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Literature summary for 2.7.4.3 extracted from

  • Onuk, E.; Badger, J.; Wang, Y.J.; Bardhan, J.; Chishti, Y.; Akcakaya, M.; Brooks, D.H.; Erdogmus, D.; Minh, D.D.L.; Makowski, L.
    Effects of catalytic action and ligand binding on conformational ensembles of adenylate kinase (2017), Biochemistry, 56, 4559-4567 .
    View publication on PubMed
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + AMP Escherichia coli
-
 2 ADP
-
 ?
ATP + AMP Escherichia coli K12
-
 2 ADP
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli P69441
-
-
Escherichia coli K12 P69441
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + AMP
-
 Escherichia coli 2 ADP
-
 ?
ATP + AMP the results of the study are more consistent with proposals that adenylate kinase belongs to a group of enzymes in which substrate binding is the predominant mechanism for driving the protein into a catalytically active state, rather than the population-shift model Escherichia coli 2 ADP
-
 ?
ATP + AMP
-
 Escherichia coli K12 2 ADP
-
 ?
ATP + AMP the results of the study are more consistent with proposals that adenylate kinase belongs to a group of enzymes in which substrate binding is the predominant mechanism for driving the protein into a catalytically active state, rather than the population-shift model Escherichia coli K12 2 ADP
-
 ?