules or glucosyl residues at non-reducing termini of other oligosaccharides forming α-1,4 or α-1,6 linkages. As the α-1,6 linked terminal glucosyl residues were less reactive than α-1,4linked terminal glucosyl residues, DDase accumulated the α-1,6linked glucosyl residues, which is dextran.Entities:
Year: 1993 PMID: 27316872 DOI: 10.1271/bbb.57.47
Source DB: PubMed Journal: Biosci Biotechnol Biochem ISSN: 0916-8451 Impact factor: 2.043