Literature summary for 2.6.1.85 extracted from

Culbertson, J.E.; Chung, D.h.; Ziebart, K.T.; Espiritu, E.; Toney, M.D.
Conversion of aminodeoxychorismate synthase into anthranilate synthase with Janus mutations: mechanism of pyruvate elimination catalyzed by chorismate enzymes (2015), Biochemistry, 54, 2372-2384.

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Application

Application	Comment	Organism
biotechnology	conversion of aminodeoxychorismate synthase into anthranilate synthase employing a bioinformatics method for predicting mutations required to functionally interconvert homologous enzymes. Complementation of an anthranilate synthase-deficient strain of Escherichia coli grown on minimal medium leads to several aminodeoxychorismate synthase mutants that allow growth in 6 days compared to 2 days for wild-type anthranilate synthase. The purified mutant enzymes catalyze the conversion of chorismate to anthranilate at rates that are about 50% of the rate of wild-type aminodeoxychorismate synthase-catalyzed conversion of chorismate to aminodeoxychorismate. The residues mutated do not contact the substrate	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
K274A/L277R/D299E/N303H/I306L/F334Y/C391G	mutant displaying anthranilate synthase activity, the kcat/Kchoris value for anthranilate formation is 25% of the wild-type aminodeoxychorismate synthase value for 4-amino-4-deoxychorismate production	Escherichia coli
N213V/L214P/K274A/L277R/D299E/N303H/F334Y/P363N/I367L/C391G/G425A	mutant displaying anthranilate synthase activity, is able to produce both 2-amino-2-deoxyisochorismate and anthranilate	Escherichia coli
N213V/L214P/R259S/K274A/L277R/N303H/F334Y/S366T/C391G/G254A	mutant displaying anthranilate synthase activity, is able to produce both 2-amino-2-deoxyisochorismate and anthranilate	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P00903	-	-

Synonyms

Synonyms	Comment	Organism
ADCS	-	Escherichia coli
PabA	-	Escherichia coli

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Release 2023.1 (January 2023)