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Literature summary for 2.7.4.3 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)

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

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

KM Value [mM]

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 [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

Organism UniProt Comment Textmining
Plasmodium falciparum Q14EL6
-
-

Posttranslational Modification

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 (Commentary)

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

Specific Activity [micromol/min/mg]

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 and Products (Substrate)

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

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

Synonyms

Synonyms Comment Organism
adenylate kinase-2
-
Plasmodium falciparum
AK2 isozyme Plasmodium falciparum

Turnover Number [1/s]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Plasmodium falciparum

pI Value

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

IC50 Value

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