Cloned (Comment) | Organism |
---|---|
coexpression of adenylate kinase 2 and N-myristoyltransferase in the presence of myristate in Escherichia coli strain C-41 | Plasmodium falciparum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
P1,P5-(diadenosine-5')-pentaphosphate | adenylate kinase-specific inhibitor | Plasmodium falciparum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.075 | - |
ATP | recombinant adenylate kinase 2, in 110 mM TEA-HCl, pH 7.6, at 25°C | Plasmodium falciparum | |
0.29 | - |
AMP | recombinant adenylate kinase 2, in 110 mM TEA-HCl, pH 7.6, at 25°C | Plasmodium falciparum |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
32500 | - |
estimated from amino acid sequence | Plasmodium falciparum |
33000 | - |
1 * 33000, recombinant adenylate kinase 2 | Plasmodium falciparum |
34000 | - |
estimated from SDS-PAGE | Plasmodium falciparum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Plasmodium falciparum | Q14EL6 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
acylation | at its N-terminus adenylate kinase 2 carries a predicted myristoylation sequence, this sequence is only present in adenylate kinase 2 of Plasmodium falciparum causing the severe tropical malaria and not in other malarial parasites, the modification significantly enhances the stability of the kinase | Plasmodium falciparum |
Purification (Comment) | Organism |
---|---|
Protino-Ni-TED column chromatography | Plasmodium falciparum |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
10 | - |
recombinant enzyme, in 110 mM TEA-HCl, pH 7.6, at 25°C | Plasmodium falciparum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + AMP | the substrate pair ATP/AMP results in maximal activity | Plasmodium falciparum | ADP + ADP | - |
? | |
CTP + AMP | 15% activity compared to ATP | Plasmodium falciparum | CDP + ADP | - |
? | |
GTP + AMP | 8.4% activity compared to ATP | Plasmodium falciparum | GDP + ADP | - |
? | |
ITP + AMP | 7.2% activity compared to ATP | Plasmodium falciparum | IDP + ADP | - |
? | |
additional information | when replacing AMP by GMP, UMP or IMP the measured activity is less than 1% | Plasmodium falciparum | ? | - |
? | |
UTP + AMP | 1.4% activity compared to ATP | Plasmodium falciparum | UDP + ADP | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 33000, recombinant adenylate kinase 2 | Plasmodium falciparum |
Synonyms | Comment | Organism |
---|---|---|
adenylate kinase-2 | - |
Plasmodium falciparum |
AK2 | isozyme | Plasmodium falciparum |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
5.4 | - |
ATP | recombinant adenylate kinase 2, in 110 mM TEA-HCl, pH 7.6, at 25°C | Plasmodium falciparum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
- |
Plasmodium falciparum |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Plasmodium falciparum | estimated from amino acid sequence | - |
7.5 |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.2 | - |
- |
Plasmodium falciparum | P1,P5-(diadenosine-5')-pentaphosphate |