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  Mutations in the nucleotide binding loop of adenylate kinase of Escherichia coli

Reinstein, J., Brune, M., & Wittinghofer, A. (1988). Mutations in the nucleotide binding loop of adenylate kinase of Escherichia coli. Biochemistry, 27(13), 4712-4720. doi:10.1021/bi00413a020.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-AE18-C Version Permalink: http://hdl.handle.net/21.11116/0000-0002-6A50-D
Genre: Journal Article

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 Creators:
Reinstein, Jochen1, Author              
Brune, Martin, Author
Wittinghofer, Alfred2, Author              
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: The adk gene of Escherichia coli has been used to overexpress the adenylate kinase protein in two ways: (1) by cloning the adk gene with its own promoter into pEMBL plasmids, which have an increased copy number, and (2) by deleting the adk promoter and cloning the gene behind the regulatable tac promoter. Adenylate kinase comprises up to 40% of the soluble cellular extracts from E. coli strains containing these plasmids. Mutations have been introduced into the gene by site-directed mutagenesis to exchange amino acids in the nucleotide binding loop, which is highly conserved in many mononucleotide binding proteins. The mutation of Lys13----Gln is nearly inactive, whereas the Pro9----Leu and the Gly10----Val mutant proteins have an increased Km for both substrates and a Vmax that is similar to wild type. Proton NMR measurements of the proteins show that a major structural change seems to have taken place for the Pro9----Leu and Gly10----Val mutants. The results are discussed in the light of the kinetic mechanism for adenylate kinase and the three-dimensional structure of the protein.

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Language(s): eng - English
 Dates: 1988-01-041988-02-231988-06
 Publication Status: Published in print
 Pages: 9
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 Table of Contents: -
 Rev. Type: Peer
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Title: Biochemistry
Source Genre: Journal
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Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 27 (13) Sequence Number: - Start / End Page: 4712 - 4720 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103