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Literature summary for 2.7.4.3 extracted from

  • Strupat, K.; Sagi, D.M.; Bönisch, H.; Schäfer, G.; Peter-Katalinic, J.
    Oligomerization and substrate binding studies of the adenylate kinase from Sulfolobus acidocaldarius by matrix-assisted laser desorption/ionization mass spectrometry (2000), Analyst, 125, 563-567.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Sulfolobus acidocaldarius

Organism

Organism UniProt Comment Textmining
Sulfolobus acidocaldarius P35028
-
-
Sulfolobus acidocaldarius DSM 639 P35028
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + AMP
-
Sulfolobus acidocaldarius 2 ADP
-
r
ATP + AMP
-
Sulfolobus acidocaldarius DSM 639 2 ADP
-
r

Subunits

Subunits Comment Organism
More investigation of the oligomerization behaviour of the recombinant enzyme. The preferred native form of the adenylate kinase is a homotrimer, whose existence is detected by a specific MALDI-MS strategy, correlating with the published results on adenylate oligomerization using X-ray structure analysis Sulfolobus acidocaldarius

Cofactor

Cofactor Comment Organism Structure
ADP the adenylate kinase protein preparation contains non-covalently bound ADP Sulfolobus acidocaldarius