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Literature summary extracted from

  • Rahlfs, S.; Koncarevic, S.; Iozef, R.; Mailu, B.M.; Savvides, S.N.; Schirmer, R.H.; Becker, K.
    Myristoylated adenylate kinase-2 of Plasmodium falciparum forms a heterodimer with myristoyltransferase (2009), Mol. Biochem. Parasitol., 163, 77-84.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.4.3 coexpression of adenylate kinase 2 and N-myristoyltransferase in the presence of myristate in Escherichia coli strain C-41 Plasmodium falciparum

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.4.3 P1,P5-(diadenosine-5')-pentaphosphate adenylate kinase-specific inhibitor Plasmodium falciparum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.4.3 0.075
-
 ATP recombinant adenylate kinase 2, in 110 mM TEA-HCl, pH 7.6, at 25°C Plasmodium falciparum
2.7.4.3 0.29
-
 AMP recombinant adenylate kinase 2, in 110 mM TEA-HCl, pH 7.6, at 25°C Plasmodium falciparum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.4.3 32500
-
 estimated from amino acid sequence Plasmodium falciparum
2.7.4.3 33000
-
 1 * 33000, recombinant adenylate kinase 2 Plasmodium falciparum
2.7.4.3 34000
-
 estimated from SDS-PAGE Plasmodium falciparum

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.3 Plasmodium falciparum Q14EL6
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.4.3 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 (Commentary)

EC Number Purification (Comment) Organism
2.7.4.3 Protino-Ni-TED column chromatography Plasmodium falciparum

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.4.3 10
-
 recombinant enzyme, in 110 mM TEA-HCl, pH 7.6, at 25°C Plasmodium falciparum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.3 ATP + AMP the substrate pair ATP/AMP results in maximal activity Plasmodium falciparum ADP + ADP
-
 ?
2.7.4.3 CTP + AMP 15% activity compared to ATP Plasmodium falciparum CDP + ADP
-
 ?
2.7.4.3 GTP + AMP 8.4% activity compared to ATP Plasmodium falciparum GDP + ADP
-
 ?
2.7.4.3 ITP + AMP 7.2% activity compared to ATP Plasmodium falciparum IDP + ADP
-
 ?
2.7.4.3 additional information when replacing AMP by GMP, UMP or IMP the measured activity is less than 1% Plasmodium falciparum ?
-
 ?
2.7.4.3 UTP + AMP 1.4% activity compared to ATP Plasmodium falciparum UDP + ADP
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.4.3 monomer 1 * 33000, recombinant adenylate kinase 2 Plasmodium falciparum

Synonyms

EC Number Synonyms Comment Organism
2.7.4.3 adenylate kinase-2
-
 Plasmodium falciparum
2.7.4.3 AK2 isozyme Plasmodium falciparum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.4.3 5.4
-
 ATP recombinant adenylate kinase 2, in 110 mM TEA-HCl, pH 7.6, at 25°C Plasmodium falciparum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.4.3 8
-
-
 Plasmodium falciparum

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.7.4.3 Plasmodium falciparum estimated from amino acid sequence
-
 7.5

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.7.4.3 0.2
-
-
 Plasmodium falciparum P1,P5-(diadenosine-5')-pentaphosphate