De novo design of catalytic proteins.

by: J Kaplan, WF DeGrado

Proc Natl Acad Sci U S A, Vol. 101, No. 32. (10 August 2004), pp. 11566-11570.

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Abstract

The de novo design of catalytic proteins provides a stringent test of our understanding of enzyme function, while simultaneously laying the groundwork for the design of novel catalysts. Here we describe the design of an O(2)-dependent phenol oxidase whose structure, sequence, and activity are designed from first principles. The protein catalyzes the two-electron oxidation of 4-aminophenol (k(cat)/K(M) = 1,500 M(-1).min(-1)) to the corresponding quinone monoimine by using a diiron cofactor. The catalytic efficiency is sensitive to changes of the size of a methyl group in the protein, illustrating the specificity of the design.

@article{citeulike:571589, abstract = {The de novo design of catalytic proteins provides a stringent test of our understanding of enzyme function, while simultaneously laying the groundwork for the design of novel catalysts. Here we describe the design of an O(2)-dependent phenol oxidase whose structure, sequence, and activity are designed from first principles. The protein catalyzes the two-electron oxidation of 4-aminophenol (k(cat)/K(M) = 1,500 M(-1).min(-1)) to the corresponding quinone monoimine by using a diiron cofactor. The catalytic efficiency is sensitive to changes of the size of a methyl group in the protein, illustrating the specificity of the design.}, address = {Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6059, USA.}, author = {Kaplan, J. and DeGrado, W. F. }, citeulike-article-id = {571589}, doi = {10.1073/pnas.0404387101}, issn = {0027-8424}, journal = {Proc Natl Acad Sci U S A}, keywords = {design, enzyme, protein}, month = {August}, number = {32}, pages = {11566--11570}, posted-at = {2008-03-31 13:45:51}, priority = {4}, title = {De novo design of catalytic proteins.}, url = {http://dx.doi.org/10.1073/pnas.0404387101}, volume = {101}, year = {2004} }

RIS record

TY - JOUR ID - citeulike:571589 L3 - citeulike-article-id:571589 TI - De novo design of catalytic proteins. JF - Proc Natl Acad Sci U S A VL - 101 IS - 32 SP - 11566 EP - 11570 AD - Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104-6059, USA. SN - 0027-8424 N2 - The de novo design of catalytic proteins provides a stringent test of our understanding of enzyme function, while simultaneously laying the groundwork for the design of novel catalysts. Here we describe the design of an O(2)-dependent phenol oxidase whose structure, sequence, and activity are designed from first principles. The protein catalyzes the two-electron oxidation of 4-aminophenol (k(cat)/K(M) = 1,500 M(-1).min(-1)) to the corresponding quinone monoimine by using a diiron cofactor. The catalytic efficiency is sensitive to changes of the size of a methyl group in the protein, illustrating the specificity of the design. KW - design KW - enzyme KW - protein AU - Kaplan, J AU - DeGrado, WF PY - 2004/08/10/ UR - http://dx.doi.org/10.1073/pnas.0404387101 ER -

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