Literature summary extracted from
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 (2004), J. Biol. Chem., 279, 24666-24672.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
4.2.1.119 |
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 |
Candida tropicalis |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
4.2.1.119 |
(2E)-2-enoyl-CoA + H2O |
Candida tropicalis |
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 |
(3R)-3-hydroxyacyl-CoA |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.2.1.119 |
Candida tropicalis |
P22414 |
2-enoyl-CoA hydratase 2 is a part of multifunctional enzyme type 2 |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
4.2.1.119 |
(2E)-2-enoyl-CoA + H2O |
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 |
Candida tropicalis |
(3R)-3-hydroxyacyl-CoA |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.2.1.119 |
2-enoyl-CoA hydratase 2 |
is a part of multifunctional enzyme type 2 |
Candida tropicalis |