The enzyme is involved in the catechol meta-cleavage pathway, a major mechanism for degradation of aromatic compounds. Also acts, more slowly, on cis-2-oxohex-4-enoate, but not on the trans-isomer. The enzyme was named when it was thought that the substrate is 2-oxopent-4-enoate. However, it was later found that the actual substrate is its tautomer (2Z)-2-hydroxypenta-2,4-dienoate. In some organisms the enzyme forms a complex with EC 4.1.1.77, 2-oxo-3-hexenedioate decarboxylase (previously named 4-oxalocrotonate decarboxylase).
The enzyme is involved in the catechol meta-cleavage pathway, a major mechanism for degradation of aromatic compounds. Also acts, more slowly, on cis-2-oxohex-4-enoate, but not on the trans-isomer. The enzyme was named when it was thought that the substrate is 2-oxopent-4-enoate. However, it was later found that the actual substrate is its tautomer (2Z)-2-hydroxypenta-2,4-dienoate. In some organisms the enzyme forms a complex with EC 4.1.1.77, 2-oxo-3-hexenedioate decarboxylase (previously named 4-oxalocrotonate decarboxylase).
divalent metal required, activation in order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ca2+. Divalent metal ion is hexa-coordinated in the enzyme. It has a catalytic rather than just a substrate binding role. Enzyme has no activity when divalent cations are excluded from the assay mixture
divalent metal required, activation in order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ca2+. Divalent metal ion is hexa-coordinated in the enzyme. It has a catalytic rather than just a substrate binding role. Enzyme has no activity when divalent cations are excluded from the assay mixture
divalent metal required, activation in order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ca2+. Divalent metal ion is hexa-coordinated in the enzyme. It has a catalytic rather than just a substrate binding role. Enzyme has no activity when divalent cations are excluded from the assay mixture
active site of MhpD consists of three acidic residues (Glu105, Glu107, and Glu138), which may be involved in coordinating the divalent cation essential for activity
divalent metal required, activation in order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ca2+. Divalent metal ion is hexa-coordinated in the enzyme. It has a catalytic rather than just a substrate binding role. Enzyme has no activity when divalent cations are excluded from the assay mixture
divalent metal required, activation in order of decreasing efficiency: Mg2+, Mn2+, Co2+, Zn2+, Ca2+. Divalent metal ion is hexa-coordinated in the enzyme. It has a catalytic rather than just a substrate binding role. Enzyme has no activity when divalent cations are excluded from the assay mixture
high activity when the organism is cultivated in medium containing 0.12% (w/v) 4-amino-3-hydroxybenzoic acid as sole carbon, nitrogen, and energy source until the late exponential phase. Low activity when the organism is cultivated in succinate-glucose medium until the late-exponential phase
high activity when the organism is cultivated in medium containing 0.12% (w/v) 4-amino-3-hydroxybenzoic acid as sole carbon, nitrogen, and energy source until the late exponential phase. Low activity when the organism is cultivated in succinate-glucose medium until the late-exponential phase
the enzyme is part of an inducible pathway encoded by the TOL plasmid pWW0 that enables selected bacterial strains to use toluene, m- and p-xylene, 3-ethyltoluene, and 1,2,4-trimethylbenzene as their sole sources of carbon and energy. vinylpyruvate hydratase is in a complex with the preceding enzyme in the pathway, 4-oxalocrotonate decarboxylase
the enzyme is part of an inducible pathway encoded by the TOL plasmid pWW0 that enables selected bacterial strains to use toluene, m- and p-xylene, 3-ethyltoluene, and 1,2,4-trimethylbenzene as their sole sources of carbon and energy. vinylpyruvate hydratase is in a complex with the preceding enzyme in the pathway, 4-oxalocrotonate decarboxylase
the enzyme is part of an inducible pathway encoded by the TOL plasmid pWW0 that enables selected bacterial strains to use toluene, m- and p-xylene, 3-ethyltoluene, and 1,2,4-trimethylbenzene as their sole sources of carbon and energy. vinylpyruvate hydratase is in a complex with the preceding enzyme in the pathway, 4-oxalocrotonate decarboxylase
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
MhpD with and without Mg2+, by hanging-drop vapour-diffusion method, to 2.8 A resolution. Space group of the crystals is H3 with unit cell parameters a = 207.35 A, b = 207.35 A, c = 545.47 A, alpha = 90°, beta = 90°, and gamma = 120°. Assembles to form a 20-nm-diameter particle comprising 60 protein subunits, arranged with 532 symmetry when crystallised at low pH in the presence of phosphate or sulphate ions. Particles form rapidly and are stable in solution during gel filtration at low pH. They are probably formed through trimers of pentamers, which are stabilised by the interaction of two phosphate ions with residues of the N-terminal domains of subunits at the 3fold axis. Once the particles are formed at high concentrations of phosphate (or sulphate), they remain stable in solution at 20fold lower concentrations of the anion. Guest molecules can be trapped within the hollow protein shell during assembly. The C-termini of the subunits are freely accessible on the surface of the protein cage
Harayama, S.; Rekik, M.; Ngai, K.L.; Ornston, L.N.
Physically associated enzymes produce and metabolize 2-hydroxy-2,4-dienoate, a chemically unstable intermediate in catechol metabolism via meta cleavage in Pseudomonas putida