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Literature summary extracted from

  • Pretzel, J.; Gehr, M.; Eisenkolb, M.; Wang, L.; Fritz-Wolf, K.; Rahlfs, S.; Becker, K.; Jortzik, E.
    Characterization and redox regulation of Plasmodium falciparum methionine adenosyltransferase (2016), J. Biochem., 160, 355-367 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.5.1.6 reduced thioredoxin increases the activity Plasmodium falciparum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.6 expression in the Escherichia coli strain M15 Plasmodium falciparum

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.6 C113S compared with the wild type enzyme the mutant enzyme is only weakly activated by PfTrx1. The mutation significantly decreases the affinity to the substrate L-methionine. The mutant enzyme shows higher affinity towards ATP when compared with the wild type Plasmodium falciparum
2.5.1.6 C187S with regard to specific activity the mutant enzyme does not show major differences compared with the wild type enzyme. The mutant enzyme shows higher affinity towards ATP when compared with the wild type Plasmodium falciparum
2.5.1.6 C52S compared with the wild type enzyme the mutant enzyme is only weakly activated by PfTrx1. With regard to specific activity the mutant enzyme does not show major differences compared with the wild type enzyme. The mutation significantly decreases the affinity to the substrate L-methionine and ATP Plasmodium falciparum

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.5.1.6 NO the enzyme is inhibited upon S-nitrosylation. S-Nitrosylation of the enzyme is mediated via several cysteine residues, including Cys52, Cys113 and Cys187. Nitrosylation is a reversible posttranslational modification upon nitrosative stress Plasmodium falciparum
2.5.1.6 S-nitrosoglutathione the enzyme is inhibited upon S-nitrosylation. S-Nitrosylation of the enzyme is not only mediated via a single cysteine but via several cysteine residues, including Cys52, Cys113 and Cys187 Plasmodium falciparum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.5.1.6 0.034
-
 L-methionine pH 8.4, 37°C Plasmodium falciparum
2.5.1.6 0.043
-
 L-methionine pH 8.4, 37°C, mutant enzyme Plasmodium falciparum
2.5.1.6 0.046
-
 L-methionine pH 8.4, 37°C, mutant enzyme Plasmodium falciparum
2.5.1.6 0.051
-
 L-methionine pH 8.4, 37°C, mutant enzyme Plasmodium falciparum
2.5.1.6 0.176
-
 ATP pH 8.4, 37°C, mutant enzyme Plasmodium falciparum
2.5.1.6 0.206
-
 ATP pH 8.4, 37°C, mutant enzyme Plasmodium falciparum
2.5.1.6 0.56
-
 ATP pH 8.4, 37°C Plasmodium falciparum
2.5.1.6 0.68
-
 ATP pH 8.4, 37°C, mutant enzyme Plasmodium falciparum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.6 ATP + L-methionine + H2O Plasmodium falciparum
-
 phosphate + diphosphate + S-adenosyl-L-methionine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.6 Plasmodium falciparum Q7K6A4
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.5.1.6 glutathionylation the enzyme is inhibited upon glutathionylation Plasmodium falciparum
2.5.1.6 nitrosylation the enzyme is inhibited upon S-nitrosylation. S-Nitrosylation of PfalMAT is mediated via several cysteine residues, including Cys52, Cys113 and Cys187. Nitrosylation is a reversible posttranslational modification upon nitrosative stress Plasmodium falciparum

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.6
-
 Plasmodium falciparum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.6 ATP + L-methionine + H2O
-
 Plasmodium falciparum phosphate + diphosphate + S-adenosyl-L-methionine
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.5.1.6 1.02
-
 ATP pH 8.4, 37°C, mutant enzyme Plasmodium falciparum
2.5.1.6 1.02
-
 L-methionine pH 8.4, 37°C, mutant enzyme Plasmodium falciparum
2.5.1.6 1.05
-
 ATP pH 8.4, 37°C, mutant enzyme Plasmodium falciparum
2.5.1.6 1.05
-
 L-methionine pH 8.4, 37°C, mutant enzyme Plasmodium falciparum
2.5.1.6 1.06
-
 ATP pH 8.4, 37°C Plasmodium falciparum
2.5.1.6 1.06
-
 L-methionine pH 8.4, 37°C Plasmodium falciparum
2.5.1.6 1.48
-
 ATP pH 8.4, 37°C, mutant enzyme Plasmodium falciparum
2.5.1.6 1.48
-
 L-methionine pH 8.4, 37°C, mutant enzyme Plasmodium falciparum

General Information

EC Number General Information Comment Organism
2.5.1.6 malfunction depletion of S-adenosylmethionine has downstream effects on polyamine metabolism and methylation reactions, and is an effective way to combat pathogenic microorganisms such as malaria parasites Plasmodium falciparum
2.5.1.6 metabolism as a methyl group donor for biochemical reactions, the product S-adenosylmethionine plays a central metabolic role in most organisms Plasmodium falciparum

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.5.1.6 1.5
-
 ATP pH 8.4, 37°C, mutant enzyme Plasmodium falciparum
2.5.1.6 1.9
-
 ATP pH 8.4, 37°C Plasmodium falciparum
2.5.1.6 5.9
-
 ATP pH 8.4, 37°C, mutant enzyme Plasmodium falciparum
2.5.1.6 7.2
-
 ATP pH 8.4, 37°C, mutant enzyme Plasmodium falciparum
2.5.1.6 22.3
-
 L-methionine pH 8.4, 37°C, mutant enzyme Plasmodium falciparum
2.5.1.6 24.5
-
 L-methionine pH 8.4, 37°C, mutant enzyme Plasmodium falciparum
2.5.1.6 31.2
-
 L-methionine pH 8.4, 37°C Plasmodium falciparum
2.5.1.6 32.2
-
 L-methionine pH 8.4, 37°C, mutant enzyme Plasmodium falciparum