OVERPRODUCTION AND SUBSTRATE-SPECIFICITY OF 3-ISOPROPYLMALATE DEHYDROGENASE FROM THIOBACILLUS-FERROOXIDANS

Authors
MATSUNAMI H KAWAGUCHI H INAGAKI K EGUCHI T KAKINUMA K TANAKA H
Citation
H. Matsunami et al., OVERPRODUCTION AND SUBSTRATE-SPECIFICITY OF 3-ISOPROPYLMALATE DEHYDROGENASE FROM THIOBACILLUS-FERROOXIDANS, Bioscience, biotechnology, and biochemistry, 62(2), 1998, pp. 372-373
Citations number
22
Categorie Soggetti
Biology,Agriculture,"Biothechnology & Applied Migrobiology","Food Science & Tenology
Journal title
Bioscience, biotechnology, and biochemistry → ACNP
ISSN journal
09168451
Volume
62
Issue
2
Year of publication
1998
Pages
372 - 373
Database
ISI
SICI code
0916-8451(1998)62:2<372:OASO3D>2.0.ZU;2-3
Abstract
We constructed an overexpression system in Escherichia coli of the leu B gene coding for 3-isopropylmalate dehydrogenase in Thiobacillus ferr ooxidans. E. coli harboring the plasmid we constructed, pKK leuB1, pro duced 17-fold the enzyme protein of the expression system previously u sed for purification. The substrate specificity of the enzyme was anal yzed with synthetic (2R, 3S)-3-alkylmalates. The 3-isopropylmalate deh ydrogenase of Thiobacillus ferrooxidans had broad specificity toward t he alkylmalates.