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Literature summary for 2.7.4.9 extracted from

  • Chen, M.D.; Fucci, I.J.; Sinha, K.; Rule, G.S.
    dGMP binding to thymidylate kinase from Plasmodium falciparum shows half-site binding and induces protein dynamics at the dimer interface (2020), Biochemistry, 59, 694-703 .
    View publication on PubMed
Search for more literature for 2.7.4.9

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Plasmodium falciparum

Protein Variants

Protein Variants Comment Organism
S108A mutant enzyme exhibits significantly higher Km and lower kcat for dGMP, but does not affect the overall enzyme kinetics toward TMP Plasmodium falciparum
S108T mutation shows minimal effect on overall kinetics toward TMP but results in significantly higher Km and lower kcat toward dGMP Plasmodium falciparum
Y153F mutant affects TMP binding. The OH of Y153F forms a direct hydrogen bond to N2 of guanine or via a bridging water molecule to O2 of thymidine Plasmodium falciparum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0242
-
 TMP mutant enzyme S108T, pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.0255
-
 TMP wild-type enzyme, pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.0258
-
 TMP mutant enzyme S108A, pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.0362
-
 dGMP wild-type enzyme, pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.0476
-
 dGMP mutant enzyme S108A, pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.0659
-
 TMP mutant enzyme Y153F, pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.0784
-
 dGMP mutant enzyme S108T, pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.0969
-
 dGMP mutant enzyme Y153F, pH 7.4, temperature not specified in the publication Plasmodium falciparum
0.1008
-
 ATP wild-type enzyme, pH 7.4, temperature not specified in the publication Plasmodium falciparum

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Plasmodium falciparum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + dGMP
-
 Plasmodium falciparum ADP + dGDP
-
 ?
ATP + TMP
-
 Plasmodium falciparum ADP + TDP
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Plasmodium falciparum

Synonyms

Synonyms Comment Organism
thymidylate kinase
-
 Plasmodium falciparum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1
-
 dGMP mutant enzyme Y153F, pH 7.4, temperature not specified in the publication Plasmodium falciparum
1.2
-
 TMP mutant enzyme Y153F, pH 7.4, temperature not specified in the publication Plasmodium falciparum
1.3
-
 dGMP mutant enzyme S108A, pH 7.4, temperature not specified in the publication Plasmodium falciparum
1.3
-
 dGMP mutant enzyme S108T, pH 7.4, temperature not specified in the publication Plasmodium falciparum
2.4
-
 dGMP wild-type enzyme, pH 7.4, temperature not specified in the publication Plasmodium falciparum
3.1
-
 TMP wild-type enzyme, pH 7.4, temperature not specified in the publication Plasmodium falciparum
3.2
-
 TMP mutant enzyme S108T, pH 7.4, temperature not specified in the publication Plasmodium falciparum
3.3
-
 TMP mutant enzyme S108A, pH 7.4, temperature not specified in the publication Plasmodium falciparum
3.3
-
 ATP wild-type enzyme, pH 7.4, temperature not specified in the publication Plasmodium falciparum

General Information

General Information Comment Organism
physiological function essential enzyme for the growth of the organism because of its critical role in the de novo synthesis of deoxythymidine 5'-diphosphate (TDP), a precursor for TTP that is required for DNA replication and repair Plasmodium falciparum