Linked Life Data

7408851

Source:http://linkedlifedata.com/resource/pubmed/id/7408851

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1980-11-25
pubmed:abstractText
The fructose-1,6-biphosphate aldolase (EC 4.1.2.13) from Staphylococcus aureus ATCC 12 600 was purified and biochemically investigated. It was found that this aldolase belongs to the class I type of aldolases since the fructose-1,6-bisphosphate cleavage activity was insensitivity to high levels of EDTA. Like class I aldolases of higher organisms, the S. aureus aldolase activity is inhibited on incubation with the substrate dihydroxyacetone-phosphate in the presence of NaBH4. Furthermore, the aldolase activity is not stimulated by monovalent or divalent cations. This enzyme exhibits an extreme stability to high temperature, acid and base. The purified enzyme is not activated after heating at 97 degrees C for 1.6 h. An incubation at 130 degrees C for 10 min is necessary to destroy irreversibly the activity of the aldolase. The optimal temperature for activity, however, is 37 degrees C. It is a monomer with a molecular weight of about 33,000 and exhibits a relatively broad pH optimum ranging over pH 7.5-9.0. Apart from fructose 1,6-bisphosphate as substrate (Km = 0.045 mM), this aldolase also revealed activity with fructose 1-phosphate (Km = 25 mM). The pH of the isoelectric point lies between 3.95 and 4.25.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
108
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
295-301
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Purification and characterisation of an unusually heat-stable and acid/base-stable class I fructose-1,6-bisphosphate aldolase from Staphylococcus aureus.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't