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Literature summary extracted from

  • Dai, Y.N.; Chi, C.B.; Zhou, K.; Cheng, W.; Jiang, Y.L.; Ren, Y.M.; Ruan, K.; Chen, Y.; Zhou, C.Z.
    Structure and catalytic mechanism of yeast 4-amino-4-deoxychorismate lyase (2013), J. Biol. Chem., 288, 22985-22992.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.3.38 recombinant expression of His-tagged wild-type and selenomethionine-labeled enzymes in Escherichia coli strain BL21(DE3) and B834(DE3), respectively Saccharomyces cerevisiae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.3.38 purified recombinant selenomethionine-labeled enzyme and of purified recombinant wild-type enzyme in complex with cofactor pyridoxal 5'-phosphate, hanging drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 100 mM NaCl, 20 mM Tris-Cl, pH 8.0, with an equal volume of reservoir solution containing 20% w/v PEG monomethyl ether 5000, 0.1 M Bis-Tris, pH 6.2, 1-2 days to 1 week, 16°C, X-ray diffraction structure determination and analysis at 1.90-2.20 A resolution Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
4.1.3.38 K180A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
4.1.3.38 N360A site-directed mutagenesis, inactive mutant Saccharomyces cerevisiae
4.1.3.38 N360D site-directed mutagenesis, inactive mutant Saccharomyces cerevisiae
4.1.3.38 T30A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae

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 Saccharomyces cerevisiae
-
 4-aminobenzoate + pyruvate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.3.38 Saccharomyces cerevisiae Q03266
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.3.38 recombinant His-tagged wild-type and selenomethionine-labeled enzymes from Escherichia coli strain BL21(DE3) and B834(DE3), respectively, by nickel affinity chromatography Saccharomyces cerevisiae

Reaction

EC Number Reaction Comment Organism Reaction ID
4.1.3.38 4-amino-4-deoxychorismate = 4-aminobenzoate + pyruvate catalytic mechanism, overview Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.3.38 4-amino-4-deoxychorismate
-
 Saccharomyces cerevisiae 4-aminobenzoate + pyruvate
-
 ?
4.1.3.38 4-amino-4-deoxychorismate simulation and validation of the substrate-binding model, overview Saccharomyces cerevisiae 4-aminobenzoate + pyruvate
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.3.38 monomer
-
 Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
4.1.3.38 4-amino-4-deoxychorismate lyase
-
 Saccharomyces cerevisiae
4.1.3.38 Abz2
-
 Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.3.38 pyridoxal 5'-phosphate dependent on, one molecule of cofactor is deeply buried in the cleft between domains I and II, pyridoxal 5'-phosphate adopts the re-face specificity facing the protein side and is covalently linked to the catalytic residue Lys251 by forming an internal aldimine bond, Schiff base linkage Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
4.1.3.38 evolution 4-amino-4-deoxychorismate lyases can be divided into two classes of dimeric and monomeric enzyme, respectively Saccharomyces cerevisiae
4.1.3.38 additional information the catalytic residue Lys251 covalently binds the cofactor pyridoxal 5'-phosphate Saccharomyces cerevisiae