BRENDA - Enzyme Database

Function and maturation of the Fe-S center in dihydroxyacid dehydratase from Arabidopsis

Gao, H.; Azam, T.; Randeniya, S.; Couturier, J.; Rouhier, N.; Johnson, M.K.; J. Biol. Chem. 293, 4422-4433 (2018)

Data extracted from this reference:

Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.2.1.9
Arabidopsis thaliana
Q9LIR4
-
-
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
4.2.1.9
[2Fe-2S]-center
DHAD can accommodate [Fe2S2] and [Fe4S4] clusters. Only the [Fe2S2] cluster-bound form is catalytically active. The [Fe2S2] cluster is coordinated by at least one non-cysteinyl ligand, which can be replaced by the thiol group(s) of dithiothreitol. [Fe2S2] cluster-containing NFU2 protein is likely the physiological cluster donor for in vivo maturation of DHAD
Arabidopsis thaliana
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
4.2.1.9
[2Fe-2S]-center
DHAD can accommodate [Fe2S2] and [Fe4S4] clusters. Only the [Fe2S2] cluster-bound form is catalytically active. The [Fe2S2] cluster is coordinated by at least one non-cysteinyl ligand, which can be replaced by the thiol group(s) of dithiothreitol. [Fe2S2] cluster-containing NFU2 protein is likely the physiological cluster donor for in vivo maturation of DHAD
Arabidopsis thaliana