|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
1
|
|
pubmed:dateCreated |
1997-9-18
|
|
pubmed:abstractText |
A thermostable l-malate dehydrogenase from the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus was isolated and characterized, and its gene was cloned and sequenced. The enzyme is a homodimer with a molecular mass of 70 kDa and catalyzes preferentially the reduction of oxaloacetic acid with NADH. A. fulgidus L-malate dehydrogenase was stable for 5 h at 90 degrees C, and the half-life at 101 degrees C was 80 min. Thus, A. fulgidus L-malate dehydrogenase is the most thermostable L-malate dehydrogenase characterized to date. Addition of K2HPO4 (1 M) increased the thermal stability by 40%. The primary structure shows a high similarity to L-lactate dehydrogenase from Thermotoga maritima and gram-positive bacteria, and to L-malate dehydrogenase from the archaeon Haloarcula marismortui and other L-lactate-dehydrogenase-like L-malate dehydrogenases.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jul
|
|
pubmed:issn |
0302-8933
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
168
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
59-67
|
|
pubmed:dateRevised |
2000-12-18
|
|
pubmed:meshHeading |
pubmed-meshheading:9211715-Amino Acid Sequence,
pubmed-meshheading:9211715-Archaea,
pubmed-meshheading:9211715-Base Sequence,
pubmed-meshheading:9211715-Cloning, Molecular,
pubmed-meshheading:9211715-Heating,
pubmed-meshheading:9211715-Malate Dehydrogenase,
pubmed-meshheading:9211715-Molecular Sequence Data,
pubmed-meshheading:9211715-NAD,
pubmed-meshheading:9211715-Oxaloacetates,
pubmed-meshheading:9211715-Oxaloacetic Acids,
pubmed-meshheading:9211715-Phosphates,
pubmed-meshheading:9211715-Phylogeny,
pubmed-meshheading:9211715-Potassium Compounds,
pubmed-meshheading:9211715-Sequence Alignment,
pubmed-meshheading:9211715-Sequence Analysis, DNA,
pubmed-meshheading:9211715-Sequence Homology, Amino Acid
|
|
pubmed:year |
1997
|
|
pubmed:articleTitle |
Properties and primary structure of a thermostable L-malate dehydrogenase from Archaeoglobus fulgidus.
|
|
pubmed:affiliation |
Department of Microbiology, University of Bergen, Jahnebakken 5, N-5020 Bergen, Norway.
|
|
pubmed:publicationType |
Journal Article
|
