» Articles » PMID: 1839141

Maltodextrin Acceptor Reactions of Streptococcus Mutans 6715 Glucosyltransferases

Overview
Journal Carbohydr Res
Publisher Elsevier
Date 1991 Sep 18
PMID 1839141
Citations 8
Authors
Affiliations
Soon will be listed here.
Abstract

The maltodextrin (maltose through maltoheptaose) acceptor reactions of two Streptococcus mutans 6715 glucosyltransferases (GTF-I and GTF-S) were studied. The acceptor product structures were determined by comparing them with the known structures of the acceptor products of Leuconostoc mesenteroides B-512FM dextransucrase (EC 2.4.1.5) and L. mesenteroides B-1355 alternansucrase (EC 2.4.1.140). When reacted with maltose (G2), both GTF-I and GTF-S transferred a D-glucopyranose from sucrose to the nonreducing glucosyl residue to give panose (6(2)-alpha-D-glucopyranosyl maltose). Panose then served as an acceptor to give two further acceptor products, 6(2)-alpha-isomaltosyl maltose and 6(2)-alpha-nigerosyl maltose. 6(2)-alpha-Isomaltosyl maltose then went on to serve as an acceptor to give a series of homologous acceptor products with isomaltodextrin chains attached to C-6 of the nonreducing-end residue of maltose, while 6(2)-alpha-nigerosyl maltose did not further react. When reacted with other maltodextrins (G3-G7), both GTF-I and GTF-S transferred a D-glucopyranose to C-6 of either the nonreducing-end or the reducing-end residues of the maltodextrins, forming alpha(1----6) linkages. When D-glucopyranose was transferred to the nonreducing-end residue by GTF-I or GTF-S, the first product was also an acceptor to give the second product, which then served as an acceptor to give the third product, etc., to give a homologous series of products. When D-glucopyranose was transferred to the reducing-end residue, the acceptor product that formed did not readily serve as an acceptor, or served only as a very poor acceptor, to give a small amount of the next homologue, as was the case for G7 with GTF-S. In addition, GTF-I also transferred D-glucopyranose to the reducing-end or to the nonreducing-end residue of maltotriose, forming alpha(1----3) linkages, to give 3(3)-alpha-D-glucopyranosyl maltotriose and 3(1)-alpha-D-glucopyranosyl maltotriose. Neither of these acceptor products further served as acceptors to give a homologous series. Under equivalent conditions of equimolar amounts of acceptor and sucrose, maltose and maltotriose are much better acceptors with GTF-I than they are with GTF-S, which is better than L. mesenteroides B-512FM dextransucrase. The three enzymes display significantly different efficiencies for the different maltodextrin acceptor reactions, GTF-I and GTF-S having much higher efficiencies than L. mesenteroides B-512FM dextransucrase.

Citing Articles

Inhibition of Streptococcus mutans polysaccharide synthesis by molecules targeting glycosyltransferase activity.

Ren Z, Chen L, Li J, Li Y J Oral Microbiol. 2016; 8:31095.

PMID: 27105419 PMC: 4841093. DOI: 10.3402/jom.v8.31095.


Streptococcus mutans-derived extracellular matrix in cariogenic oral biofilms.

Klein M, Hwang G, Santos P, Campanella O, Koo H Front Cell Infect Microbiol. 2015; 5:10.

PMID: 25763359 PMC: 4327733. DOI: 10.3389/fcimb.2015.00010.


4,6-α-glucanotransferase, a novel enzyme that structurally and functionally provides an evolutionary link between glycoside hydrolase enzyme families 13 and 70.

Kralj S, Grijpstra P, van Leeuwen S, Leemhuis H, Dobruchowska J, van der Kaaij R Appl Environ Microbiol. 2011; 77(22):8154-63.

PMID: 21948833 PMC: 3209003. DOI: 10.1128/AEM.05735-11.


Biology of Streptococcus mutans-derived glucosyltransferases: role in extracellular matrix formation of cariogenic biofilms.

Bowen W, Koo H Caries Res. 2011; 45(1):69-86.

PMID: 21346355 PMC: 3068567. DOI: 10.1159/000324598.


Dynamics of Streptococcus mutans transcriptome in response to starch and sucrose during biofilm development.

Klein M, DeBaz L, Agidi S, Lee H, Xie G, Lin A PLoS One. 2010; 5(10):e13478.

PMID: 20976057 PMC: 2957427. DOI: 10.1371/journal.pone.0013478.