Literature summary for 2.6.1.85 extracted from

Ziebart, K.T.; Toney, M.D.
Nucleophile specificity in anthranilate synthase, aminodeoxychorismate synthase, isochorismate synthase, and salicylate synthase (2010), Biochemistry, 49, 2851-2859.

Search for more literature for 2.6.1.85

Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
K213A	subunit PabB, numbering used is based on the EntC protein from Escherichia coli, reduced activity	Escherichia coli
K213A/Q147K	subunit PabB, numbering used is based on the EntC protein from Escherichia coli, strongly reduced activity	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
chorismate + L-glutamine	-	Escherichia coli	L-glutamate + 4-amino-4-deoxychorismate	-	?

Subunits

Subunits	Comment	Organism
heterodimer	PabA-PabB	Escherichia coli

Synonyms

Synonyms	Comment	Organism
aminodeoxychorismate synthase	-	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.6	-	L-glutamine	mutant K213A/Q147K amidotransferase activity, pH 8.0, 25°C	Escherichia coli
0.67	-	L-glutamine	wild type amidotransferase activity, pH 8.0, 25°C	Escherichia coli

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Release 2023.1 (January 2023)