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Literature summary for 4.1.3.38 extracted from
- Completing the folate biosynthesis pathway in Plasmodium falciparum: p-aminobenzoate is produced by a highly divergent promiscuous aminodeoxychorismate lyase (2013), Biochem. J., 455, 149-155.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene PF14_0557, functional overexpression as His6-tagged protein in Escherichia coli cells | Plasmodium falciparum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| D-glutamate | D-Glu (in the absence of 2-oxoacids) inhibits the aminodeoxychorismate lyase activity of the enzyme | Plasmodium falciparum |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-amino-4-deoxychorismate | Plasmodium falciparum | - |
4-aminobenzoate + pyruvate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Plasmodium falciparum | Q8IKP7 | plasmodial gene PF14_0557 encodes a functional ADCL; gene PF14_0557 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged enzyme from Escherichia coli by metal affinity chromatography | Plasmodium falciparum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-amino-4-deoxychorismate | - |
Plasmodium falciparum | 4-aminobenzoate + pyruvate | - |
? | |
| 4-amino-4-deoxychorismate | the enzyme catalyzes the beta-elimination of pyruvate and the aromatization of the ADC ring to yield 4-aminobenzoate. Substrate synthesis from chorismate and ammonia by chorismate aminase in a coupled assay, the substrate is unstable | Plasmodium falciparum | 4-aminobenzoate + pyruvate | - |
? | |
| additional information | The enzyme shows some transaminase activity towards different D-amino acids (D-Asp, D-Ala and D-Glu, in particular) using 2-oxoacids such as oxaloacetate or pyruvate as amino group acceptors. This activity corresponds to EC 2.6.1.21. | Plasmodium falciparum | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ADCL | - |
Plasmodium falciparum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Plasmodium falciparum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.5 | - |
assay at | Plasmodium falciparum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| pyridoxal 5'-phosphate | dependent on | Plasmodium falciparum | |
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