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Information on EC 5.3.3.8 - DELTA3-DELTA2-enoyl-CoA isomerase and Organism(s) Mus musculus and UniProt Accession Q78JN3

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EC Tree
     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.3 Transposing C=C bonds
                5.3.3.8 DELTA3-DELTA2-enoyl-CoA isomerase
IUBMB Comments
The enzyme participates in the beta-oxidation of fatty acids with double bonds at an odd position. Processing of these substrates via the beta-oxidation system results in intermediates with a cis- or trans-double bond at position C3, which cannot be processed further by the regular enzymes of the beta-oxidation system. This enzyme isomerizes the bond to a trans bond at position C2, which can be processed further. The reaction rate is ten times higher for the (3Z) isomers than for (3E) isomers. The enzyme can also catalyse the isomerization of 3-acetylenic fatty acyl thioesters to 2,3-dienoyl fatty acyl thioesters.
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Mus musculus
UNIPROT: Q78JN3
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The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Synonyms
eci1p, delta3,delta2-enoyl-coa isomerase, 3,2-trans-enoyl-coa isomerase, ateci3, ateci2, delta3-delta2-enoyl-coa isomerase, d3,d2-enoyl-coa isomerase, ateci1, 3-cis-2-trans-enoyl-coa isomerase, 2,3-enoyl-coa isomerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA3,DELTA2-enoyl-CoA isomerase
-
Eci3
isoform
2,3-Enoyl-CoA isomerase
-
-
-
-
3,2-trans-Enoyl-CoA isomerase
-
-
-
-
3-2trans-Enoyl-CoA isomerase
-
-
-
-
3-cis-2-trans-Enoyl-CoA isomerase
-
-
-
-
Acetylene-allene isomerase
-
-
-
-
D3,D2-enoyl-CoA isomerase
-
-
-
-
DELTA3,DELTA2-enoyl-CoA isomerase
DELTA3-cis,DELTA2-trans-Enoyl-CoA isomerase
-
-
-
-
DELTA3-cis-DELTA2-trans-enoyl-CoA isomerase
-
-
-
-
Dodecenoyl-CoA delta-isomerase
-
-
-
-
dodecenoyl-CoA DELTA3-cis-DELTA2-trans-isomerase
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-
-
-
ECI
-
-
-
-
Hepatocellular carcinoma-associated antigen 88
-
-
-
-
Isomerase, dodecenoyl coenzyme A Delta-
-
-
-
-
Long-chain DELTA3,DELTA2-enoyl-CoA isomerase
-
-
-
-
PECI
-
-
Short chain DELTA3,DELTA2-enoyl-CoA isomerase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
-
-
-
intramolecular oxidoreduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(3Z/3E)-alk-3-enoyl-CoA (2E)-isomerase
The enzyme participates in the beta-oxidation of fatty acids with double bonds at an odd position. Processing of these substrates via the beta-oxidation system results in intermediates with a cis- or trans-double bond at position C3, which cannot be processed further by the regular enzymes of the beta-oxidation system. This enzyme isomerizes the bond to a trans bond at position C2, which can be processed further. The reaction rate is ten times higher for the (3Z) isomers than for (3E) isomers. The enzyme can also catalyse the isomerization of 3-acetylenic fatty acyl thioesters to 2,3-dienoyl fatty acyl thioesters.
CAS REGISTRY NUMBER
COMMENTARY hide
62213-29-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3Z)-nonenoyl CoA
(2Z)-nonenoyl CoA
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
kidney-specific expression
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ECI3_MOUSE
317
0
35231
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39400
-
x * 39400, calculation from nucleotide sequence
75000
-
multifunctional enzyme with activity of EC 5.3.3.8, EC 4.2.1.17 and EC 1.1.1.35, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 39400, calculation from nucleotide sequence
monomer
-
1 * 75000, multifunctional enzyme with activity of EC 5.3.3.8, EC 4.2.1.17 and EC 1.1.1.35, SDS-PAGE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stark, A.; Meijer, J.
Purification and characterization of a multifunctional enzyme from mouse liver peroxisomes
Comp. Biochem. Physiol. B
108
471-480
1994
Mus musculus
Manually annotated by BRENDA team
Stoffel, W.; Duker, M.; Hofmann, K.
Molecular cloning and gene organization of the mouse mitochondrial 3,2-trans-enoyl-CoA isomerase
FEBS Lett.
333
119-122
1993
Mus musculus
Manually annotated by BRENDA team
Geisbrecht, B.V.; Zhang, D.; Schulz, H.; Gould, S.J.
Characterization of PECI, a novel monofunctional DELTA(3),DELTA(2)-enoyl-CoA isomerase of mammalian peroxisomes
J. Biol. Chem.
274
21797-21803
1999
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Van Weeghel, M.; Ofman, R.; Argmann, C.; Ruiter, J.; Claessen, N.; Oussoren, S.; Wanders, R.; Aten, J.; Houten, S.
Identification and characterization of Eci3, a murine kidney-specific DELTA3,DELTA2-enoyl-CoA isomerase
FASEB J.
28
1365-1374
2014
Rattus norvegicus, Mus musculus (Q78JN3)
Manually annotated by BRENDA team