Beta-glucose 1-phosphate-interconverting enzymes in maltose- and trehalose-fermenting lactic acid bacteria.
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/107811
- author
- Andersson, Ulrika LU and Rådström, Peter LU
- organization
- publishing date
- 2002
- type
- 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
- 2016-04-01 12:35:48
- date last changed
- 2022-01-27 07:17:18
@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}},
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}},
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}},
doi = {{10.1046/j.1462-2920.2002.00268.x}},
volume = {{4}},
year = {{2002}},
}