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Literature summary for 4.1.3.27 extracted from

  • Kwak, J.H.; Hong, K.W.; Lee, S.H.; Hong, J.H.; Lee, S.Y.
    Identification of amino acid residues involved in feedback inhibition of the anthranilate synthase in Escherichia coli (1999), J. Biochem. Mol. Biol., 32, 20-24.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
mutant anthanilate synthase Pro21Ser that is insensitive to feedback inhibition by Trp Escherichia coli

Protein Variants

Protein Variants Comment Organism
P21S insensitive to feedback inhibition by Trp Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
L-Trp strain with a anthanilate synthase that is insensitive to feedback inhibition by Trp, the 61st nucleotide, C to A substitution, that changes Pro21 to Ser is the cause of the desensitization to feedback inhibition by Trp Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli first enzyme in the branch pathway in Trp biosynthesis ?
-
?

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum
-
-
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Escherichia coli
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strain with a mutant anthranilate synthase Pro21Gln that is insensitive to feedback inhibition by Trp
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
chorismate + L-Gln
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Escherichia coli anthranilate + pyruvate + L-glutamate
-
?
chorismate + L-Gln
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Corynebacterium glutamicum anthranilate + pyruvate + L-glutamate
-
?
additional information first enzyme in the branch pathway in Trp biosynthesis Escherichia coli ?
-
?