Linked Life Data

9760270

Source:http://linkedlifedata.com/resource/pubmed/id/9760270

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
40
pubmed:dateCreated
1998-11-4
pubmed:abstractText
In this report recombinant estrogen binding protein (EBP1), isolated originally from Candida albicans as a result of its high affinity for 17beta-estradiol, has been purified extensively using a modified affinity purification scheme originally developed for a homolog of EBP1, old yellow enzyme (OYE). It is shown that like OYE, the protein binds a variety of compounds with a phenolic structure, including 17beta-estradiol, and compounds with an alpha, beta-unsaturated keto or aldehyde structure. In addition, EBP1 exhibits an NADPH oxidoreductase activity, transferring electrons from NADPH to all alpha,beta-unsaturated ketones and aldehydes tested via the tightly bound FMN cofactor. Analysis of the steady-state kinetics of these reactions indicate a tetra uni ping-pong mechanism. Inhibition of the steady-state reaction by 17beta-estradiol gives a Ki = 10 +/- 2 nM, and indicates exclusive binding of this steroid to the enzyme in its oxidized state. In contrast, 19-nortestosterone binds to both oxidized and reduced forms of the enzyme with dissociation constants of 600 +/- 100 and 650 +/- 90 nM, respectively. EBP1 also catalyzes a disproportionation reaction with certain compounds, in which two molecules of a cylic alpha,beta-unsaturated ketone, including the steroid 19-nortestosterone, are individually aromatized and reduced to the corresponding saturated ketone. Despite the extensive similarity in sequence and enzymic activity, notable differences between EBP1 and the OYE family of proteins exist with regard to the binding behavior and reactivity with the two steroids tested here, estradiol and 19-nortestosterone.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14326-36
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Binding and reactivity of Candida albicans estrogen binding protein with steroid and other substrates.
pubmed:affiliation
Department of Pharmaceutical Chemistry, University of California, San Francisco 94143-0446, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't