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Literature summary extracted from

  • Magnani, G.; Lomazzi, M.; Peracchi, A.
    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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.3.38 gene PF14_0557, functional overexpression as His6-tagged protein in Escherichia coli cells Plasmodium falciparum

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.3.38 D-glutamate D-Glu (in the absence of 2-oxoacids) inhibits the aminodeoxychorismate lyase activity of the enzyme Plasmodium falciparum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.3.38 4-amino-4-deoxychorismate Plasmodium falciparum
-
 4-aminobenzoate + pyruvate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.3.38 Plasmodium falciparum Q8IKP7 plasmodial gene PF14_0557 encodes a functional ADCL; gene PF14_0557
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.3.38 recombinant His6-tagged enzyme from Escherichia coli by metal affinity chromatography Plasmodium falciparum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.3.38 4-amino-4-deoxychorismate
-
 Plasmodium falciparum 4-aminobenzoate + pyruvate
-
 ?
4.1.3.38 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
-
 ?
4.1.3.38 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

EC Number Synonyms Comment Organism
4.1.3.38 ADCL
-
 Plasmodium falciparum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.3.38 30
-
 assay at Plasmodium falciparum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.3.38 8.5
-
 assay at Plasmodium falciparum

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.3.38 pyridoxal 5'-phosphate dependent on Plasmodium falciparum