4.2.1.119: enoyl-CoA hydratase 2

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For detailed information about enoyl-CoA hydratase 2, go to the full flat file.

Reaction

Synonyms

(3R)-hydroxyacyl-CoA dehydrogenase/2-enoyl-CoA hydratase 2, (R)-specific ECH, (R)-specific enoyl coenzyme A hydratase, (R)-specific enoyl-CoA hydratase, (R)-specific enoyl-coenzyme A hydratase, 2-enoyl-CoA hydratase, 2-enoyl-CoA hydratase 2, 2-enoyl-hydratase 2, 2E-enoyl-CoA hydratase 2, At1g76150, AtECH2, D-(-)-3-hydroxyacyl-CoA hydro-lyase, D-3-hydroxyacyl-CoA dehydratase, D-3-hydroxyacyl-CoA hydro-lyase, D-bifunctional enzyme, D-BP, D-specific 2-trans-enoyl-CoA hydratase, ECH-2, ECH2, enoyl-CoA hydratase 2, HFX_1483, hydratase 2, MaoC, MaoC-like protein, MFE-2, MFE2, MFE2 hydratase, Mfe2p [CtMfe2p(dha+bdelta)], multifunctional enzyme type 2, multifunctional enzyme type 2 hydratase, perMFE-II, peroxisomal enoyl-CoA hydratase 2, phaJ, PhaJ1, PhaJ1Pa, PhaJ1Pp, PhaJ4, PhaJ4aRe, PhaJ4bRe, PhaJ4cRe, PhaJAc, PhaJYB4, R-ECH, R-hydratase, R-specific enoyl coenzyme A hydratase, R-specific enoyl-CoA hydratase

ECTree

     4 Lyases

         4.2 Carbon-oxygen lyases

             4.2.1 Hydro-lyases

                4.2.1.119 enoyl-CoA hydratase 2

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Results	in table
30318	AA Sequence
1	Application
1	CAS Registry Number
19	Cloned(Commentary)
8	Crystallization (Commentary)
11	Disease/ Diagnostics
34	General Information
4	Inhibitors
3	kcat/KM [mM/s]
3	Ki Value [mM]
41	KM Value [mM]
19	Localization
19	Molecular Weight [Da]
28	Natural Substrates/ Products (Substrates)
241	Organism
14	Pathway
6	PDB ID
11	pH Optimum
1	pH Range
2	pI Value
63	Protein Variants
14	Purification (Commentary)
1	Reaction
3	Reaction Type
36	Reference
19	Source Tissue
37	Specific Activity [micromol/min/mg]
2	Storage Stability
95	Substrates and Products (Substrate)
17	Subunits
105	Synonyms
1	Systematic Name
10	Temperature Optimum [°C]
1	Temperature Range [°C]
13	Turnover Number [1/s]

Crystallization

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Crystallization on EC 4.2.1.119 - enoyl-CoA hydratase 2

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

sitting drop vapour diffusion against a reservoir solution containing 20% polyethylene glycol 4000, 5% 2-propanol and 20 mM HEPES pH 7.0 at 25°C. Crystals belong to the monoclinic space group C2, with unit-cell parameters a = 111.54 A, b = 59.29 A, c = 47.27 A, beta = 113.04° and contain a dimeric molecule in the asymmetric unit

Aeromonas caviae

-

649144

hanging-drop vapour-diffusion method. Crystals of native and SeMet CtMfe2p(dha+bdelta)

Candida tropicalis

-

649201

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

P22414

665519

purified recombinant detagged MFE-2, 5 mg/ml protein in 0.1 Msodium phosphate, pH 7.2, and 0.2 M NaF, sitting and hanging drop vapour diffusion methods are used at 21°C, mixing of equal volumes of protein and reservoir solutions, the latter contains 100 mM Tris-HCl, pH 8.0, 1.0 M NaCl, 20% w/v PEG 5000 MME and 5 mM NAD+, X-ray diffraction structure determination and analysis at 2.15 A resolution

Drosophila melanogaster

-

714098

hanging-drop vapor diffusion method, crystal structure to 3 A resolution. MFE-2 has a two-domain subunit structure with a C-domain complete hot-dog fold housing the active site, and an N-domain incomplete hot-dog fold housing the cavity for the aliphatic acyl part of the substrate molecule. The ability of human hydratase 2 to utilize such bulky compounds which are not physiological substrates for the fungal ortholog, e.g. CoA esters of C26 fatty acids, pristanic acid and di/trihydroxycholestanoic acids, is explained by a large hydrophobic cavity formed upon the movements of the extremely mobile loops I–III in the N-domain. In the unliganded form of human hydratase 2, however, the loop I blocks the entrance of fatty enoyl-CoAs with chain-length above C8

Homo sapiens

P51659

659723

homology modeling of strcuture. In the acyl-chain binding pocket, the amino acid at position 72 is the only difference between the two structures of Pseudomonas aeruginosa and Pseudomonas putida isoforms

Pseudomonas aeruginosa

Q9LBK2

746834

purified recombinant enzyme PhaJ1Pa, sitting drop vapor diffusion, mixing of 10 mg/ml protein in 20 mM Tris-HCl, pH 7.5, with mother liquor containing 15 to 20% w/v PEG 3350, 20% v/v glycerol, and 0.1 M bis-Tris, pH 6.0-6.5, X-ray diffraction structure determination and analysis at 1.7 A resolution

Pseudomonas aeruginosa

Q9LBK2

746834

homology modeling of strcuture. In the acyl-chain binding pocket, the amino acid at position 72 is the only difference between the two structures of Pseudomonas aeruginosa and Pseudomonas putida isoforms

Pseudomonas putida

A0A177YY42, E9P3X9

746834