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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)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Extremophiles
volume
6
issue
1
pages
51 - 56
publisher
Springer
external identifiers
  • wos:000173961500007
  • scopus:27144542431
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
2007-07-02 15:44:43
date last changed
2017-01-01 04:57:33
@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},
  volume       = {6},
  year         = {2002},
}