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PDBsum entry 3b3d
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Oxidoreductase
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PDB id
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3b3d
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References listed in PDB file
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Key reference
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Title
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Structural and biochemical analyses of yvgn and ytbe from bacillus subtilis.
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Authors
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J.Lei,
Y.F.Zhou,
L.F.Li,
X.D.Su.
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Ref.
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Protein Sci, 2009,
18,
1792-1800.
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PubMed id
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Abstract
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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.
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