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  Structural and catalytic role of arginine 88 in Escherichia coli adenylate kinase as evidenced by chemical modification and site-directed mutagenesis

Reinstein, J., Gilles, A., Rose, T., Wittinghofer, A., Saint−Girons, I., Barzu, O., et al. (1989). Structural and catalytic role of arginine 88 in Escherichia coli adenylate kinase as evidenced by chemical modification and site-directed mutagenesis. The Journal of Biological Chemistry, 264(14), 8107-8112. Retrieved from https://www.ncbi.nlm.nih.gov/labs/articles/2542263/.

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 Creators:
Reinstein, Jochen1, 2, Author              
Gilles, Anne−Marie, Author
Rose, Thierry, Author
Wittinghofer, Alfred3, Author              
Saint−Girons, Isabelle, Author
Barzu, Octavian, Author
Surewicz, Witold K., Author
Mantsch, Henry H., Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Molecular chaperones, Max Planck Institute for Medical Research, Max Planck Society, ou_1497728              
3Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: Phenylglyoxal inactivates Escherichia coli adenylate kinase by modifying a single arginine residue (Arg-88). ATP, ADP, P1,P5-di(adenosine 5')-pentaphosphate, and to a lesser extent AMP protect the enzyme against inactivation by phenylglyoxal. Site-directed mutagenesis of Arg-88 to glycine yields a modified form of adenylate kinase (RG88 mutant) closely related structurally to the wild-type protein as indicated by Fourier transform infrared spectroscopy, differential scanning calorimetry, and limited proteolysis. However, this modified protein has only 1% of the maximum catalytic activity of the wild-type enzyme and 5- and 85-fold higher apparent Km values for ATP and AMP, respectively, than the parent adenylate kinase. Arg-88, which is a highly conserved residue in all known molecular forms of adenylate kinases (corresponding to Arg-97 in muscle cytosolic enzyme), should be located inside a big cleft of the molecule, close to the phosphate-binding loop. It possibly stabilizes the transferable gamma-phosphate group from ATP to AMP in the transition state.

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Language(s): eng - English
 Dates: 1988-09-161989-05-15
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 264 (14) Sequence Number: - Start / End Page: 8107 - 8112 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1