Sequence of ACOX1_RAT
EC Number:1.3.3.6
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
acyl-CoA + O2 = trans-2,3-dehydroacyl-CoA + H2O2
Other sequences found for EC No. 1.3.3.6
General information:
Sequence
0 MNPDLRKERA SATFNPELIT HILDGSPENT RRRREIENLI LNDPDFQHED YNFLTRSQRY
60 EVAVKKSATM VKKMREYGIS DPEEIMWFKK LYLANFVEPV GLNYSMFIPT LLNQGTTAQQ
120 EKWMRPSQEL QIIGTYAQTE MGHGTHLRGL ETTATYDPKT QEFILNSPTV TSIKWWPGGL
180 GKTSNHAIVL AQLITQGECY GLHAFVVPIR EIGTHKPLPG ITVGDIGPKF GYEEMDNGYL
240 KMDNYRIPRE NMLMKYAQVK PDGTYVKPLS NKLTYGTMVF VRSFLVGNAA QSLSKACTIA
300 IRYSAVRRQS EIKQSEPEPQ ILDFQTQQYK LFPLLATAYA FHFVGRYMKE TYLRINESIG
360 QGDLSELPEL HALTAGLKAF TTWTANAGIE ECRMACGGHG YSHSSGIPNI YVTFTPACTF
420 EGENTVMMLQ TARFLMKIYD QVRSGKLVGG MVSYLNDLPS QRIQPQQVAV WPTMVDINSL
480 EGLTEAYKLR AARLVEIAAK NLQTHVSHRK SKEVAWNLTS VDLVRASEAH CHYVVVKVFS
540 DKLPKIQDKA VQAVLRNLCL LYSLYGISQK GGDFLEGSII TGAQLSQVNA RILELLTLIR
600 PNAVALVDAF DFKDMTLGSV LGRYDGNVYE NLFEWAKKSP LNKTEVHESY HKHLKPLQSK
660 L
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1854
Miyazawa S.,Hayashi H.,Hijikata M.,Ishii N.,Furuta S.,Kagamiyama H.,Osumi T.,Hashimoto T.
Complete nucleotide sequence of cDNA and predicted amino acid sequence of rat acyl-CoA oxidase.
J. Biol. Chem.
262
8131-8137
1987
1855
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
1856
Osumi T.,Ishii N.,Miyazawa S.,Hashimoto T.
Isolation and structural characterization of the rat acyl-CoA oxidase gene.
J. Biol. Chem.
262
8138-8143
1987
1857
Kawaguchi A.,Tsubotani S.,Seyama Y.,Yamakawa T.,Osumi T.,Hashimoto T.,Kikuchi T.,Ando M.,Okuda S.
Stereochemistry of dehydrogenation catalyzed by Acyl-CoA oxidase.
J. Biochem.
88
1481-1486
1980
1858
Van Veldhoven P.P.,Vanhove G.,Assselberghs S.,Eyssen H.J.,Mannaerts G.P.
Substrate specificities of rat liver peroxisomal acyl-CoA oxidases: palmitoyl-CoA oxidase (inducible acyl-CoA oxidase), pristanoyl-CoA oxidase (non-inducible acyl-CoA oxidase), and trihydroxycoprostanoyl-CoA oxidase.
J. Biol. Chem.
267
20065-20074
1992
1859
Setoyama C.,Tamaoki H.,Nishina Y.,Shiga K.,Miura R.
Functional expression of two forms of rat acyl-CoA oxidase and their substrate specificities.
Biochem. Biophys. Res. Commun.
217
482-487
1995
1860
Chung H.L.,Wangler M.F.,Marcogliese P.C.,Jo J.,Ravenscroft T.A.,Zuo Z.,Duraine L.,Sadeghzadeh S.,Li-Kroeger D.,Schmidt R.E.,Pestronk A.,Rosenfeld J.A.,Burrage L.,Herndon M.J.,Chen S.,Shillington A.,Vawter-Lee M.,Hopkin R.,Rodriguez-Smith J.,Henrickson M.,Lee B.,Moser A.B.,Jones R.O.,Watkins P.,Yoo T.,Mar S.,Choi M.,Bucelli R.C.,Yamamoto S.,Lee H.K.,Prada C.E.,Chae J.H.,Vogel T.P.,Bellen H.J.
Loss- or Gain-of-Function Mutations in ACOX1 Cause Axonal Loss via Different Mechanisms.
Neuron
106
0-0
2020
1861
Nakajima Y.,Miyahara I.,Hirotsu K.,Nishina Y.,Shiga K.,Setoyama C.,Tamaoki H.,Miura R.
Three-dimensional structure of the flavoenzyme acyl-CoA oxidase-II from rat liver, the peroxisomal counterpart of mitochondrial acyl-CoA dehydrogenase.
J. Biochem.
131
365-374
2002
1862
Tokuoka K.,Nakajima Y.,Hirotsu K.,Miyahara I.,Nishina Y.,Shiga K.,Tamaoki H.,Setoyama C.,Tojo H.,Miura R.
Three-dimensional structure of rat-liver acyl-CoA oxidase in complex with a fatty acid: insights into substrate-recognition and reactivity toward molecular oxygen.
J. Biochem.
139
789-795
2006
