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Structural insight into the stereoselective production of PGF2α by Old Yellow Enzyme from Trypanosoma cruzi.

Authors :
Okamoto, Naoki
Yamaguchi, Keishi
Mizohata, Eiichi
Tokuoka, Keiji
Uchiyama, Nahoko
Sugiyama, Shigeru
Matsumura, Hiroyoshi
Inaka, Koji
Urade, Yoshihiro
Inoue, Tsuyoshi
Source :
Journal of Biochemistry. Nov2011, Vol. 150 Issue 5, p563-568. 6p.
Publication Year :
2011

Abstract

Old yellow enzyme (OYE) is an NADPH oxidoreductase capable of reducing a variety of compounds. It contains flavin mononucleotide (FMN) as a prosthetic group. A ternary complex structure of OYE from Trypanosoma cruzi (TcOYE) with FMN and one of the substrates, p-hydroxybenzaldehyde, shows a striking movement around the active site upon binding of the substrate. From a structural comparison of other OYE complexed with 12-oxophytodienoate, we have constructed a complex structure with another substrate, prostaglandin H2 (PGH2), to provide a proposed stereoselective reaction mechanism for the reduction of PGH2 to prostaglandin F2α by TcOYE. [ABSTRACT FROM PUBLISHER]

Details

Language :
English
ISSN :
0021924X
Volume :
150
Issue :
5
Database :
Academic Search Index
Journal :
Journal of Biochemistry
Publication Type :
Academic Journal
Accession number :
67007519
Full Text :
https://doi.org/10.1093/jb/mvr096