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Beta-glucose 1-phosphate-interconverting enzymes in maltose- and trehalose-fermenting lactic acid bacteria.

Andersson, Ulrika LU and Rådström, Peter LU (2002) In Environmental Microbiology 4(2). p.81-88
Abstract
Maltose and trehalose catabolic pathways are linked through their common enzyme, beta-phosphoglucomutase, and metabolite, beta-glucose 1-phosphate, in Lactococcus lactis. Maltose is degraded by the concerted action of maltose phosphorylase and beta-phosphoglucomutase, whereas trehalose is assimilated by a novel pathway, including the recently discovered enzyme, trehalose 6-phosphate phosphorylase, and beta-phosphoglucomutase. In the present study, 40 strains of lactic acid bacteria were investigated for utilization of metabolic reactions involving beta-glucose 1-phosphate. All genera of the low G+C content lactic acid bacteria belonging to the clostridial subbranch of Gram-positive bacteria were represented in the study. The strains, which... (More)
Maltose and trehalose catabolic pathways are linked through their common enzyme, beta-phosphoglucomutase, and metabolite, beta-glucose 1-phosphate, in Lactococcus lactis. Maltose is degraded by the concerted action of maltose phosphorylase and beta-phosphoglucomutase, whereas trehalose is assimilated by a novel pathway, including the recently discovered enzyme, trehalose 6-phosphate phosphorylase, and beta-phosphoglucomutase. In the present study, 40 strains of lactic acid bacteria were investigated for utilization of metabolic reactions involving beta-glucose 1-phosphate. All genera of the low G+C content lactic acid bacteria belonging to the clostridial subbranch of Gram-positive bacteria were represented in the study. The strains, which fermented maltose or trehalose, were investigated for beta-phosphoglucomutase, maltose phosphorylase and trehalose 6-phosphate phosphorylase activity, as indications of maltose and trehalose catabolic pathways involving beta-glucose 1-phosphate interconversions. Eighty per cent of all strains fermented maltose and, of these strains, 63% were shown to use a maltose phosphorylase/beta- phosphoglucomutase pathway. One-third of the strains fermenting trehalose were found to harbour trehalose 6-phosphate phosphorylase activity, and these were also shown to possess beta-phosphoglucomutase activity. Mainly L. lactis and Enterococcus faecalis strains were found to harbour the novel trehalose 6-phosphate phosphorylase/beta-phosphoglucomutase pathway. As lower beta-glucose 1-phosphate interconverting enzyme activities were observed in the majority of glucose-cultivated lactic acid bacteria, glucose was suggested to repress the synthesis of these enzymes in most strains. Thus, metabolic reactions involving the beta-anomer of glucose 1-phosphate are frequently found in both maltose- and trehalose-utilizing lactic acid bacteria. (Less)
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organization
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Contribution to journal
publication status
published
subject
keywords
Support, Phosphoglucomutase : metabolism, Maltose : metabolism, Lactococcus lactis : growth & development, Lactococcus lactis : enzymology, Glucosyltransferases : metabolism, Glucosephosphates : metabolism, Glucose, Culture Media, Comparative Study, Non-U.S. Gov't, Trehalose : metabolism
in
Environmental Microbiology
volume
4
issue
2
pages
81 - 88
publisher
Wiley-Blackwell
external identifiers
  • pmid:11972617
  • wos:000175092500003
  • scopus:0036010638
ISSN
1462-2920
DOI
10.1046/j.1462-2920.2002.00268.x
language
English
LU publication?
yes
id
0f2648ac-9ab0-4973-a600-a4274bea3249 (old id 107811)
date added to LUP
2007-06-28 11:28:24
date last changed
2017-07-02 03:47:03
@article{0f2648ac-9ab0-4973-a600-a4274bea3249,
  abstract     = {Maltose and trehalose catabolic pathways are linked through their common enzyme, beta-phosphoglucomutase, and metabolite, beta-glucose 1-phosphate, in Lactococcus lactis. Maltose is degraded by the concerted action of maltose phosphorylase and beta-phosphoglucomutase, whereas trehalose is assimilated by a novel pathway, including the recently discovered enzyme, trehalose 6-phosphate phosphorylase, and beta-phosphoglucomutase. In the present study, 40 strains of lactic acid bacteria were investigated for utilization of metabolic reactions involving beta-glucose 1-phosphate. All genera of the low G+C content lactic acid bacteria belonging to the clostridial subbranch of Gram-positive bacteria were represented in the study. The strains, which fermented maltose or trehalose, were investigated for beta-phosphoglucomutase, maltose phosphorylase and trehalose 6-phosphate phosphorylase activity, as indications of maltose and trehalose catabolic pathways involving beta-glucose 1-phosphate interconversions. Eighty per cent of all strains fermented maltose and, of these strains, 63% were shown to use a maltose phosphorylase/beta- phosphoglucomutase pathway. One-third of the strains fermenting trehalose were found to harbour trehalose 6-phosphate phosphorylase activity, and these were also shown to possess beta-phosphoglucomutase activity. Mainly L. lactis and Enterococcus faecalis strains were found to harbour the novel trehalose 6-phosphate phosphorylase/beta-phosphoglucomutase pathway. As lower beta-glucose 1-phosphate interconverting enzyme activities were observed in the majority of glucose-cultivated lactic acid bacteria, glucose was suggested to repress the synthesis of these enzymes in most strains. Thus, metabolic reactions involving the beta-anomer of glucose 1-phosphate are frequently found in both maltose- and trehalose-utilizing lactic acid bacteria.},
  author       = {Andersson, Ulrika and Rådström, Peter},
  issn         = {1462-2920},
  keyword      = {Support,Phosphoglucomutase : metabolism,Maltose : metabolism,Lactococcus lactis : growth & development,Lactococcus lactis : enzymology,Glucosyltransferases : metabolism,Glucosephosphates : metabolism,Glucose,Culture Media,Comparative Study,Non-U.S. Gov't,Trehalose : metabolism},
  language     = {eng},
  number       = {2},
  pages        = {81--88},
  publisher    = {Wiley-Blackwell},
  series       = {Environmental Microbiology},
  title        = {Beta-glucose 1-phosphate-interconverting enzymes in maltose- and trehalose-fermenting lactic acid bacteria.},
  url          = {http://dx.doi.org/10.1046/j.1462-2920.2002.00268.x},
  volume       = {4},
  year         = {2002},
}