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Literature summary for 2.7.4.3 extracted from

  • Sheng, X.R.; Li, X.; Pan, X.M.
    An iso-random Bi Bi mechanism for adenylate kinase (1999), J. Biol. Chem., 274, 22238-22242.
    View publication on PubMed
Search for more literature for 2.7.4.3

Inhibitors

Inhibitors Comment Organism Structure
ADP
-
 Oryctolagus cuniculus
AMP
-
 Oryctolagus cuniculus
P1,P5-diadenosine 5'-pentaphosphate competitive for formation of ADP, noncompetitive for formation of ATP Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.028
-
 ADP pH 8.1 Oryctolagus cuniculus
0.06
-
 ATP pH 7.5 Oryctolagus cuniculus
0.06
-
 ATP ATP in form of MgATP2- Oryctolagus cuniculus
0.12
-
 AMP pH 7.5 Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + AMP = 2 ADP iso-random bi-bi mechanism Oryctolagus cuniculus
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1600 1700 muscle enzyme, pH 8.1 Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + AMP
-
 Oryctolagus cuniculus ADP + ADP
-
 r
ATP + AMP
-
 Oryctolagus cuniculus 2 ADP
-
 ?

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.000002
-
 P1,P5-diadenosine 5'-pentaphosphate
-
 Oryctolagus cuniculus
0.91
-
 ADP pH 8.1 Oryctolagus cuniculus
3.3
-
 AMP pH 7.5 Oryctolagus cuniculus