Disease relevance of NTR1

• The relative positions of the domains in A. thaliana thioredoxin reductase differ from those of the E. coli reductase [1].

High impact information on NTR1

• We also have characterized AtNTRA, a gene encoding a protein highly similar to the previously described cytosolic NADPH-dependent thioredoxin reductase AtNTRB but with a putative presequence for import into mitochondria [2].
• Thioredoxin is reduced by the flavoenzyme thioredoxin reductase using NADPH [1].
• When the FAD domains are superimposed, the NADPH domain of A. thaliana thioredoxin reductase must be rotated by 8 degrees to superimpose on the corresponding domain of the E. coli enzyme [1].
• Their sequence homology with Escherichia coli NRT (the only thioredoxin reductase of known primary structure) is about 45% [3].
• AtNTRB is the major mitochondrial thioredoxin reductase in Arabidopsis thaliana [4].

Associations of NTR1 with chemical compounds

• Incubation of reduced TR in the presence of tetryl or 2,4-dinitrochlorobenzene resulted in a loss of thioredoxin reductase activity, most probably due to modification of reduced catalytic disulfide, whereas nitroreductase reaction rates were unchanged [5].

Other interactions of NTR1

• Among them, NTR1 codes for a membrane protein with weak histidine transport activity [6].

References