Sequence of ECHP_RAT
EC Number:1.1.1.35
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
Other sequences found for EC No. 1.1.1.35
EC Number:4.2.1.17
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H2O
Other sequences found for EC No. 4.2.1.17
EC Number:5.3.3.8
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
a (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA
Other sequences found for EC No. 5.3.3.8
General information:
Sequence
0 MAEYLRLPHS LAMIRLCNPP VNAVSPTVIR EVRNGLQKAG SDHTVKAIVI CGANGNFCAG
60 ADIHGFSAFT PGLALGSLVD EIQRYQKPVL AAIQGVALGG GLELALGCHY RIANAKARVG
120 LPEVTLGILP GARGTQLLPR VVGVPVALDL ITSGKYLSAD EALRLGILDA VVKSDPVEEA
180 IKFAQKIIDK PIEPRRIFNK PVPSLPNMDS VFAEAIAKVR KQYPGVLAPE TCVRSIQASV
240 KHPYEVGIKE EEKLFMYLRA SGQAKALQYA FFAEKSANKW STPSGASWKT ASAQPVSSVG
300 VLGLGTMGRG IAISFARVGI SVVAVESDPK QLDAAKKIIT FTLEKEASRA HQNGQASAKP
360 KLRFSSSTKE LSTVDLVVEA VFEDMNLKKK VFAELSALCK PGAFLCTNTS ALNVDDIASS
420 TDRPQLVIGT HFFSPAHVMR LLEVIPSRYS SPTTIATVMS LSKKIGKIGV VVGNCYGFVG
480 NRMLAPYYNQ GFFLLEEGSK PEDVDGVLEE FGFKMGPFRV SDLAGLDVGW KIRKGQGLTG
540 PSLPPGTPVR KRGNSRYSPL GDMLCEAGRF GQKTGKGWYQ YDKPLGRIHK PDPWLSTFLS
600 QYREVHHIEQ RTISKEEILE RCLYSLINEA FRILEEGMAA RPEHIDVIYL HGYGWPRHKG
660 GPMFYAASVG LPTVLEKLQK YYRQNPDIPQ LEPSDYLRRL VAQGSPPLKE WQSLAGPHGS
720 KL
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
793202
Osumi T.,Ishii N.,Hijikata M.,Kamijo K.,Ozasa H.,Furuta S.,Miyazawa S.,Kondo K.,Inoue K.,Kagamiyama H.,Hashimoto T.
Molecular cloning and nucleotide sequence of the cDNA for rat peroxisomal enoyl-CoA: hydratase-3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme.
J. Biol. Chem.
260
8905-8910
1985
793203
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
793204
Ishii N.,Hijikata M.,Osumi T.,Hashimoto T.
Structural organization of the gene for rat enoyl-CoA hydratase:3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme.
J. Biol. Chem.
262
8144-8150
1987
793205
Dieuaide-Noubhani M.,Novikov D.,Baumgart E.,Vanhooren J.C.T.,Fransen M.,Goethals M.,Vandekerckhove J.,Van Veldhoven P.P.,Mannaerts G.P.
Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver. Relationship between the different dehydrogenases and evidence that fatty acids and the C27 bile acids di- and tri-hydroxycoprostanic acids are metabolized by separate multifunctional proteins.
Eur. J. Biochem.
240
660-666
1996
793206
Palosaari P.M.,Hiltunen J.K.
Peroxisomal bifunctional protein from rat liver is a trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities.
J. Biol. Chem.
265
2446-2449
1990
793207
Kiema T.R.,Taskinen J.P.,Pirilae P.L.,Koivuranta K.T.,Wierenga R.K.,Hiltunen J.K.
Organization of the multifunctional enzyme type 1: interaction between N- and C-terminal domains is required for the hydratase-1/isomerase activity.
Biochem. J.
367
433-441
2002
793208
Zhang D.,Yu W.,Geisbrecht B.V.,Gould S.J.,Sprecher H.,Schulz H.
Functional characterization of delta3,delta2-enoyl-CoA isomerases from rat liver.
J. Biol. Chem.
277
9127-9132
2002
793209
Kasaragod P.,Schmitz W.,Hiltunen J.K.,Wierenga R.K.
The isomerase and hydratase reaction mechanism of the crotonase active site of the multifunctional enzyme (type-1), as deduced from structures of complexes with 3S-hydroxy-acyl-CoA.
FEBS J.
280
3160-3175
2013
793210
Taskinen J.P.,Kiema T.R.,Hiltunen J.K.,Wierenga R.K.
Structural studies of MFE-1: the 1.9 A crystal structure of the dehydrogenase part of rat peroxisomal MFE-1.
J. Mol. Biol.
355
734-746
2006
