title: Structural and biochemical analyses of YvgN and YtbE from Bacillus subtilis.
abstract: Bacillus subtilis is one of the most studied gram-positive bacteria. In this work, YvgN and YtbE from B. subtilis, assigned as AKR5G1 and AKR5G2 of aldo-keto reductase (AKR) superfamily. AKR catalyzes the NADPH-dependent reduction of aldehyde or aldose substrates to alcohols. YvgN and YtbE were studied by crystallographic and enzymatic analyses. The apo structures of these proteins were determined by molecular replacement, and the structure of holoenzyme YvgN with NADPH was also solved, revealing the conformational changes upon cofactor binding. Our biochemical data suggest both YvgN and YtbE have preferential specificity for derivatives of benzaldehyde, such as nitryl or halogen group substitution at the 2 or 4 positions. These proteins also showed broad catalytic activity on many standard substrates of AKR, such as glyoxal, dihydroxyacetone, and DL-glyceraldehyde, suggesting a possible role in bacterial detoxification.
authors: National laboratory of Protein Engineering and Plant Genetic Engineering, College of Life Sciences, Peking University, Beijing 100871, China.
authors: Jian
authors: J
authors: Lei
authors: Yan-Feng
authors: YF
authors: Zhou
authors: Lan-Fen
authors: LF
authors: Li
authors: Xiao-Dong
authors: XD
authors: Su
mesh_terms: D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D000449:Aldehyde Reductase; D000074408:Aldo-Keto Reductases; D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism; D018360:Crystallography, X-Ray; D004098:Dihydroxyacetone / Q000378:metabolism; D005985:Glyceraldehyde / Q000378:metabolism; D006037:Glyoxal / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D016415:Sequence Alignment
chemical_list: D005985:Glyceraldehyde; D006037:Glyoxal; D000429:Alcohol Oxidoreductases; D000074408:Aldo-Keto Reductases; D000449:Aldehyde Reductase; D004098:Dihydroxyacetone