Linked Life Data

2124611

Source:http://linkedlifedata.com/resource/pubmed/id/2124611

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1991-2-7
pubmed:abstractText
Fumarate hydratase (EC 4.2.1.2) from the extremely thermophilic archaeobacterium Solfolobus solfataricus has been purified to homogeneity by a rapid purification procedure using affinity chromatography and high-performance size-exclusion chromatography, and the enzyme's physical and biochemical properties have been determined. The native enzyme has a molecular mass of 170 kDa and is composed of identical subunits with a molecular mass of 45 kDa, thus indicating a tetrameric structure similar to fumarases isolated from other organisms. The enzyme was active at temperatures ranging from 40 degrees C to 90 degrees C, with a maximum activity at 85 degrees C. The pH optimum for generation of fumarate was found to be pH 8.0. The enzyme showed high stability to denaturation by heat and organic solvents.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-1287
pubmed:author
pubmed:issnType
Print
pubmed:volume
136
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1537-41
pubmed:dateRevised
2005-1-21
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Purification and properties of a thermostable fumarate hydratase from the archaeobacterium Sulfolobus solfataricus.
pubmed:affiliation
Institut für Mikrobiologie (Medizinische Fakultät), Universität Innsbruck, Austria.
pubmed:publicationType
Journal Article