Literature summary for 2.2.1.6 extracted from

Kyselkova, M.; Janata, J.; Sagova-Mareckova, M.; Kopecky, J.
Subunit-subunit interactions are weakened in mutant forms of acetohydroxy acid synthase insensitive to valine inhibition (2010), Arch. Microbiol., 192, 195-200.

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Protein Variants

Protein Variants	Comment	Organism
DeltaQ217	mutation in the beta-domain of the catalytic subunit, affecting regulation by valine. Mutation is located on the surface of the catalytic subunit dimer and lowers the interaction with the regulatory subunit	Streptomyces virginiae
E139A	mutation in the alpha-domain of the catalytic subunit, affecting regulation by valine. Mutation is located on the surface of the catalytic subunit dimer and lowers the interaction with the regulatory subunit	Streptomyces virginiae
G16D	mutation in the N-terminal part of the regulatory subunit ilvN, affecting regulation by valine. Mutation considerably reduces the interaction of the subunits	Streptomyces virginiae
L18F	mutation in the N-terminal part of the regulatory subunit ilvN, affecting regulation by valine. Mutation does not influence the interaction of the subunits	Streptomyces virginiae
additional information	shortening of the regulatory subunit to 107 residues reduces the interaction with the catalytic subunit essentially	Streptomyces virginiae
V17D	mutation in the N-terminal part of the regulatory subunit ilvN, affecting regulation by valine. Mutation considerably reduces the interaction of the subunits	Streptomyces virginiae

Organism

Organism	UniProt	Comment	Textmining
Streptomyces virginiae	Q5S3P7	catalytic subunit ilvB	-
Streptomyces virginiae	Q9RFQ7	-	-

Synonyms

Synonyms	Comment	Organism
ilvB	-	Streptomyces virginiae
IlvN	-	Streptomyces virginiae

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Release 2023.1 (January 2023)