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Literature summary for 2.7.4.3 extracted from

  • Ye, C.; Ding, C.; Ma, R.; Wang, J.; Zhang, Z.
    Electrostatic interactions determine entrance/release order of substrates in the catalytic cycle of adenylate kinase (2019), Proteins, 87, 337-347 .
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + AMP Escherichia coli the enzyme is involved in regulating concentration of ATP in cells 2 ADP
-
?
ATP + AMP Escherichia coli K12 the enzyme is involved in regulating concentration of ATP in cells 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 the enzyme is involved in regulating concentration of ATP in cells Escherichia coli 2 ADP
-
?
ATP + AMP electrostatic interactions determine entrance and release order of substrates in the catalytic cycle of adenylate kinase Escherichia coli 2 ADP
-
?
ATP + AMP the enzyme is involved in regulating concentration of ATP in cells Escherichia coli K12 2 ADP
-
?
ATP + AMP electrostatic interactions determine entrance and release order of substrates in the catalytic cycle of adenylate kinase Escherichia coli K12 2 ADP
-
?

Subunits

Subunits Comment Organism
monomer
-
Escherichia coli

General Information

General Information Comment Organism
physiological function the enzyme is involved in regulating concentration of ATP in cells Escherichia coli