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1.6.2.2: cytochrome-b5 reductase

This is an abbreviated version!
For detailed information about cytochrome-b5 reductase, go to the full flat file.

Word Map on EC 1.6.2.2

Reaction

NADH
+ 2 ferricytochrome b5 =
NAD+
 +
H+
 + 2 ferrocytochrome b5

Synonyms

b5 plusb5R, b5/b5R, B5R, cb5r, CBR, CBR1, CBR1A, CBR1B, CyB5R, CYB5R2, CYB5R3, Cyb5R4, cyt b5r, cyt b5R protein, cytochrome b5 reductase, cytochrome b5 reductase 2, cytochrome b5 reductase 3, DIA1, diaphorase I, dihydronicotinamide adenine dinucleotide-cytochrome b5 reductase, HPO-19, methemoglobin reductase, NADH cytochrome b5 oxidoreductase, NADH cytochrome B5 reductase, NADH-b5R, NADH-cytochrome b 5 reductase, NADH-cytochrome b5 reductase, NADH-cytochrome b5 reductase 3, NADH-cytochrome-b5 reductase, NADH-cytochrome-b5 reductase 3, NADH-dependent cytochrome b5 reductase, NADH-ferricyanide reductase, NADH-ferricytochrome b5 oxidoreductase, NADH-ferricytochrome reductase, NADH: ferricytochrome b5 oxidoreductase, NADH:cytochrome b5 reductase, NADH:ferricytochrome b5 oxidoreductase, Ncb5or, P34/P32, P35, reduced nicotinamide adeninedinucleotide-cytochrome b5 reductase, reductase, cytochrome b5, T05H4.4

ECTree

     1 Oxidoreductases
         1.6 Acting on NADH or NADPH
             1.6.2 With a heme protein as acceptor
                1.6.2.2 cytochrome-b5 reductase

Crystallization

Crystallization on EC 1.6.2.2 - cytochrome-b5 reductase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 2 M (NH4)2SO4, 100 mM sodium/potassium phosphate, pH 6.2, 200 mM Li2SO4, at 4°C
sitting-drop vapor diffusion method
-
structure of a construct comprising the naturally fused CHORD-Sgt1 and b5R domains with bound FAD and NAD+ or NADP+. The linker between the CHORD-Sgt1 and b5R cores is more ordered than predicted, with much of it extending the beta-sandwich motif of the CHORD-Sgt1 domain. This limits the flexibility between the two domains
vapor equilibrium method, 3.6% protein solution, 30% polyethyleneglycol 4000, preliminary X-ray data
-
hanging-drop vapour-diffusion method
-
sitting drop method
-
sitting drop method, complete data set collected for the D239T mutant enzyme
sitting drop method, reservoir: 8% poly ethylene glycol 6000, 5% 2-methyl-2,4-pentanediol in 100 mM 4-(2-hydroxyethyl)piperazine-1-ethanesulfonic acid, pH 7.5, X-ray structure, resolution: enzyme 2.0 A, enzyme-NAD+ complex, 2.3 A
fully reduced form and the oxidized form of the purified liver enzyme, X-ray diffraction structure determination and analysis at 1.68 A resolution
hanging drop vapor diffusion method, using 9-12% (w/v) PEG 4,000, 100 mM potassium phosphate (pH 7.7) and 5 mM dithiothreitol
vapor diffusion method, 5 mg/ml protein, 12.5% polyethylenglycol 4000, 50 mM potassium phosphate pH 6.0-8.0, 0.1 mM EDTA, preliminary X-ray data
-
X-ray structure, 2.4 A resolution
-
structure of the cytochrome b5 reductase domain. The N-terminal FAD-binding domain primarily consists of six antiparallel beta-strands, a C-terminal NADH-binding domain forming a Rossmann fold, and a three beta-stranded linker region connecting these two domains. The FAD cofactor is located in the cleft between the two domains and interacts primarily with the FAD-binding domain