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Probing the active site of L-aspartate oxidase by site-directed mutagenesis : role of basic residues in fumarate reduction

Authors :
Tedeschi, Gabriella
Ronchi, Severino
Simonic, Tatjana
Treu, Chiara
Mattevi, Andrea
Negri, Armando
Source :
Biochemistry. April 17, 2001, Vol. 40 Issue 15, p4738, 7 p.
Publication Year :
2001

Abstract

Site-directed mutagenesis of L-aspartate oxidase, which behaves as a fumarate reductase in anaerobic conditions, reveals that R386, H244, and H31 are involved in the fumarate binding and catalysis while R290 is involved only in the catalysis. Data show that L-aspartate active site is similar to that of fumarate reductase.

Details

ISSN :
00062960
Volume :
40
Issue :
15
Database :
Gale General OneFile
Journal :
Biochemistry
Publication Type :
Academic Journal
Accession number :
edsgcl.73635973