NDLI: Biochemical characterization of prephenate dehydrogenase from the hyperthermophilic bacterium Aquifex aeolicus

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Biochemical characterization of prephenate dehydrogenase from the hyperthermophilic bacterium Aquifex aeolicus

Content Provider	PubMed Central
Author	Bonvin, Julie Aponte, Raphael A. Marcantonio, Maria Singh, Sasha Dinesh, Christendat Turnbull, Joanne L.
Abstract	A monofunctional prephenate dehydrogenase (PD) from Aquifex aeolicus was expressed as a His-tagged protein in Escherichia coli and was purified by nickel affinity chromatography allowing the first biochemical and biophysical characterization of a thermostable PD. A. aeolicus PD is susceptible to proteolysis. In this report, the properties of the full-length PD are compared with one of these products, an N-terminally truncated protein variant (Δ19PD) also expressed recombinantly in E. coli. Both forms are dimeric and show maximum activity at 95°C or higher. Δ19PD is more sensitive to temperature effects yielding a half-life of 55 min at 95°C versus 2 h for PD, and values of k cat and K m for prephenate, which are twice those determined for PD at 80°C. Low concentrations of guanidine-HCl activate enzyme activity, but at higher concentrations activity is lost concomitant with a multi-state pathway of denaturation that proceeds through unfolding of the dimer, oligomerization, then unfolding of monomers. Measurements of steady-state fluorescence intensity and its quenching by acrylamide in the presence of Gdn-HCl suggest that, of the two tryptophan residues per monomer, one is buried in a hydrophobic pocket and does not become solvent exposed until the protein unfolds, while the less buried tryptophan is at the active site. Tyrosine is a feedback inhibitor of PD activity over a wide temperature range and enhances the cooperativity between subunits in the binding of prephenate. Properties of this thermostable PD are compared and contrasted with those of E. coli chorismate mutase-prephenate dehydrogenase and other mesophilic homologs.
Related Links	http://dx.doi.org/10.1110/ps.051942206
Ending Page	1432
Page Count	16
Starting Page	1417
File Format	PDF
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science : A Publication of the Protein Society
Issue Number	6
Volume Number	15
Language	English
Publisher	Cold Spring Harbor Laboratory Press
Publisher Date	2006-06-01
Access Restriction	Open
Rights Holder	Cold Spring Harbor Laboratory Press
Subject Keyword	Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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Biochemical and Biophysical Characterization of a Prephenate Dehydrogenase from the Hyperthermophilic Bacterium Aquifex aeolicus

Biochemical characterization of prephenate dehydrogenase from the hyperthermophilic bacterium Aquifex aeolicus.

The Crystal Structure of Aquifex aeolicus Prephenate Dehydrogenase Reveals the Mode of Tyrosine Inhibition*

Biochemical characterization of prephenate dehydrogenase from the hyperthermophilic bacteriumAquifex aeolicus

New Functional Sulfide Oxidase-Oxygen Reductase Supercomplex in the Membrane of the Hyperthermophilic Bacterium Aquifex aeolicus *

Structural and mechanistic characterization of 6S RNA from the hyperthermophilic bacterium Aquifex aeolicus.

Crystal Structure of Prephenate Dehydrogenase from Aquifex aeolicus INSIGHTS INTO THE CATALYTIC MECHANISM

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Biochemical characterization of prephenate dehydrogenase from the hyperthermophilic bacterium Aquifex aeolicus

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