Linked Life Data

10867710

Source:http://linkedlifedata.com/resource/pubmed/id/10867710

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-9-1
pubmed:abstractText
The macrophage migration inhibitory factor (MIF) is a cytokine that is structurally similar to certain isomerases and for which multiple immune and catalytic roles have been proposed. Different catalytic activities have been reported for MIF, yet the exact mechanism by which MIF acts is not completely known. As a tautomerase, the enzyme uses a general acid-base mechanism of proton transfer in which the amino-terminal proline has been shown to function as the catalytic base. We report the results of molecular docking simulations of macrophage migration inhibitory factor with three substrates, D-dopachrome, L-dopachrome methyl ester and p-(hydroxyphenyl)pyruvate. Electrostatic pK(a) predictions were also performed for the free and complexed forms of the enzyme. The predicted binding mode of p-(hydroxyphenyl)pyruvate is in agreement with the recently published X-ray structure. A model for the binding mode of D-dopachrome and L-dopachrome methyl ester to MIF is proposed which offers insights into the catalytic mechanism of D-dopachrome tautomerase activity of MIF. The proposed catalytic mechanism is further supported by the pK(a) predictions, which suggest that residue Lys32 acts as the general acid for the enzymatic catalysis of D-dopachrome.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0952-3499
pubmed:author
pubmed:copyrightInfo
Copyright 2000 John Wiley & Sons, Ltd.
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
146-56
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:articleTitle
Ionization state and molecular docking studies for the macrophage migration inhibitory factor: the role of lysine 32 in the catalytic mechanism.
pubmed:affiliation
Department of Biology and Biochemistry, University of Houston, TX 77204-5513, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't