Sequence of ECHM_RAT
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
EC Number:5.3.3.21
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
a (3E,5Z)-alka-3,5-dienoyl-CoA = a (2E,4E)-alka-2,4-dienoyl-CoA
Other sequences found for EC No. 5.3.3.21
General information:
Sequence
0 MAALRALLPR ACNSLLSPVR CPEFRRFASG ANFQYIITEK KGKNSSVGLI QLNRPKALNA
60 LCNGLIEELN QALETFEEDP AVGAIVLTGG EKAFAAGADI KEMQNRTFQD CYSGKFLSHW
120 DHITRIKKPV IAAVNGYALG GGCELAMMCD IIYAGEKAQF GQPEILLGTI PGAGGTQRLT
180 RAVGKSLAME MVLTGDRISA QDAKQAGLVS KIFPVETLVE EAIQCAEKIA NNSKIIVAMA
240 KESVNAAFEM TLTEGNKLEK KLFYSTFATD DRREGMSAFV EKRKANFKDH
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
793166
Minami-Ishii N.,Taketani S.,Osumi T.,Hashimoto T.
Molecular cloning and sequence analysis of the cDNA for rat mitochondrial enoyl-CoA hydratase. Structural and evolutionary relationships linked to the bifunctional enzyme of the peroxisomal beta-oxidation system.
Eur. J. Biochem.
185
73-78
1989
793167
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
793168
Mueller-Newen G.,Janssen U.,Stoffel W.
Enoyl-CoA hydratase and isomerase form a superfamily with a common active-site glutamate residue.
Eur. J. Biochem.
228
68-73
1995
793169
Kiema T.R.,Engel C.K.,Schmitz W.,Filppula S.A.,Wierenga R.K.,Hiltunen J.K.
Mutagenic and enzymological studies of the hydratase and isomerase activities of 2-enoyl-CoA hydratase-1.
Biochemistry
38
2991-2999
1999
793170
Engel C.K.,Mathieu M.,Zeelen J.P.,Hiltunen J.K.,Wierenga R.K.
Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5-A resolution: a spiral fold defines the CoA-binding pocket.
EMBO J.
15
5135-5145
1996
793171
Engel C.K.,Kiema T.R.,Hiltunen J.K.,Wierenga R.K.
The crystal structure of enoyl-CoA hydratase complexed with octanoyl-CoA reveals the structural adaptations required for binding of a long chain fatty acid-CoA molecule.
J. Mol. Biol.
275
847-859
1998
793172
Bahnson B.J.,Anderson V.E.,Petsko G.A.
Structural mechanism of enoyl-CoA hydratase: three atoms from a single water are added in either an E1cb stepwise or concerted fashion.
Biochemistry
41
2621-2629
2002
793173
Bell A.F.,Feng Y.,Hofstein H.A.,Parikh S.,Wu J.,Rudolph M.J.,Kisker C.,Whitty A.,Tonge P.J.
Stereoselectivity of enoyl-CoA hydratase results from preferential activation of one of two bound substrate conformers.
Chem. Biol.
9
1247-1255
2002
