Sequence of NB5R3_PIG
EC Number:1.6.2.2
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
NADH + 2 ferricytochrome b5 = NAD+ + H+ + 2 ferrocytochrome b5
Other sequences found for EC No. 1.6.2.2
General information:
Sequence
0 STPAITLENP DIKYPLRLID KEVVNHDTRR FRFALPSPEH ILGLPVGQHI YLSARIDGNL
60 VIRPYTPVSS DDDKGFVDLV IKVYFKDTHP KFPAGGKMSQ YLESMKIGDT IEFRGPNGLL
120 VYQGKGKFAI RPDKKSSPVI KTVKSVGMIA GGTGITPMLQ VIRAIMKDPD DHTVCHLLFA
180 NQTEKDILLR PELEELRNEH SARFKLWYTV DRAPEAWDYS QGFVNEEMIR DHLPPPEEEP
240 LVLMCGPPPM IQYACLPNLE RVGHPKERCF AF
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
193787
Kimura S.,Emi Y.,Ikushiro S.,Iyanagi T.
Systematic mutations of highly conserved His49 and carboxyl-terminal of recombinant porcine liver NADH-cytochrome b5 reductase solubilized domain.
Biochim. Biophys. Acta
1430
290-301
1999
193788
Crabb J.W.,Tarr G.E.,Yasunobu K.T.,Iyanagi T.,Coon M.J.
Terminal sequences of lysosome solubilized pig liver cytochrome b5 reductase.
Biochem. Biophys. Res. Commun.
95
1650-1655
1980
193789
Ghesquier D.,Robert J.C.,Soumarmon A.,Abastado M.,Grelac F.,Lewin M.J.M.
Gastric microsomal NADH-cytochrome b5 reductase: characterization and solubilization.
Comp. Biochem. Physiol.
80B
165-169
1985
193790
Nishida H.,Inaka K.,Miki K.
Specific arrangement of three amino acid residues for flavin-binding barrel structures in NADH-cytochrome b5 reductase and the other flavin-dependent reductases.
FEBS Lett.
361
97-100
1995
193791
Iyanagi T.
Redox properties of microsomal reduced nicotinamide adenine dinucleotide-cytochrome b5 reductase and cytochrome b5.
Biochemistry
16
2725-2730
1977
193792
Kobayashi K.,Iyanagi T.,Ohara H.,Hayashi K.
One-electron reduction of hepatic NADH-cytochrome b5 reductase as studied by pulse radiolysis.
J. Biol. Chem.
263
7493-7499
1988
193793
Kimura S.,Nishida H.,Iyanagi T.
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on protein stability and catalysis.
J. Biochem.
130
481-490
2001
193794
Kimura S.,Kawamura M.,Iyanagi T.
Role of Thr(66) in porcine NADH-cytochrome b5 reductase in catalysis and control of the rate-limiting step in electron transfer.
J. Biol. Chem.
278
3580-3589
2003
193795
Havemeyer A.,Bittner F.,Wollers S.,Mendel R.,Kunze T.,Clement B.
Identification of the missing component in the mitochondrial benzamidoxime prodrug converting system as a novel molybdenum enzyme.
J. Biol. Chem.
281
34796-34802
2006
193796
Nishida H.,Inaka K.,Yamanaka M.,Kaida S.,Kobayashi K.,Miki K.
Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution.
Biochemistry
34
2763-2767
1995
193797
Nishida H.,Miki K.
Electrostatic properties deduced from refined structures of NADH-cytochrome b5 reductase and the other flavin-dependent reductases: pyridine nucleotide-binding and interaction with an electron-transfer partner.
Proteins
26
32-41
1996
