Rhodothermus marinus: a thermophilic bacterium producing dimeric and hexameric citrate synthase isoenzymes.
Nordberg Karlsson, Eva LU
; Abou-Hachem, Maher
LU
; Holst, Olle
LU
; Danson, Michael J
and Hough, David W
(2002)
In Extremophiles
6(1).
p.51-56
- Abstract
- Two separate citrate synthases from the extremely thermophilic bacterium Rhodothermus marinus have been identified and purified. One of the enzymes is a hexameric protein and is the first thermostable, hexameric citrate synthase to be isolated. The other is a dimeric enzyme, which is also thermostable but possesses both citrate synthase and 2-methyl citrate synthase activities. 2-Methyl citrate synthase uses propionyl-coenzyme A as one of its substrates and in Escherichia coli, for example, it has been implicated in the metabolism of propionate. However, no growth of R. marinus was observed using minimal medium with propionate as the sole carbon source, and both hexameric and dimeric enzymes were produced irrespective of whether propionate... (More)
- Two separate citrate synthases from the extremely thermophilic bacterium Rhodothermus marinus have been identified and purified. One of the enzymes is a hexameric protein and is the first thermostable, hexameric citrate synthase to be isolated. The other is a dimeric enzyme, which is also thermostable but possesses both citrate synthase and 2-methyl citrate synthase activities. 2-Methyl citrate synthase uses propionyl-coenzyme A as one of its substrates and in Escherichia coli, for example, it has been implicated in the metabolism of propionate. However, no growth of R. marinus was observed using minimal medium with propionate as the sole carbon source, and both hexameric and dimeric enzymes were produced irrespective of whether propionate was included in the growth medium. The data are discussed with respect to the evolutionary relationships between the known hexameric and dimeric citrate synthases and 2-methyl citrate synthase. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/106345
- author
- Nordberg Karlsson, Eva
LU
; Abou-Hachem, Maher
LU
; Holst, Olle
LU
; Danson, Michael J
and Hough, David W
- organization
- publishing date
- 2002
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Extremophiles
- volume
- 6
- issue
- 1
- pages
- 51 - 56
- publisher
- Springer
- external identifiers
-
- wos:000173961500007
- scopus:0036483839
- ISSN
- 1433-4909
- DOI
- 10.1007/s007920100226
- language
- English
- LU publication?
- yes
- id
- 1c37f2a5-20b3-4e2a-a528-6da43ce290ab (old id 106345)
- date added to LUP
- 2016-04-01 12:13:54
- date last changed
- 2022-01-27 00:44:12
@article{1c37f2a5-20b3-4e2a-a528-6da43ce290ab,
abstract = {{Two separate citrate synthases from the extremely thermophilic bacterium Rhodothermus marinus have been identified and purified. One of the enzymes is a hexameric protein and is the first thermostable, hexameric citrate synthase to be isolated. The other is a dimeric enzyme, which is also thermostable but possesses both citrate synthase and 2-methyl citrate synthase activities. 2-Methyl citrate synthase uses propionyl-coenzyme A as one of its substrates and in Escherichia coli, for example, it has been implicated in the metabolism of propionate. However, no growth of R. marinus was observed using minimal medium with propionate as the sole carbon source, and both hexameric and dimeric enzymes were produced irrespective of whether propionate was included in the growth medium. The data are discussed with respect to the evolutionary relationships between the known hexameric and dimeric citrate synthases and 2-methyl citrate synthase.}},
author = {{Nordberg Karlsson, Eva and Abou-Hachem, Maher and Holst, Olle and Danson, Michael J and Hough, David W}},
issn = {{1433-4909}},
language = {{eng}},
number = {{1}},
pages = {{51--56}},
publisher = {{Springer}},
series = {{Extremophiles}},
title = {{Rhodothermus marinus: a thermophilic bacterium producing dimeric and hexameric citrate synthase isoenzymes.}},
url = {{http://dx.doi.org/10.1007/s007920100226}},
doi = {{10.1007/s007920100226}},
volume = {{6}},
year = {{2002}},
}