Linked Life Data

4041238

Source:http://linkedlifedata.com/resource/pubmed/id/4041238

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1985-11-6
pubmed:abstractText
Juglone-induced cells of Pseudomonas putida J 1 were shown to contain two isofunctional juglone hydroxylases. Both enzymes were purified about 125-fold to homogeneity in polyacrylamide gel electrophoresis. The molecular masses of the native enzymes, as determined by Sephacryl S-200 gel filtration were 59 000 Da for enzyme 1 and 56 000 Da for enzyme 2. The molecular masses of the subunits were determined by dodecyl sulfate polyacrylamide gel electrophoresis as 25 000 Da (enzyme 1) and 23 500 Da (enzyme 2). Both enzymes hydroxylated juglone, naphthazarin, 1,4-naphthoquinone and 2-chloro-1,4-naphthoquinone, but they were completely inactive against naphtholes. The activity of both hydroxylases was not affected by chelating agents, thiol reagents, however, were found to be strong inhibitors. No external cofactors such as Fe2, NADH, NADPH, FAD, FMN were required for activity. Concomitant with the hydroxylation of juglone the consumption of oxygen in a molar ratio 2: 1 (juglone: oxygen) was observed but none of the enzymes incorporated 18O2 into the substrate juglone. By activity staining enzyme 1 was found to be present in induced and non-induced cells of P. putida J 1, enzyme 2, however, only in juglone-induced cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0177-3593
pubmed:author
pubmed:issnType
Print
pubmed:volume
366
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
637-46
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Purification and some properties of two isofunctional juglone hydroxylases from Pseudomonas putida J1.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't