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3.7.1.8: 2,6-dioxo-6-phenylhexa-3-enoate hydrolase

This is an abbreviated version!
For detailed information about 2,6-dioxo-6-phenylhexa-3-enoate hydrolase, go to the full flat file.

Word Map on EC 3.7.1.8

Reaction

2,6-dioxo-6-phenylhexa-3-enoate
+
H2O
=
benzoate
 +
2-oxopent-4-enoate

Synonyms

2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoic acid hydrolase, 2-hydroxy-6-oxo-6-phenylhexa-2, 4-dienoate hydrolase, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolase, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dieonic acid hydrolase, 6-phenyl HODA hydrolase, BphD, BphD enzyme, BphDP6, CarC, HOHPDA hydrolase, HOPD hydrolase, HOPDA hydrolase, HPDA hydrolase, HsaD, hydrolase, 2,6-dioxo-6-phenylhexa-3-enoate, LigY, MCP hydrolase, meta-cleavage product hydrolase, MhpC

ECTree

     3 Hydrolases
         3.7 Acting on carbon-carbon bonds
             3.7.1 In ketonic substances
                3.7.1.8 2,6-dioxo-6-phenylhexa-3-enoate hydrolase

Crystallization

Crystallization on EC 3.7.1.8 - 2,6-dioxo-6-phenylhexa-3-enoate hydrolase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
H263 mutant by hanging drop vapor diffusion, to 2 A resolution
-
mutant S114A in complex with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, 8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid, or 4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid, sitting drop vapor diffusion, 0.001 ml of 8 mg/ml protein solution is mixed with 0.001 ml of precipitant solution containing 200 mM KSCN, 24% PEG 3350, and 100 mM bis-tris propane, pH 7.0, soaking of S114A crystals in 0.01 ml of precipitant solution supplemented with 15 mM of each ligand for 30-60 min, X-ray diffractin structure determination and analysis at 1.8-2.1 A resolution, molecular replacement
BphD H265Q and S112A/H265Q mutants in complex with substrate 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, sitting drop vapour diffusion method, 0.001 ml of protein solution containing 4 mg/ml protein in 20 mM HEPES, pH 7.5, 20°C, 9 days, is mixed with 0.001 ml of reservoir solution containing 2.4 M malonate at pH 6.0-7.0, X-ray diffraction structure determination and analysis at 1.3 A and 1.9 A resolutions, respectively
enzyme structure determination and analysis, PDB IDs 2OG1, 2PU5, 2RI6, 2PU7, 2PUH and 2PUJ
S112A and H265Q mutants crystal structure analysis, PDB IDs 2PUH and 3V1N, modeling
-
wild-type, the S112C variant and S112C incubated with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid by hanging drop vapor diffusion method at 20°C, to 1.6 A resolution, interaction between conserved active side residues and dienoate moiety of the substrate, the residue His265 is hydrogen-bonded to the 2-hydroxy/oxo substituent of the substrate, consistent with a role in catalyzing ketonization
-
at 2.4 A resolution, active-site residues are Ser110, Asp235 and His263, situated inside the cavity between the core and the lid domains, this substrate binding pocket has a hydrophobic and hydrophilic region
enzyme structure determination and analysis, PDB ID 1C4X