Function and engineering of the 15beta-hydroxylase CYP106A2.
CYP106A2 from Bacillus megaterium ATCC 13368 is a bacterial cytochrome P450 that is capable of transforming steroid hormones. It can be easily expressed in Escherichia coli with a high yield. Its activity in vitro can be achieved by using the adrenal redox proteins adrenodoxin and adrenodoxin reductase. So far, it was not possible to crystallize CYP106A2 because of degradation during the crystallization process. Nevertheless, CYP106A2 is an interesting enzyme for biotechnological use. It hydroxylates pharmaceutically important steroids such as progesterone and 11-deoxycortisol. However, it will be necessary for efficient application of CYP106A2 in biotechnology to improve the hydroxylation activity and manipulate the regiospecificity. The present paper gives an overview of recent developments in protein engineering of CYP106A2.
Virus
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Naturwissenschaftlich-Technische Fakultät III, Institut für Biochemie, Universität des Saarlandes, Postfach 151150, 66041 Saarbrücken, Germany.
Lisurek
M
M
Simgen
B
B
Hannemann
F
F
Bernhardt
R
R
D001410:Bacillus megaterium / Q000201:enzymology / Q000235:genetics*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D003460:Crystallization; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D004795:Enzyme Stability; D019143:Evolution, Molecular; D005818:Genetic Engineering; D007700:Kinetics; D008958:Models, Molecular; D011487:Protein Conformation
D001426:Bacterial Proteins; D003577:Cytochrome P-450 Enzyme System; C517094:15beta-hydroxylase CYP106A2, Bacillus megaterium