Linked Life Data

1917897

Source:http://linkedlifedata.com/resource/pubmed/id/1917897

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1991-10-31
pubmed:abstractText
Two distinct types of fumarase were purified to homogeneity from aerobically grown Escherichia coli W cells. The amino acid sequences of their NH2-terminals suggest that the two enzymes are the products of the fumA gene (FUMA) and fumC gene (FUMC), respectively. FUMA was separated from FUMC by chromatography on a Q-Sepharose column, and was further purified to homogeneity on Alkyl-Superose, Mono Q, and Superose 12 columns. FUMA is a dimer composed of identical subunits (Mr = 60,000). Although the activity of FUMA rapidly decreased during storage, reactivation was attained by anaerobic incubation with Fe2+ and thiols. Studies on the inactivation and reactivation of FUMA suggested that oxidation and the concomitant release of iron inactivated the enzyme in a reversible manner. While the inactivated FUMA was EPR-detectable, through a signal with g perpendicular = 2.02 and g = 2.00, the active enzyme was EPR-silent. These results suggested FUMA is a member of the 4Fe-4S hydratases represented by aconitase. After the separation of FUMC from FUMA, purification of the former enzyme was accomplished by chromatography on Phenyl-Superose and Matrex Gel Red A columns. FUMC was stable, Fe-independent and quite similar to mammalian fumarases in enzymatic properties.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
109
pubmed:geneSymbol
fumA, fumC
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
728-33
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Purification and characterization of two types of fumarase from Escherichia coli.
pubmed:affiliation
Department of Chemistry, Faculty of Science, Kyoto University.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't