N0163
Nitrate Reductase from Arabidopsis thaliana
vial of ≥0.5 unit
Sinónimos:
NADH:nitrate oxidoreductase
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About This Item
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
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recombinant
expressed in Pichia pastoris
Quality Level
form
lyophilized powder
packaging
vial of ≥0.5 unit
shipped in
wet ice
storage temp.
−20°C
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Application
Catalyzes the NADH-dependent reduction of nitrate to nitrite.
Nitrate reductase from Arabidopsis thaliana has been used in a study to assess the amino acid sequence of chicken hepatic sulfite oxidase.
Biochem/physiol Actions
Nitrate reductase activity is induced in Arabidopsis thaliana plants by sumoylation via the E3 ligase activity of AtSIZ1.
Unit Definition
One unit will reduce 1.0 micromole of nitrate to nitrite per min in a NADH system at pH 7.5 at 30 deg C.
Physical form
Supplied as a lyophilized powder containing 50 mM MOPS, pH 7.0, 0.1 mM EDTA and a proprietary sugar
signalword
Warning
hcodes
Hazard Classifications
Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Gloves
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Conserved domains in molybdenum hydroxylases. The amino acid sequence of chicken hepatic sulfite oxidase
Neame, P. and M. Barber
The Journal of Biological Chemistry, 164, 20894-20901 (1989)
Arabidopsis nitrate reductase activity is stimulated by the E3 SUMO ligase AtSIZ1
Park, BS
Nature Communications, 19, 400-400 (2011)
Vittoria Martino di Rigano et al.
Plant, cell & environment, 29(7), 1400-1409 (2006-11-04)
Temperature responses of nitrate reductase (NR) were studied in the psychrophilic unicellular alga, Koliella antarctica, and in the mesophilic species, Chlorella sorokiniana. Enzymes from both species were purified to near homogeneity by Blue Sepharose (Pharmacia, Uppsala, Sweden) affinity chromatography and
L Skipper et al.
The Journal of biological chemistry, 276(29), 26995-27002 (2001-05-18)
Recombinant Arabidopsis NADH:nitrate reductase was expressed in Pichia pastoris using fermentation. Large enzyme quantities were purified for pre-steady-state kinetic analysis, which had not been done before with any eukaryotic nitrate reductase. Basic biochemical properties of recombinant nitrate reductase were similar
Werner M Kaiser et al.
Journal of experimental botany, 53(370), 875-882 (2002-03-26)
The mechanism of the post-translational modulation of nitrate reductase activity (NR, EC 1.6.6.1) is briefly summarized, and it is shown that by this mechanism nitric oxide production through NR is also rapidly modulated. New and partly unexpected details on the
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