1.1.1.382: ketol-acid reductoisomerase (NAD+)
This is an abbreviated version!
For detailed information about ketol-acid reductoisomerase (NAD+), go to the full flat file.
Reaction
Synonyms
ilvC
ECTree
1.1.1.382 ketol-acid reductoisomerase (NAD+)Advanced search results
results (
results (Crystallization
Crystallization on EC 1.1.1.382 - ketol-acid reductoisomerase (NAD+)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
in complex with substrate analog L-tartaric acid, to 2.5 A resolution. The enzyme displays a six-member specificity loop, with residues Arg48 and Ser52 forming hydrogen bonds to the NAD(H) phosphate
apo-enzyme, to 1.39 A resolution, and in complex with NADP+. Enzyme accepts both cofactors NADH and NADPH. Insertions near the N-terminus of the specificity loop probably determine cofactor specificity, the laboratory engineering of NADH preference involved specific loop substitution
in complex with NADH, to 1.54 A resolution. The specificity loop differs significantly from any other crystallized ketol-acid reductoisomerases. Glu46, the first residue of the beta2alphaB-loop, lies along the N3 edge of the adenine moiety and forms a bi-dentate interaction with the O2' hydroxy of the ribose. The position of this glutamate is stabilized by a hydrogen bond interaction with Asn55
to 1.54 A resolution. Structure contains 2 Mg2+ ions and NADH. Glu46, the first residue of the beta2alphaB-loop, lies along the N3 edge of the adenine moiety and forms a bi-dentate interaction with the O2 hydroxy of the ribose. The position of this glutamate is stabilized by a hydrogen bond interaction with Asn55
