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Information on EC 4.2.1.119 - enoyl-CoA hydratase 2 and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q02207

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.119 enoyl-CoA hydratase 2
IUBMB 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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Saccharomyces cerevisiae
UNIPROT: Q02207
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-enoyl-CoA hydratase 2
2-enoyl-CoA hydratase 2
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 hide
9027-13-8
cf. EC 4.2.1.17
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
show the reaction diagram
-
-
-
?
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
(2E)-2-enoyl-CoA + H2O
(3R)-3-hydroxyacyl-CoA
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
fox2 mutant strain
UniProt
Manually annotated by BRENDA team
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA629-990
truncated version (lacking the carboxyl-terminal 271 amino acids). The truncated form contains only the D-3-hydroxyacyl-CoA dehydrogenase activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the FOX2 gene is overexpressed from a multicopy vector (YEp352) in Saccharomyces cerevisiae and the gene product purified to apparent homogenity. A truncated version of MFP lacking 271 carboxyl-terminal amino acids is also overexpressed and purified
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hiltunen, J.K.; Wenzel, B.; Beyer, A.; Erdmann, R.; Fossa, A.; Kunau, W.H.
Peroxisomal multifunctional beta-oxidation protein of Saccharomyces cerevisiae. Molecular analysis of the fox2 gene and gene product
J. Biol. Chem.
267
6646-6653
1992
Saccharomyces cerevisiae (Q02207)
Manually annotated by BRENDA team