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Information on EC 5.1.2.3 - 3-hydroxybutyryl-CoA epimerase
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5.1.2.3 3-hydroxybutyryl-CoA epimeraseSpecify your search results
Word Map
- 5.1.2.3
-
beta-oxidation
-
polyunsaturated
- unsaturated
-
2,4-dienoyl-coa
-
multienzyme
-
5.3.3.8
-
hydratase
- linoleate
- peroxisomal
-
thiolase
- acyl-coa
-
auxiliary
-
even-numbered
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
3-Hydroxyacyl-coenzyme A epimerase, 3-Hydroxybutyryl coenzyme A epimerase, Epimerase, 3-hydroxybutyryl coenzyme A, TFP, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-Hydroxyacyl-coenzyme A epimerase
-
-
-
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3-Hydroxybutyryl coenzyme A epimerase
-
-
-
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Epimerase, 3-hydroxybutyryl coenzyme A
-
-
-
-
TFP
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trifunctional beta-oxidation protein with activities of EC 1.1.1.35, EC 4.2.1.17 and EC 5.1.2.3
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-3-Hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA
Rattus norvegicus
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-
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(S)-3-Hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA
Escherichia coli
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
epimerization
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
3-hydroxybutanoyl-CoA 3-epimerase
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CAS REGISTRY NUMBER
COMMENTARY
9024-21-9
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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
D-3-Hydroxydodecanoyl-CoA
L-3-Hydroxydodecanoyl-CoA
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-
-
-
?
additional information
?
-
-
3-hydroxyacyl-CoA epimerase activity as a part of a system capable of degrading products formed as a result of Gram-negative bacterial infections. In addition the enzyme may play a role in the metabolism of leukotrienes, specifically 5(S)-hydroxy-6,8,11,14-eicosatetraenoic acid, i.e. the 5-lipoxygenase oxidation product of arachidonic acid
-
-
?
additional information
?
-
-
enzyme may not be involved in the beta-oxidation of unsaturated fatty acids at all
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-
?
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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
?
-
-
3-hydroxyacyl-CoA epimerase activity as a part of a system capable of degrading products formed as a result of Gram-negative bacterial infections. In addition the enzyme may play a role in the metabolism of leukotrienes, specifically 5(S)-hydroxy-6,8,11,14-eicosatetraenoic acid, i.e. the 5-lipoxygenase oxidation product of arachidonic acid
-
-
?
additional information
?
-
-
enzyme may not be involved in the beta-oxidation of unsaturated fatty acids at all
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Tris(hydroxymethyl)aminomethane
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remains active in presence of potassium phosphate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52.4
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3-hydroxyacyl-CoA epimerase activity of the trifunctional beta-oxidation protein
additional information
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
and mutant with a multienzyme complex with a defective L-3-hydroxyacyl-CoA dehydrogenase, EC 1.1.1.35, fadB64
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (8259 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
365000
-
trifunctional beta-oxidation protein with activities of EC 1.1.1.35, EC 4.2.1.17 and EC 5.1.2.3, gel filtration
42000
73000
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multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, EC 1.1.1.35, and EC 5.3.3.3, 2 * 42000 + 2 * 73000, SDS-PAGE
78000
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multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, and EC 5.3.3.3, 2 * 42000 + 2 * 78000, SDS-PAGE
79047
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multifunctional enzyme which exhibits activities of EC 4.2.1.17, EC 1.1.1.211, EC 5.3.3.8 and EC 5.1.2.3, 1 * 79047, calculation from nucleotide sequence, monomeric protein exhibiting all 4 activities
93000
additional information
42000
-
multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, EC 1.1.1.35, and EC 5.3.3.3, 2 * 42000 + 2 * 73000, SDS-PAGE
42000
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multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, and EC 5.3.3.3, 2 * 42000 + 2 * 78000, SDS-PAGE
93000
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trifunctional enzyme which exhibits activities of EC 5.1.2.3, EC 4.2.1.17, and EC 1.1.1.35, 4 * 93000, SDS-PAGE, each subunit of the tetrameric protein consists of at least two large domains, the amino-terminal one possessing activities of EC 4.2.1.17 and EC 1.1.1.35 and the carboxy-terminal one bearing activity of EC 5.1.2.3
93000
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4 * 93000, trifunctional beta-oxidation protein with activities of EC 1.1.1.35, EC 4.2.1.17 and EC 5.1.2.3, SDS-PAGE
additional information
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trifunctional enzyme which exhibits activities of EC 5.1.2.3, EC 4.2.1.17, and EC 1.1.1.35, MW 365000, gel filtration 1
additional information
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multifunctional enzyme which exhibits activities of EC 4.2.1.17, EC 1.1.1.211, EC 5.3.3.8 and EC 5.1.2.3, MW 79047, calculation from nucleotide sequence
additional information
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multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, and EC 5.3.3.3, MW 260000, native PAGE, gel filtration
additional information
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multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, EC 1.1.1.35, and EC 5.3.3.3 has a MW of 240000, gel filtration
additional information
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trimeric form of the multienzyme complex which exhibits activities of EC 5.1.2.3, EC 5.3.3.3, EC 4.2.1.17, EC 1.1.1.35, and EC 2.3.1.16 has MW of 820000, native PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
-
4 * 93000, trifunctional beta-oxidation protein with activities of EC 1.1.1.35, EC 4.2.1.17 and EC 5.1.2.3, SDS-PAGE
additional information
additional information
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multifunctional enzyme which exhibits activities of EC 4.2.1.17, EC 1.1.1.211, EC 5.3.3.8 and EC 5.1.2.3, 1 * 79047, calculation from nucleotide sequence, monomeric protein exhibiting all 4 activities
additional information
-
multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, and EC 5.3.3.3, 2 * 42000 + 2 * 78000, SDS-PAGE
additional information
-
multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, and EC 5.3.3.3, 2 * 42000 + 2 * 78000, SDS-PAGE
additional information
Escherichia coli B / ATCC 11303
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multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, and EC 5.3.3.3, 2 * 42000 + 2 * 78000, SDS-PAGE
-
additional information
-
trifunctional enzyme which exhibits activities of EC 5.1.2.3, EC 4.2.1.17, and EC 1.1.1.35, 4 * 93000, SDS-PAGE, each subunit of the tetrameric protein consists of at least two large domains, the amino-terminal one possessing activities of EC 4.2.1.17 and EC 1.1.1.35 and the carboxy-terminal one bearing activity of EC 5.1.2.3
additional information
-
trifunctional enzyme which exhibits activities of EC 5.1.2.3, EC 4.2.1.17, and EC 1.1.1.35, 4 * 93000, SDS-PAGE, each subunit of the tetrameric protein consists of at least two large domains, the amino-terminal one possessing activities of EC 4.2.1.17 and EC 1.1.1.35 and the carboxy-terminal one bearing activity of EC 5.1.2.3
additional information
-
multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, EC 1.1.1.35, and EC 5.3.3.3, 2 * 42000 + 2 * 73000, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
lipoprotein
lipoprotein
-
the multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, and EC 5.3.3.3, contains 63 nmol of lipid phosphate per mg of protein
lipoprotein
-
the multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, and EC 5.3.3.3, contains phospholipid
lipoprotein
Escherichia coli B / ATCC 11303
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the multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, and EC 5.3.3.3, contains 63 nmol of lipid phosphate per mg of protein
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lipoprotein
Escherichia coli B / ATCC 11303
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the multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, and EC 5.3.3.3, contains phospholipid
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G116F
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both the enoyl-CoA hydratase activity, EC 4.2.1.17 and the 3-hydroxyacyl-CoA epimerase activity, EC 5.1.2.3 are eliminated by the site-directed mutation alpha/Gly116 to Phe. This provides direct evidence that both enzymes are associated with a common active site on the amino-terminal domain of the multifunctional enzyme complex which exhibits the activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, EC 1.1.1.35, and EC 5.3.3.3
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, and EC 5.3.3.3, is stable for months when stored in 0.2 M potassium phosphate, pH 6.6, containing 25% v/v glycerol and 10 mM mercaptoethanol
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, EC 1.1.1.35, and EC 5.3.3.3
multifunctional enzyme which exhibits activities of EC 4.2.1.17, EC 1.1.1.211, EC 5.3.3.8 and EC 5.1.2.3
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multifunctional enzyme with domain structure. Isolation of fragments containing single enzyme activities provide evidence for hinge regions
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trifunctional beta-oxidation protein with activities of EC 1.1.1.35, EC 4.2.1.17 and EC 5.1.2.3
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trifunctional enzyme possessing activities of EC 5.1.2.3, EC 1.1.1.35, and EC 4.2.1.17
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multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, EC 1.1.1.35, and EC 5.3.3.3
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multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, EC 1.1.1.35, and EC 5.3.3.3
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli, multifunctional enzyme which exhibits activities of EC 4.2.1.17, EC 1.1.1.211, EC 5.3.3.8 and EC 5.1.2.3
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pramanik, A.; Pawar, S.; Antonian, E.; Schulz, H.
Five different enzymatic activities are associated with the multienzyme complex of fatty acid oxidation from Escherichia coli
J. Bacteriol.
137
469-473
1979
Escherichia coli
brenda
Pawar, S.; Schulz, H.
The structure of the multienzyme complex of fatty acid oxidation from Escherichia coli
J. Biol. Chem.
256
3894-3899
1981
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Pramanik, A.; Schulz, H.
Multienzyme complexes of fatty acid oxidation from Escherichia coli K-12 and from a mutant with a defective L-3-hydroxyacyl coenzyme A dehydrogenase
Biochim. Biophys. Acta
750
41-46
1983
Escherichia coli
brenda
Yang, S.Y.; Li, J.; He, X.Y.; Cosloy, S.D.; Schulz, H.
Evidence that the fadB gene of the fadAB operon of Escherichia coli encodes 3-hydroxyacyl-coenzyme A (CoA) epimerase, DELTA3-cis-DELTA2-trans-enoyl-CoA isomerase, and enoyl-CoA hydratase in addition to 3-hydroxyacyl-CoA dehydrogenase
J. Bacteriol.
170
2543-2548
1988
Escherichia coli
brenda
Smeland, T.E.; Li, J.; Chu, C.h.; Cuebas, D.; Schulz, H.
The 3-hydroxyacyl-CoA epimerase activity of rat liver peroxisomes is due to the combined actions of two enoyl-CoA hydratases: a revision of the epimerase-dependent pathway of unsaturated fatty acid oxidation
Biochem. Biophys. Res. Commun.
160
988-992
1989
Rattus norvegicus
brenda
Hiltunen, J.K.; Kunau, W.H.
Epimerization of 3-hydroxyacyl-CoA esters as an auxiliary reaction in the beta-oxidation of unsaturated fatty acids
Prog. Clin. Biol. Res.
321
265-272
1990
Yarrowia lipolytica, Candida tropicalis, Cucumis sativus, Escherichia coli, Neurospora crassa, Rattus norvegicus
brenda
Imamura, S.; Ueda, S.; Mizugaki, M.; Kawaguchi, A.
Purification of the multienzyme complex for fatty acid oxidation from Pseudomonas fragi and reconstitution of the fatty acid oxidation system
J. Biochem.
107
184-189
1990
Pseudomonas fragi
brenda
Smeland, T.E.; Cuebas, D.; Schulz, H.
Epimerization of 3-hydroxy-4-trans-decenoyl coenzyme A by a dehydration/hydration mechanism catalyzed by the multienzyme complex of fatty acid oxidation from Escherichia coli
J. Biol. Chem.
266
23904-23908
1991
Escherichia coli
brenda
Smeland, T.E.; Li, J.; Cuebas, D.; Schulz, H.
The mechanism and function of 3-hydroxyacyl-CoA epimerase in rat liver and Escherichia coli
Prog. Clin. Biol. Res.
375
85-93
1992
Yarrowia lipolytica, Candida tropicalis, Cucumis sativus, Escherichia coli, Gram-negative bacteria, Mammalia, Neurospora crassa, Pseudomonas fragi, Rattus norvegicus
brenda
Yang, S.Y.; Elzinga, M.
Association of both enoyl coenzyme A hydratase and 3-hydroxyacyl coenzyme A epimerase with an active site in the amino-terminal domain of the multifunctional fatty acid oxidation protein from Escherichia coli
J. Biol. Chem.
268
6588-6592
1993
Escherichia coli
brenda
Guhnemann-Schfer, K.; Engeland, K.; Linder, D.; Kindl, H.
Evidence for domain structures of the trifunctional protein and the tetrafunctional protein acting in glyoxysomal fatty acid beta-oxidation
Eur. J. Biochem.
226
909-915
1994
Cucumis sativus
brenda
Preisig-Muller, R.; Guhnemann-Schfer, K.; Kindl, H.
Domains of the tetrafunctional protein acting in glyoxysomal fatty acid beta-oxidation
J. Biol. Chem.
269
20475-20481
1994
Cucumis sativus
brenda
Thieringer, R.; Kunau, W.H.
beta-Oxidation system of the filamentous fungus Neurospora crassa. Structural characterization of the trifunctional protein
J. Biol. Chem.
266
13118-13123
1991
Neurospora crassa
brenda
Thieringer, R.; Kunau, W.H.
The beta-oxidation system in catalase-free microbodies of the filamentous fungus Neurospora crassa. Purification of a multifunctional protein possessing 2-enoyl-CoA hydratase, L-3-hydroxyacyl-CoA dehydrogenase, and 3-hydroxyacyl-CoA epimerase activities
J. Biol. Chem.
266
13110-13117
1991
Neurospora crassa
brenda
Binstock, J.F.; Schulz, H.
Fatty acid oxidation complex from Escherichia coli
Methods Enzymol.
71
403-411
1981
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
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