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• W1979684402 abstract "An aprE mutant from B. subtilis 168 lacking the connecting loop<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:msub><mml:mtext>Leu</mml:mtext><mml:mrow><mml:mn>75</mml:mn></mml:mrow></mml:msub><mml:mtext>–</mml:mtext><mml:msub><mml:mtext>Leu</mml:mtext><mml:mrow><mml:mn>82</mml:mn></mml:mrow></mml:msub></mml:math>which is predicted to encode a<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:msup><mml:mtext>Ca</mml:mtext><mml:mrow><mml:mn>2</mml:mn><mml:mo>+</mml:mo></mml:mrow></mml:msup></mml:math>binding site was constructed. Expression of the mutant gene ( aprE <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>Δ</mml:mi><mml:mi>L</mml:mi><mml:mi>e</mml:mi><mml:msub><mml:mi>u</mml:mi><mml:mrow><mml:mn>75</mml:mn></mml:mrow></mml:msub><mml:mtext>–</mml:mtext><mml:mi>L</mml:mi><mml:mi>e</mml:mi><mml:msub><mml:mi>u</mml:mi><mml:mrow><mml:mn>82</mml:mn></mml:mrow></mml:msub></mml:math>) produced B. subtilis colonies lacking protease activity. Intrinsic fluorescence analysis revealed spectral differences between wild-type AprE and AprE<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>Δ</mml:mi><mml:msub><mml:mtext>L</mml:mtext><mml:mrow><mml:mn>75</mml:mn></mml:mrow></mml:msub><mml:mtext>–</mml:mtext><mml:msub><mml:mtext>L</mml:mtext><mml:mrow><mml:mn>82</mml:mn></mml:mrow></mml:msub></mml:math>. An AprE<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>Δ</mml:mi><mml:msub><mml:mtext>L</mml:mtext><mml:mrow><mml:mn>75</mml:mn></mml:mrow></mml:msub><mml:mtext>–</mml:mtext><mml:msub><mml:mtext>L</mml:mtext><mml:mrow><mml:mn>82</mml:mn></mml:mrow></mml:msub></mml:math>variant with reestablished enzyme activity was selected by directed evolution. The novel mutations<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:msub><mml:mtext>Thr</mml:mtext><mml:mrow><mml:mn>66</mml:mn></mml:mrow></mml:msub></mml:math>Met/<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:msub><mml:mtext>Gly</mml:mtext><mml:mrow><mml:mn>102</mml:mn></mml:mrow></mml:msub></mml:math>Asp located in positions which are predicted to be important for catalytic activity were identified in this variant. Although these mutations restored hydrolysis, they had no effect with respect to thermal inactivation of AprE<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>Δ</mml:mi><mml:msub><mml:mtext>L</mml:mtext><mml:mrow><mml:mn>75</mml:mn></mml:mrow></mml:msub><mml:mtext>–</mml:mtext><mml:msub><mml:mtext>L</mml:mtext><mml:mrow><mml:mn>82</mml:mn></mml:mrow></mml:msub></mml:math> <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:msub><mml:mtext>T</mml:mtext><mml:mrow><mml:mtext>66</mml:mtext></mml:mrow></mml:msub><mml:mtext>M</mml:mtext></mml:math> <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:msub><mml:mtext>G</mml:mtext><mml:mrow><mml:mn>102</mml:mn></mml:mrow></mml:msub><mml:mtext>D</mml:mtext></mml:math>. These results support the proposal that in addition to function as a calcium binding site, the loop that connects<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>β</mml:mi></mml:math>-sheet e3 with<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mi>α</mml:mi></mml:math>-helix c plays a structural role on enzyme activity of AprE from B. subtilis 168." @default.
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• W1979684402 date "2009-01-01" @default.
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• W1979684402 title "Engineering and Directed Evolution of a Ca2+Binding Site A-Deficient AprE Mutant Reveal an Essential Contribution of the Loop Leu75–Leu82to Enzyme Activity" @default.
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• W1979684402 doi "https://doi.org/10.1155/2009/201075" @default.
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