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Information on EC 4.2.1.119 - enoyl-CoA hydratase 2 and Organism(s) Arabidopsis thaliana and UniProt Accession Q8VYI3
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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
-
r-3-hydroxyacyl-coas
- aconitate
-
phajs
- caviae
-
3r-hydroxyacyl-coa
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even-numbered
- biotechnology
The taxonomic range for the selected organisms is: Arabidopsis thaliana
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
AtECH2
enoyl-CoA hydratase 2
AtECH2
gene name. Alignment of AtECH2 with homologous proteins is shown
enoyl-CoA hydratase 2
monofunctional enzyme in Arabidopsis thaliana
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)-hexadecenoyl-CoA + H2O
(3R)-3-hydroxyhexadecanoyl-CoA
-
-
-
?
(3R)-3-hydroxyacyl-CoA
(2E)-2-enoyl-CoA + H2O
AtECH2 participates in vivo in the conversion of the intermediate (3R)-hydroxyacyl-CoA, generated by the metabolism of fatty acids with a cis (Z)-unsaturated bond on an even-numbered carbon, to the (2E)-enoyl-CoA for further degradation through the core beta-oxidation cycle. AtECH2 is a monofunctional enzyme in Arabidopsis thaliana that is devoid of 3-hydroxyacyl-CoA dehydrogenase activity
-
-
?
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
(3R)-3-hydroxyacyl-CoA
(2E)-2-enoyl-CoA + H2O
AtECH2 participates in vivo in the conversion of the intermediate (3R)-hydroxyacyl-CoA, generated by the metabolism of fatty acids with a cis (Z)-unsaturated bond on an even-numbered carbon, to the (2E)-enoyl-CoA for further degradation through the core beta-oxidation cycle. AtECH2 is a monofunctional enzyme in Arabidopsis thaliana that is devoid of 3-hydroxyacyl-CoA dehydrogenase activity
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
AtECH2 gene expression is strongest in tissues with high beta-oxidation activity, such as germinating seedlings and senescing leaves
AtECH2 gene expression is strongest in tissues with high beta-oxidation activity, such as germinating seedlings and senescing leaves
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
defects in either HC-PPase or ECH2 compromise cell proliferation due to defects in mobilizing seed storage lipids, phenotype, overview. Enoyl-CoA hydratase 2 (ECH2) gene mutation causes the A#3-1sm phenotypes, overview. Mutant A#3-1 has a cell size that is severely reduced, but the cell number remains similar to that of original fugu5-1. The cell number decreases in A#3-1 single mutant (A#3-1sm), similar to that of fugu5-1, but cell size is almost equal to that of the wild-type. A#3-1 mutation does not affect CCE in other compensation exhibiting mutant backgrounds, such as an3-4 and fugu2-1/fas1-6
physiological function
role of the monofunctional peroxisomal enoyl-CoA hydratase 2 in compensated cell enlargement (CCE). Enzyme ECH2 alone likely promotes CCE during the post-mitotic cell expansion stage of cotyledon development, probably by converting indolebutyric acid to indole acetic acid
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). ECH2_ARATH
309
0
34082
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
mutagenesis of fugu5-1 seeds with heavy-ion irradiation and screening of mutations that restrain compensated cell enlargement (CCE) to gain insight into the genetic pathway(s) involved in CCE. Mutant A#3-1 has a cell size that is severely reduced, but the cell number remains similar to that of original fugu5-1. The cell number decreases in A#3-1 single mutant (A#3-1sm), similar to that of fugu5-1, but cell size is almost equal to that of the wild-type. A#3-1 mutation does not affect CCE in other compensation exhibiting mutant backgrounds, such as an3-4 and fugu2-1/fas1-6. Subsequent map-based cloning combined with genome sequencing and HRM curve analysis identified enoyl-CoA hydratase 2 (ECH2) as the causal gene of A#3-1. The above phenotypes are consistently observed in the ech2-1 allele and supplying sucrose restores the morphological and cellular phenotypes in fugu5-1, ech2-1, A#3-1sm, fugu5-1 ech2-1, and A#3-1; fugu5-1. The ech2-1 mutant allele is indistinguishable from A#3-1sm and suppresses CCEin fugu5. Analysis of ech2-1 mutant. Enoyl-CoA hydratase 2 gene mutation causes the A#3-1sm phenotypes, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
AtECH2 contains a peroxisome targeting signal at the C-terminal end, is addressed to the peroxisome in Saccharomyces cerevisiae, and a fusion protein between AtECH2 and a fluorescent protein is targeted to peroxisomes in onion cells. To assess the peroxisomal addressing of AtECH2, a fusion protein between an EYFP at the N terminus and AtECH2 at the C terminus is constructed and expressed under the control of a double cauliflower mosaic virus (CaMV) 35 S viral promoter to allow transient expression of the fusion protein in onion cells following biolistic bombardment. The fluorescence is examined by confocal microscopy after 12 h
gene ECH2, DNA and amino acid sequence determination and analysis, map-based cloning
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Goepfert, S.; Hiltunen, J.K.; Poirier, Y.
Identification and functional characterization of a monofunctional peroxisomal enoyl-CoA hydratase 2 that participates in the degradation of even cis-unsaturated fatty acids in Arabidopsis thaliana
J. Biol. Chem.
281
35894-35903
2006
Arabidopsis thaliana (Q8VYI3), Arabidopsis thaliana
Katano, M.; Takahashi, K.; Hirano, T.; Kazama, Y.; Abe, T.; Tsukaya, H.; Ferjani, A.
Suppressor screen and phenotype analyses revealed an emerging role of the monofunctional peroxisomal enoyl-CoA hydratase 2 in compensated cell enlargement
Front. Plant Sci.
7
132
2016
Arabidopsis thaliana (Q8VYI3), Arabidopsis thaliana Col-0 (Q8VYI3)
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