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Literature summary for 2.7.4.3 extracted from

  • Wang, Y.; Makowski, L.
    Fine structure of conformational ensembles in adenylate kinase (2018), Proteins, 86, 332-343 .
    View publication on PubMed
Search for more literature for 2.7.4.3

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on Mg2+ Escherichia coli

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 enzyme has 3 domains, the LID, NMP, and CORE domains, that undergo large conformational rearrangements during catalytic cycle of adenylate kinase. The pathway from open to closed forms is explored using coarse-grained molecular dynamics trajectories of adenosine kinase calculated by GROMACS using a SMOG model and classify the conformations within the resultant trajectories by K-means clustering Escherichia coli 2 ADP
-
 ?
ATP + AMP
-
 Escherichia coli K12 2 ADP
-
 ?
ATP + AMP the enzyme has 3 domains, the LID, NMP, and CORE domains, that undergo large conformational rearrangements during catalytic cycle of adenylate kinase. The pathway from open to closed forms is explored using coarse-grained molecular dynamics trajectories of adenosine kinase calculated by GROMACS using a SMOG model and classify the conformations within the resultant trajectories by K-means clustering Escherichia coli K12 2 ADP
-
 ?

General Information

General Information Comment Organism
physiological function the reaction is a major player in cellular energy homeostasis and the isoform network of adenylate kinase plays an important role in AMP metabolic signaling circuits Escherichia coli