Sequence of HMOX1_RAT
EC Number:1.3.1.24
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
bilirubin + NAD(P)+ = biliverdin + NAD(P)H + H+
Other sequences found for EC No. 1.3.1.24
General information:
Sequence
0 MERPQLDSMS QDLSEALKEA TKEVHIRAEN SEFMRNFQKG QVSREGFKLV MASLYHIYTA
60 LEEEIERNKQ NPVYAPLYFP EELHRRAALE QDMAFWYGPH WQEAIPYTPA TQHYVKRLHE
120 VGGTHPELLV AHAYTRYLGD LSGGQVLKKI AQKAMALPSS GEGLAFFTFP SIDNPTKFKQ
180 LYRARMNTLE MTPEVKHRVT EEAKTAFLLN IELFEELQAL LTEEHKDQSP SQTEFLRQRP
240 ASLVQDTTSA ETPRGKSQIS TSSSQTPLLR WVLTLSFLLA TVAVGIYAM
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1069371
Mueller R.M.,Taguchi H.,Shibahara S.
Nucleotide sequence and organization of the rat heme oxygenase gene.
J. Biol. Chem.
262
6795-6802
1987
1069372
Shibahara S.,Mueller R.,Taguchi H.,Yoshida T.
Cloning and expression of cDNA for rat heme oxygenase.
Proc. Natl. Acad. Sci. U.S.A.
82
7865-7869
1985
1069373
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
1069374
Ishikawa K.,Sato M.,Yoshida T.
Expression of rat heme oxygenase in Escherichia coli as a catalytically active, full-length form that binds to bacterial membranes.
Eur. J. Biochem.
202
161-165
1991
1069375
McCoubrey W.K. Jr.,Ewing J.F.,Maines M.D.
Human heme oxygenase-2: characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal.
Arch. Biochem. Biophys.
295
13-20
1992
1069376
Lundby A.,Secher A.,Lage K.,Nordsborg N.B.,Dmytriyev A.,Lundby C.,Olsen J.V.
Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues.
Nat. Commun.
3
876-876
2012
1069377
Sugishima M.,Omata Y.,Kakuta Y.,Sakamoto H.,Noguchi M.,Fukuyama K.
Crystal structure of rat heme oxygenase-1 in complex with heme.
FEBS Lett.
471
61-66
2000
