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 |
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 |
|