Hydroxylation of oleanolic acid to queretaroic acid by cytochrome P450 from Nonomuraea recticatena.
A gene for cytochrome P450 (moxA) from Nonomuraea recticatena, coexpressed with camAB for pseudomonad redox partners in Escherichia coli, hydroxylated oleanolic acid to produce queretaroic acid. When we used the P450-induced whole-cell as a catalyst, only a small amount of queretaroic acid was produced, probably due to poor permeability of oleanolic acid into the E. coli cell. In an alternative approach with the cell-free reaction system, the conversion ratio increased up to 17%.
Fujii
Yoshikazu
Y
Bioresource Laboratories, Mercian Corp., Iwata-shi, Shizuoka, Japan. fujii-ysk@mercian.co.jp
Hirosue
Shinji
S
Fujii
Tadashi
T
Matsumoto
Naoki
N
Agematu
Hitosi
H
Arisawa
Akira
A
D039903:Actinobacteria / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D002474:Cell-Free System; D003577:Cytochrome P-450 Enzyme System / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D006900:Hydroxylation; D007218:Industrial Microbiology / Q000379:methods*; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D009828:Oleanolic Acid / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D021241:Spectrometry, Mass, Electrospray Ionization
D011994:Recombinant Proteins; D009828:Oleanolic Acid; D003577:Cytochrome P-450 Enzyme System