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Literature summary for 2.7.4.3 extracted from

  • Wang, Y.; Gan, L.; Wang, E.; Wang, J.
    Exploring the dynamic functional landscape of adenylate kinase modulated by substrates (2013), J. Chem. Theory Comput., 9, 84-95.
    View publication on PubMed
Search for more literature for 2.7.4.3

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli
Mg2+ required Homo sapiens
Mg2+ required Saccharomyces cerevisiae
Mg2+ required Geobacillus stearothermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + AMP Escherichia coli
-
 2 ADP
-
 r
ATP + AMP Homo sapiens
-
 2 ADP
-
 r
ATP + AMP Saccharomyces cerevisiae
-
 2 ADP
-
 r
ATP + AMP Geobacillus stearothermophilus
-
 2 ADP
-
 r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Geobacillus stearothermophilus
-
-
-
Homo sapiens
-
-
-
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + AMP = 2 ADP induced-fit and change between open and closed conformation, random Bi-Bi reaction mechanism, the conformational change of the ADK enzyme very much follows two parallel stepwise pathways as a functional requirement for the double substrate catalysis Escherichia coli
a
ATP + AMP = 2 ADP induced-fit and change between open and closed conformation, random Bi-Bi reaction mechanism, the conformational change of the ADK enzyme very much follows two parallel stepwise pathways as a functional requirement for the double substrate catalysis Homo sapiens
a
ATP + AMP = 2 ADP induced-fit and change between open and closed conformation, random Bi-Bi reaction mechanism, the conformational change of the ADK enzyme very much follows two parallel stepwise pathways as a functional requirement for the double substrate catalysis Saccharomyces cerevisiae
a
ATP + AMP = 2 ADP induced-fit and change between open and closed conformation, random Bi-Bi reaction mechanism, the conformational change of the ADK enzyme very much follows two parallel stepwise pathways as a functional requirement for the double substrate catalysis Geobacillus stearothermophilus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + AMP
-
 Escherichia coli 2 ADP
-
 r
ATP + AMP
-
 Homo sapiens 2 ADP
-
 r
ATP + AMP
-
 Saccharomyces cerevisiae 2 ADP
-
 r
ATP + AMP
-
 Geobacillus stearothermophilus 2 ADP
-
 r
ATP + AMP substrate ligand-binding modeling, detailed overview Escherichia coli 2 ADP
-
 r
ATP + AMP substrate ligand-binding modeling, detailed overview Homo sapiens 2 ADP
-
 r
ATP + AMP substrate ligand-binding modeling, detailed overview Saccharomyces cerevisiae 2 ADP
-
 r
ATP + AMP substrate ligand-binding modeling, detailed overview Geobacillus stearothermophilus 2 ADP
-
 r

Synonyms

Synonyms Comment Organism
ADK
-
 Escherichia coli
ADK
-
 Homo sapiens
ADK
-
 Saccharomyces cerevisiae
ADK
-
 Geobacillus stearothermophilus

General Information

General Information Comment Organism
additional information enzyme adenylate kinase dynamics-function relationships, modelling using crystal structure PDB ID 1ANK, comparisons of different enzyme structures and substrate binding structures, detailed overview Escherichia coli
additional information enzyme adenylate kinase dynamics-function relationships, modelling using crystal structure PDB ID 1DVR, comparisons of different enzyme structures and substrate binding structures, detailed overview Saccharomyces cerevisiae
additional information enzyme adenylate kinase dynamics-function relationships, modelling using crystal structure PDB ID 1ZIN, comparisons of different enzyme structures and substrate binding structures, detailed overview Geobacillus stearothermophilus
additional information enzyme adenylate kinase dynamics-function relationships, modelling using crystal structure PDB ID 2BBW, comparisons of different enzyme structures and substrate binding structures, detailed overview Homo sapiens