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.
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 |
|
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 |