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Residues Around the Catalytic Pocket of DdsA Are Important for Isoprenoids Chain Elongation

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Nineteen mutants of decaprenyl diphosphate synthase from Gluconobacter suboxydans were generated and their production of ubiquinones (UQs) was compared to that of the wild type protein. The accessible surface area and the polarity of amino acid around the catalytic pocket wield remarkable influences on the isoprenoid chain elongation of UQs.

Keywords: Decaprenyl diphosphate synthase; site-directed mutagenesis; ubiquinone

Document Type: Research Article


Affiliations: State Key Laboratory of Bioreactor Engineering, Mailbox 431, East China University of Science and Technology, Shanghai 200237, China.

Publication date: January 1, 2007

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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