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J. Bacteriol., 06 1995, 2977-2981, Vol 177, No. 11
Copyright © 1995, American Society for Microbiology

The adenylate kinases from a mesophilic and three thermophilic methanogenic members of the Archaea

P Rusnak, P Haney and J Konisky
Department of Microbiology, University of Illinois, Urbana 61801, USA.

Adenylate kinase has been isolated from four related methanogenic members of the Archaea. For each, the optimum temperature for enzyme activity was similar to the temperature for optimal microbial growth and was approximately 30 degrees C for Methanococcus voltae, 70 degrees C for Methanococcus thermolithotrophicus, 80 degrees C for Methanococcus igneus, and 80 to 90 degrees C for Methanococcus jannaschii. The enzymes were sensitive to the adenylate kinase inhibitor P1, P5-di(adenosine-5')pentaphosphate, a property that was exploited to purify the enzymes by CIBACRON Blue affinity chromatography. The enzymes had an estimated molecular mass (approximately 23 to 25 kDa) in the range common for adenylate kinases. Each of the enzymes had a region of amino acid sequence close to its N terminus that was similar to the canonical P-loop sequence reported for all adenylate kinases. However, the methanogen sequences lacked a lysine residue that has previously been found to be invariant in adenylate kinases, including an enzyme isolated from the archaeon Sulfolobus acidocaldarius. If verified as a nucleotide-binding domain, the methanogen sequence would represent a novel nucleotide-binding motif. There was no correlation between amino acid abundance and the optimal temperature for enzyme activity.

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• Schafer, G., Engelhard, M., Muller, V. (1999). Bioenergetics of the Archaea. Microbiol. Mol. Biol. Rev. 63: 570-620 [Abstract] [Full Text]