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2.7.4.3: adenylate kinase

This is an abbreviated version!
For detailed information about adenylate kinase, go to the full flat file.

Word Map on EC 2.7.4.3

Reaction

ATP
+
AMP
=
2 ADP

Synonyms

5'-AMP-kinase, ABC adenylate kinase, AD-004 like protein, adenosine 5'-triphosphate:adenosine 5'-monophosphate phosphotransferase, adenylate kinase, adenylate kinase 1, adenylate kinase 2, adenylate kinase 4, adenylate kinase 5, adenylate kinase 6, adenylate kinase 9, adenylate kinase isoenzyme 1, adenylate kinase isozyme 2, adenylate kinase-2, adenylate kinase-like protein 1, adenylic kinase, adenylokinase, ADK, ADK1, ADK2, ADLP, AK1, AK2, AK4, AK5, AK5p1, AK5p2, AK6, AK7, AK8, AK9, AKE, AKlse4, AKm, AKmeso, AKp, AKpsycrho, AKthermo, ATP:AMP phosphotransferase, CFTR, CINAP, coilin interacting nuclear ATPase protein, cystic fibrosis transmembrane conductance regulator, DAK2, Dak6, kinase, adenylate (phosphorylating), kinase, myo- (phosphorylating), MeADK1, MeADK2, MJ0458, myokinase, nonstructural protein 4B, NS4B, pfSMCnbd, phosphotransferase, Rv0733, Saci_0573, SpAdK, structural maintenance of chromosome protein

ECTree

     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.4 Phosphotransferases with a phosphate group as acceptor
                2.7.4.3 adenylate kinase

General Stability

General Stability on EC 2.7.4.3 - adenylate kinase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol or various metal ions do not improve recovery during purification
-
adenylate kinase is unstable at 37°C in dilute aqueous solution with a half-life of 8 min, bovine serum albumin stabilizes in part. Enzyme is also stabilized by presence of living cells such as human umbilical vein endothelial cells
-
at low dithioerythritol concentrations enzyme tends to aggregate
-
bovine serum albumin, 1 mg/ml, stabilizes dilute enzyme solutions
-
diadenosine pentaphosphate, i.e. AP5A, stabilizes during preparative electrophoresis
-
dilution inactivates, inert proteins stabilize
-
dithiothreitol and 2-mercaptoethanol are not necessary as protecting agents
-
enzyme from Bacillus stearothermophilus is more resistant to trypsin inactivation than that from E. coli or Bacillus subtilis
-
enzyme is fully active in air
high stability towards heat and treatment with acids
-
in crude haemolysates type 1 enzyme is more stable than type 2, DTT or bovine serum albumin stabilizes
-
inactivation by contact with glass or cellophane
-
low ionic strength inactivates
-
more stable at high concentrations or in the presence of bovine serum albumin
NADH or MgATP2- or ATP plus AMP protect against proteolysis by pronase or trypsin and against heat denaturation
-
P1,P5-di(adenosine 5')-pentaphosphate binding stabilizes the enzyme
PMSF and 5'-AMP stabilize the bovine liver enzyme, 5'-AMP stabilizes the rabbit muscle enzyme
remarkably stable in dilute solution in the absence of any protective agent
-
repeated freeze-thawing inactivates
-
stable to dialysis in the presence of 4 mM dithioerythritol
-
stable to dilution to 0.001-0.002 mg enzyme/ml
-
Stable to freeze-thawing
-
stable to repeated freeze-thaw cycles, at 5-10 mg/ml
the application of 50 MPa pressure does not increase the thermostability
the application of 50 MPa pressure does not increase the thermostability. Imposition of 50-MPa pressure has a destabilizing influence
Triton X-100, EDTA, dithiothreitol and electrolyte protect enzyme in dilute solution and against denaturation by heat or extreme pH-values
-
unstable in dilute solution
-
unstable in dilute solution, 0.2 mg/ml, dithioerythritol, and bovine serum albumin stabilize
-
unstable in dilute solutions and in the absence of SH-compounds
-