Linked Life Data

6285983

Source:http://linkedlifedata.com/resource/pubmed/id/6285983

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1982-10-12
pubmed:abstractText
1. Treatment of prolyl 4-hydroxylase (prolyl-glycyl-peptide, 2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating), EC 1.14.11.2) with 2-oxoglutarate in the absence of added Fe2+ for 10 s causes partial inactivation of the enzyme which is not reversed by subsequent addition of Fe2+. It appears that 2-oxoglutarate prevents loss of enzyme-bound iron and prevents access of added iron to its binding site. 2. For optimal enzyme activity the enzyme should be preincubated for 15 s with Fe2+ (5 microM). 3. Under turnover conditions prolyl 4-hydroxylase does not release iron. 4. The inactivation brought about by pre-incubation with 2-oxoglutarate and O2 in the absence of ascorbate is partly reversed by removal of 2-oxoglutarate. 5. It is proposed that dead-end complex formation with 2-oxoglutarate is responsible for the inactivation of the enzyme by 2-oxoglutarate in the absence of either ascorbate or Fe2+. 6. Optimal enzyme activity is obtained if the reactants are added to the reaction medium in the following order: enzyme, iron and ascorbate in any order, then after at least 15 s 2-oxoglutarate and finally (Pro-Pro-Gly)5 to start the reaction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
704
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
321-5
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
The influence of 2-oxoglutarate on the activity of prolyl 4-hydroxylase.
pubmed:publicationType
Journal Article