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Information on EC 5.3.3.8 - DELTA3-DELTA2-enoyl-CoA isomerase and Organism(s) Homo sapiens
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5.3.3.8 DELTA3-DELTA2-enoyl-CoA isomeraseIUBMB 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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Word Map
- 5.3.3.8
-
beta-oxidation
- peroxisomal
- unsaturated
-
hydratase
-
auxiliary
-
2,4-dienoyl-coa
-
isomerization
-
oleic
-
odd-numbered
- 3-ketoacyl-coa
- crotonase
-
trifunctional
-
thiolase
-
protic
- d-3-hydroxyacyl-coa
-
4.2.1.17
-
1.3.1.34
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
eci1p, delta3,delta2-enoyl-coa isomerase, 3,2-trans-enoyl-coa isomerase, ateci3, ateci2, delta3-delta2-enoyl-coa isomerase, 3-cis-2-trans-enoyl-coa isomerase, 2,3-enoyl-coa isomerase, 3-2trans-enoyl-coa isomerase, d3,d2-enoyl-coa isomerase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,3-Enoyl-CoA isomerase
-
-
-
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3,2-trans-Enoyl-CoA isomerase
3-2trans-Enoyl-CoA isomerase
-
-
-
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3-cis-2-trans-Enoyl-CoA isomerase
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-
-
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Acetylene-allene isomerase
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-
-
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D3,D2-enoyl-CoA isomerase
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-
-
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DELTA3,DELTA2-enoyl-CoA isomerase
DELTA3-cis,DELTA2-trans-Enoyl-CoA isomerase
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-
-
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DELTA3-cis-DELTA2-trans-enoyl-CoA isomerase
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-
-
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Dodecenoyl-CoA delta-isomerase
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-
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dodecenoyl-CoA DELTA3-cis-DELTA2-trans-isomerase
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-
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ECI
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-
-
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Hepatocellular carcinoma-associated antigen 88
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-
-
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Isomerase, dodecenoyl coenzyme A Delta-
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-
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Long-chain DELTA3,DELTA2-enoyl-CoA isomerase
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-
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Short chain DELTA3,DELTA2-enoyl-CoA isomerase
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-
-
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3,2-trans-Enoyl-CoA isomerase
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-
-
-
DELTA3,DELTA2-enoyl-CoA isomerase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular oxidoreduction
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-
-
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isomerization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -, -, -, -, -, -, -, -
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
62213-29-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the velocity ratios with 3-trans-C6:C10:C12-enoyl-CoA is 1:2.1:1.2 for the liver enzyme and 1:3.4:2.3 for the heart enzyme
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-
?
additional information
?
-
-
the enzyme is essential for unsaturated fatty acid metabolism
-
?
additional information
?
-
-
involved in mitochondrial beta-oxidation of unsaturated fatty acids. Decreased levels of this enzyme in metastatic breast cancer cells might have impact on the aberrant behavior of cancer cells
-
-
?
additional information
?
-
involved in mitochondrial beta-oxidation of unsaturated fatty acids. Decreased levels of this enzyme in metastatic breast cancer cells might have impact on the aberrant behavior of cancer cells
-
-
?
additional information
?
-
catalyzes the transformation of 3-cis- and 3-trans-enoyl-CoA esters arising during the stepwise degradation of cis-, mono-, and polyunsaturated fatty acids to the 2-trans-enoyl-CoA intermediates
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-
?
additional information
?
-
-
catalyzes the transformation of 3-cis- and 3-trans-enoyl-CoA esters arising during the stepwise degradation of cis-, mono-, and polyunsaturated fatty acids to the 2-trans-enoyl-CoA intermediates
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme is essential for unsaturated fatty acid metabolism
-
?
additional information
?
-
-
involved in mitochondrial beta-oxidation of unsaturated fatty acids. Decreased levels of this enzyme in metastatic breast cancer cells might have impact on the aberrant behavior of cancer cells
-
-
?
additional information
?
-
involved in mitochondrial beta-oxidation of unsaturated fatty acids. Decreased levels of this enzyme in metastatic breast cancer cells might have impact on the aberrant behavior of cancer cells
-
-
?
additional information
?
-
catalyzes the transformation of 3-cis- and 3-trans-enoyl-CoA esters arising during the stepwise degradation of cis-, mono-, and polyunsaturated fatty acids to the 2-trans-enoyl-CoA intermediates
-
-
?
additional information
?
-
-
catalyzes the transformation of 3-cis- and 3-trans-enoyl-CoA esters arising during the stepwise degradation of cis-, mono-, and polyunsaturated fatty acids to the 2-trans-enoyl-CoA intermediates
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
catalytic activity of E136A variant below detection limit
additional information
-
catalytic activity of E136A variant below detection limit
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.3
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
at least 2 isoforms in liver: 1. monofunctional mitochondrial enzyme, 2. peroxisomal enzyme forming a part of a multifunctional enzyme
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-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
primary cultures of epithelial cells from breast cancer tissue samples
primary cultures of epithelial cells from breast cancer tissue samples
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at least 2 isoforms in liver: 1. monofunctional mitochondrial enzyme, 2. peroxisomal enzyme forming a part of a multifunctional enzyme
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
2,3-trans-enoyl-CoA isomerase is involved in mitochondrial beta-oxidation of unsaturated fatty acids
physiological function
the enzyme is involved in mitochondrial beta-oxidation of unsaturated fatty acids
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ECHM_HUMAN
290
0
31387
Swiss-Prot
Mitochondrion (Reliability: 1)
ECHP_HUMAN
723
0
79495
Swiss-Prot
Mitochondrion (Reliability: 5)
ECI1_HUMAN
302
0
32816
Swiss-Prot
Mitochondrion (Reliability: 2)
ECI2_HUMAN
394
0
43585
Swiss-Prot
Mitochondrion (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
70000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of DELTA3,DELTA2-enoyl-CoA isomerase complexed with the substrate analogue octanoyl-CoA has been refined a 1.3 angstrom resolution
sitting drop vapor diffusion method, using 100 mM MES pH 6.5, 1 M (NH4)2SO4
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
2,3-trans-enoyl-CoA isomerase expression is decreased in metastatic breast cancer tissue
dodecenoyl-coenzyme A DELTA isomerase mRNA in omental fat depots from normal and obese individuals demonstrates a 1.6fold underexpression in obese patients
expression of 2,3-trans-enoyl-CoA isomerase is decreased in metastatic tumor tissue
the level of 2,3-trans-enoyl-CoA isomerase is decreased in metastatic breast cancer
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
decreased levels of 2,3-trans-enoyl-CoA isomerase might have impact on the aberrant behaviour of cancer cells
medicine
enzyme is involved in controlling host metabolic reprogramming during hepatitis C virus infection. Hepatitis C virus growth and RNA replication in hepatoma cell lines stably expressing dodecenoyl coenzyme A delta isomerase-targeting short hairpin RNA (shRNA) are abrogated, indicating that dodecenoyl coenzyme A delta isomerase is required for productive infection. Pharmacologic inhibition of fatty acid oxidation also blocks hepatitis C virus replication. Production of infectious hepatitis C virus is restored by overexpression of an shRNA-resistant dodecenoyl coenzyme A delta isomerase allele
medicine
in primary cultures of epithelial cells from 23 breast cancer tissue samples, nucleophosmin is increased in the group with metastases. The levels of 2,3-trans-enoyl-CoA isomerase and glutathione peroxidase 1 are decreased
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Palossari, P.M.; Kilponen, J.M.; Sormunen, R.T.; Hassinen, I.E.; Hiltunen, J.K.
DELTA3,DELTA2-Enoyl-CoA isomerases. Characterization of the mitochondrial isoenzyme in the rat
J. Biol. Chem.
265
3347-3353
1990
Bos taurus, Homo sapiens, Rattus norvegicus, Sus scrofa
Kilponen, J.M.; Hyrinen, H.M.; Rehn, M.; Hiltunen, J.K.
cDNA cloning and amino acid sequence of human mitochondrial DELTA3DELTA2-enoyl-CoA isomerase: comparison of the human enzyme with its rat counterpart, mitochondrial short-chain isomerase
Biochem. J.
300
1-5
1994
Homo sapiens
Takahashi, Y.; Hirata, Y.; Burstein, Y.; Listowsky, I.
DELTA3,DELTA2-enoyl-CoA isomerase is the protein that copurifies with human glutathione S-transferase from S-hexylglutathione affinity matrices
Biochem. J.
304
849-852
1994
Homo sapiens
Kilponen, J.M.; Hiltunen, J.K.
beta-Oxidation of unsaturated fatty acids in humans. Isoforms of DELTA3,DELTA2-enoyl-CoA isomerase
FEBS Lett.
322
299-303
1993
Homo sapiens
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
Partanen, S.T.; Novikov, D.K.; Popov, A.N.; Mursula, A.M.; Hiltunen, J.K.; Wierenga, R.K.
The 1.3 A crystal structure of human mitochondrial DELTA3-DELTA2-enoyl-CoA isomerase shows a novel mode of binding for the fatty acyl group
J. Mol. Biol.
342
1197-1208
2004
Homo sapiens (P42126), Homo sapiens
Vydra, J.; Selicharova, I.; Smutna, K.; Sanda, M.; Matouskova, E.; Burskova, E.; Prchalova, M.; Velenska, Z.; Coufal, D.; Jiracek, J.
Two-dimensional electrophoretic comparison of metastatic and non-metastatic human breast tumors using in vitro cultured epithelial cells derived from the cancer tissues
BMC Cancer
8
107
2008
Homo sapiens, Homo sapiens (P42126)
Walewski, J.L.; Ge, F.; Gagner, M.; Inabnet, W.B.; Pomp, A.; Branch, A.D.; Berk, P.D.
Adipocyte accumulation of long-chain fatty acids in obesity is multifactorial, resulting from increased fatty acid uptake and decreased activity of genes involved in fat utilization
Obes. Surg.
20
93-107
2010
Homo sapiens (P42126), Homo sapiens
Rasmussen, A.L.; Diamond, D.L.; McDermott, J.E.; Gao, X.; Metz, T.O.; Matzke, M.M.; Carter, V.S.; Belisle, S.E.; Korth, M.J.; Waters, K.M.; Smith, R.D.; Katze, M.G.
Systems virology identifies a mitochondrial fatty acid oxidation enzyme, dodecenoyl coenzyme A delta isomerase, required for hepatitis C virus replication and likely pathogenesis
J. Virol.
85
11646-11654
2011
Hepacivirus C, Homo sapiens (P42126)
Vydra, J.; Selicharova, I.; Smutna, K.; Sanda, M.; Matouskova, E.; Burskova, E.; Prchalova, M.; Velenska, Z.; Coufal, D.; Jiracek, J.
Two-dimensional electrophoretic comparison of metastatic and non-metastatic human breast tumors using in vitro cultured epithelial cells derived from the cancer tissues
BMC Cancer
8
107
2008
Homo sapiens (P42126), Homo sapiens
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