Literature summary for 2.2.1.6 extracted from

Megha Karanth, N.; Mitra, A.; Sarma, S.
Solution NMR studies of acetohydroxy acid synthase I: Identification of the sites of inter-subunit interactions using multidimensional NMR methods (2009), J. Mol. Catal. B, 61, 7-13.

No PubMed abstract available

Crystallization (Commentary)

Crystallization (Comment)	Organism
solution NMR studies. The secondary structure of the FAD binding domain of large subunit ilvB is similar to the structure of this domain in the catalytic subunit of yeast AHAS. The regulatory subunit ilvN interacts with ilvBalpha and ilvBbeta domains of the catalytic subunit and not with the ilvBgamma domain. ilvN binds close to the FAD binding site in ilvBbeta and proximal to the intrasubunit ilvBalpha/ilvBbeta domain interface	Escherichia coli

Crystallization (Comment)

Organism

solution NMR studies. The secondary structure of the FAD binding domain of large subunit ilvB is similar to the structure of this domain in the catalytic subunit of yeast AHAS. The regulatory subunit ilvN interacts with ilvBalpha and ilvBbeta domains of the catalytic subunit and not with the ilvBgamma domain. ilvN binds close to the FAD binding site in ilvBbeta and proximal to the intrasubunit ilvBalpha/ilvBbeta domain interface

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	isozyme AHAS I	-

Cofactor

Cofactor	Comment	Organism	Structure
FAD	the secondary structure of the FAD binding domain of large subunit ilvB is similar to the structure of this domain in the catalytic subunit of yeast AHAS. The regulatory subunit ilvN interacts with ilvBalpha and ilvBbeta domains of the catalytic subunit and not with the ilvBgamma domain. ilvN binds close to the FAD binding site in ilvBbeta and proximal to the intrasubunit ilvBalpha/ilvBbeta domain interface	Escherichia coli

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Release 2023.1 (January 2023)