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Information on EC 4.2.1.119 - enoyl-CoA hydratase 2 and Organism(s) Candida tropicalis and UniProt Accession P22414
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4.2.1.119 enoyl-CoA hydratase 2IUBMB Comments
This enzyme catalyses a hydration step in peroxisomal beta-oxidation. The human multifunctional enzyme type 2 (MFE-2) is a 79000 Da enzyme composed of three functional units: (3R)-hydroxyacyl-CoA dehydrogenase, 2-enoyl-CoA hydratase 2 and sterol carrier protein 2-like units . The enzymes from Aeromonas caviae and Arabidopsis thaliana are monofunctional enzymes. 2-Enoyl-CoA hydratase 3 from Candida tropicalis is a part from multifunctional enzyme type 2 .
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Word Map
- 4.2.1.119
-
beta-oxidation
- enoyl-coas
- polyhydroxyalkanoate
- mfe-2s
- trans-2-enoyl-coa
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r-3-hydroxyacyl-coas
- aconitate
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phajs
- caviae
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3r-hydroxyacyl-coa
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even-numbered
- biotechnology
The taxonomic range for the selected organisms is: Candida tropicalis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
hydratase 2, multifunctional enzyme type 2, phaj1, phaj4, atech2, enoyl-coa hydratase 2, phaj1pp, phaj1pa, r-hydratase, phajyb4, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-enoyl-CoA hydratase 2
MFE-2
Mfe2p [CtMfe2p(dha+bdelta)]
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2-enoyl-CoA hydratase 2 domain of Candida tropicalis
multifunctional enzyme type 2
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(3R)-hydroxyacyl-CoA dehydrogenase/2-enoyl-CoA hydratase 2
2-enoyl-CoA hydratase 2
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domain of multifunctional enzyme type 2 (MFE-2), (3R)-hydroxyacyl-CoA dehydrogenase/2-enoyl-CoA hydratase 2
MFE-2
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multifunctional enzyme with 2-enoyl-CoA hydratase 2 activity and 2/(3R)-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.36) activity
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(3R)-3-hydroxyacyl-CoA hydro-lyase
This enzyme catalyses a hydration step in peroxisomal beta-oxidation. The human multifunctional enzyme type 2 (MFE-2) is a 79000 Da enzyme composed of three functional units: (3R)-hydroxyacyl-CoA dehydrogenase, 2-enoyl-CoA hydratase 2 and sterol carrier protein 2-like units [1]. The enzymes from Aeromonas caviae [4] and Arabidopsis thaliana [5] are monofunctional enzymes. 2-Enoyl-CoA hydratase 3 from Candida tropicalis is a part from multifunctional enzyme type 2 [3].
CAS REGISTRY NUMBER
COMMENTARY
9027-13-8
cf. EC 4.2.1.17
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
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
2-enoyl-CoA hydratase 2 is a part of multifunctional enzyme type 2, hydrates trans-2-enoyl-CoA to 3-hydroxyacyl-CoA as a key enzyme in the (3R)-hydroxy-dependent route of peroxisomal beta-oxidation of fatty acids
-
-
?
(2E)-2-decenoyl-CoA + H2O
(3R)-3-hydroxydecanoyl-CoA
-
activity measurements are based on the formation of the magnesium complex of 3-ketoacyl-CoA from (2E)-2-decenoyl-CoA
-
-
?
additional information
?
-
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domains A and B have different enzymatic properties and both domains play a functional role in the beta-oxidation of fatty acids in yeast peroxisomes
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-
?
additional information
?
-
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in yeast, the second and the third reaction of the fatty-acid beta-oxidation spiral are catalysed by peroxisomal multifunctional enzyme type 2 (Mfe2p/Fox2p). This protein has two (3R)-hydroxyacyl-CoA dehydrogenase domains and a C-terminal 2-enoyl-CoA hydratase 2 domain
-
-
?
additional information
?
-
-
MFE-2 is a multifunctional enzyme with 2-enoyl-CoA hydratase 2 activity and 2/(3R)-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.36) activity
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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
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
2-enoyl-CoA hydratase 2 is a part of multifunctional enzyme type 2, hydrates trans-2-enoyl-CoA to 3-hydroxyacyl-CoA as a key enzyme in the (3R)-hydroxy-dependent route of peroxisomal beta-oxidation of fatty acids
-
-
?
additional information
?
-
-
domains A and B have different enzymatic properties and both domains play a functional role in the beta-oxidation of fatty acids in yeast peroxisomes
-
-
?
additional information
?
-
-
in yeast, the second and the third reaction of the fatty-acid beta-oxidation spiral are catalysed by peroxisomal multifunctional enzyme type 2 (Mfe2p/Fox2p). This protein has two (3R)-hydroxyacyl-CoA dehydrogenase domains and a C-terminal 2-enoyl-CoA hydratase 2 domain
-
-
?
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
2-enoyl-CoA hydratase 2 is a part of multifunctional enzyme type 2
UniProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). FOX2_CANTR
906
0
99469
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
63000
-
both recombinant CtMfe2p(dha+bdelta) and its SeMet analogue, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 63000, both recombinant CtMfe2p(dha+bdelta) and its SeMet analogue, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure determination. The eukaryotic hydratase 2 has a complete hot dog fold only in its C-domain, whereas the N-domain lacks a long central alpha-helix, thus creating space for bulkier substrates in the binding pocket. The hydrogen bonding network of the active site of 2-enoyl-CoA hydratase 2 resembles the active site geometry of mitochondrial (S)-specific 2-enoyl-CoA hydratase 1, although in a mirror image fashion
hanging-drop vapour-diffusion method. Crystals of native and SeMet CtMfe2p(dha+bdelta)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
CtMfe2p(dha+bdelta) labelled with selenomethionine (SeMet), the plasmid pET3a::CtMfe2p(dha+bdelta) is transformed to the methionine-auxotrophic Escherichia coli strain B834(DE3). The incorporation of SeMet into the structure does not affect the hydratase 2 activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Koski, M.K.; Haapalainen, A.M.; Hiltunen, J.K.; Glumoff, T.
Crystallization and preliminary crystallographic data of 2-enoyl-CoA hydratase 2 domain of Candida tropicalis peroxisomal multifunctional enzyme type 2
Acta Crystallogr. Sect. D
59
1302-1305
2003
Candida tropicalis
Koski, M.K.; Haapalainen, A.M.; Hiltunen, J.K.; Glumoff, T.
A two-domain structure of one subunit explains unique features of eukaryotic hydratase 2
J. Biol. Chem.
279
24666-24672
2004
Candida tropicalis (P22414), Candida tropicalis
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