title: The substrate binding cavity of particulate methane monooxygenase from Methylosinus trichosporium OB3b expresses high enantioselectivity for n-butane and n-pentane oxidation to 2-alcohol.
abstract: The particulate methane monooxygenase (pMMO) of Methylosinus trichosporium OB3b oxidized n-butane and n-pentane and mainly produced (R)-2-butanol and (R)-2-pentanol that comprised 78 and 89% of the product, respectively, indicating that the pro-R hydrogen of the 2-position carbon of n-butane and n-pentane is oriented toward a catalytic site within the substrate binding site of pMMO. The protein cavity adjacent to the catalytic center for pMMO has optimum volume for recognizing n-butane and n-pentane for enantioselective hydroxylation.
authors: Department of Environmental Chemistry and Engineering, Tokyo Institute of Technology, Midori-ku, Yokohama, Japan. akimiyaji@chemenv.titech.ac.jp
authors: Akimitsu
authors: A
authors: Miyaji
authors: Teppei
authors: T
authors: Miyoshi
authors: Ken
authors: K
authors: Motokura
authors: Toshihide
authors: T
authors: Baba
mesh_terms: D002073:Butanes / Q000378:metabolism*; D000440:Butanols / Q000378:metabolism*; D020134:Catalytic Domain; D020602:Methylosinus trichosporium / Q000201:enzymology*; D010084:Oxidation-Reduction; D010105:Oxygenases / Q000737:chemistry* / Q000378:metabolism*; D010420:Pentanes / Q000378:metabolism*; D000439:Pentanols / Q000378:metabolism*; D011487:Protein Conformation; D013237:Stereoisomerism; D013379:Substrate Specificity
chemical_list: D002073:Butanes; D000440:Butanols; D010420:Pentanes; D000439:Pentanols; C043958:2-butanol; C033353:pentane; C046888:butane; D010105:Oxygenases; C021555:methane monooxygenase