Literature summary for 4.1.3.38 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)

Cloned (Comment)	Organism
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)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

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

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
4-amino-4-deoxychorismate	Saccharomyces cerevisiae	-	4-aminobenzoate + pyruvate	-	?

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	Q03266	-	-

Purification (Commentary)

Purification (Comment)	Organism
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

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

Substrates and Products (Substrate)

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

Subunits

Subunits	Comment	Organism
monomer	-	Saccharomyces cerevisiae

Synonyms

Synonyms	Comment	Organism
4-amino-4-deoxychorismate lyase	-	Saccharomyces cerevisiae
Abz2	-	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
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

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