Linked Life Data

4019499

Source:http://linkedlifedata.com/resource/pubmed/id/4019499

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
1985-9-25
pubmed:abstractText
Mannitol-1-phosphate dehydrogenase (EC 1.1.1.17) has been purified from Aspergillus parasiticus, a filamentous fungus which produces the polyketide mycotoxin, versicolorin A. Its kinetic properties have been compared with those of mannitol-1-phosphate dehydrogenase from the related non-toxin-producing fungus, A. niger. Both enzymes are inhibited by divalent transition metals, especially Zn2+ and Cd2+, but only the enzyme from A. parasiticus exhibits inhibitor-induced cooperative binding of the substrate, fructose-6 phosphate. Double reciprocal plots (1/v versus 1/Fru-6-P) are linear in the absence of Zn2+ but in the presence of Zn2+ are concave upward, with Hill coefficients of 1.5. The extent of cooperativity is inversely related to ionic strength, disappearing at 100 mM KCl. The enzymes from both organisms are relatively stable to incubation at 30 degrees C, but only the enzyme from A. parasiticus is rendered thermally unstable by the addition of divalent transition metals. A model is proposed to explain how binding of transition metal ions affects substrate binding and thermal stability of the enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
260
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10019-22
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Zn2+-induced cooperativity of mannitol-1-phosphate dehydrogenase from Aspergillus parasiticus.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't