Structural Evolution of Differential Amino Acid Effector Regulation in Plant Chorismate Mutases

Westfall, Corey S.; Xu, Ang; Jez, Joseph M.

doi:10.1074/jbc.m114.591123

Cited by 44 publications

(53 citation statements)

References 40 publications

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“…4c). CM activity in the plastid fraction was completely inhibited by 1 mM L-Tyr and showed approximately threefold induction by 1 mM L-Trp, in agreement with previous reports from other plant species [30][31][32][33] . In contrast, CM activity in the cytosol was only slightly decreased and increased by L-Tyr and L-Trp, respectively (Fig.…”

Section: Soybean Has Tyr-and Trp-insensitive Cytosolic CM Activitysupporting

confidence: 91%

“…2) as well as in a previous report 18 . The remaining ADH activity associated with PDH activity (fractions [26][27][28][29][30][31][32][33][34][35][36] was approximately 50-fold lower than PDH activity. Thus, soybean appears to have a highly active, dedicated PDH enzyme (or enzymes) and hence was the primary focus of this study.…”

Section: Soybean and Medicago Exhibit Pdh Activitymentioning

confidence: 95%

“…A phylogenetic analysis of plant CM orthologs identified two distinct clades: one with plastid-localized CMs having a CTP and another containing cytosolic CMs lacking a CTP [30][31][32] (Supplementary Fig. 10).…”

Section: Soybean Has Tyr-and Trp-insensitive Cytosolic CM Activitymentioning

confidence: 99%

“…Cytosolic CMs have been identified in some plant species [30][31][32][33] , which, if present in legumes, may provide the prephenate substrate for the cytosolic PDH enzymes. A phylogenetic analysis of plant CM orthologs identified two distinct clades: one with plastid-localized CMs having a CTP and another containing cytosolic CMs lacking a CTP [30][31][32] (Supplementary Fig.…”

Section: Soybean Has Tyr-and Trp-insensitive Cytosolic CM Activitymentioning

confidence: 99%

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Non-plastidic, tyrosine-insensitive prephenate dehydrogenases from legumes

et al. 2014

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L-Tyrosine (Tyr) and its plant-derived natural products are essential in both plants and humans. In plants, Tyr is generally assumed to be synthesized in the plastids via arogenate dehydrogenase (TyrA(a), also known also ADH), which is strictly inhibited by L-Tyr. Using phylogenetic and expression analyses, together with recombinant enzyme and endogenous activity assays, we identified prephenate dehydrogenases (TyrA(p)s, also known as PDHs) from two legumes, Glycine max (soybean) and Medicago truncatula. The identified PDHs were phylogenetically distinct from canonical plant ADH enzymes, preferred prephenate to arogenate substrate, localized outside of the plastids and were not inhibited by L-Tyr. The results provide molecular evidence for the diversification of primary metabolic Tyr pathway via an alternative cytosolic PDH pathway in plants.

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Section: Soybean Has Tyr-and Trp-insensitive Cytosolic CM Activitysupporting

confidence: 91%

Section: Soybean and Medicago Exhibit Pdh Activitymentioning

confidence: 95%

Section: Soybean Has Tyr-and Trp-insensitive Cytosolic CM Activitymentioning

confidence: 99%

Section: Soybean Has Tyr-and Trp-insensitive Cytosolic CM Activitymentioning

confidence: 99%

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Non-plastidic, tyrosine-insensitive prephenate dehydrogenases from legumes

et al. 2014

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“…For this enzyme, a complex allosteric response involving activation by Trp and inhibition by Tyr is mediated by changes in the relative positioning of the two domains of the homodimeric structure. The allosteric sites are found at the interface, illustrating the importance of protein-protein interactions in determining the activity of a remote active site (33)(34)(35).…”

Section: Discussionmentioning

confidence: 99%

Complex Formation between Two Biosynthetic Enzymes Modifies the Allosteric Regulatory Properties of Both

Blackmore

Nazmi

Hutton

et al. 2015

Journal of Biological Chemistry

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Background: Two enzymes from Mycobacterium tuberculosis involved in aromatic amino acid biosynthesis form a heterooctameric complex. Results: Complex formation boosts the catalytic activity of both enzymes and greatly extends the allosteric effector sensitivity. Conclusion: Enzyme interactions allow complex allosteric machinery of one of the complex partners to be shared. Significance: Sophisticated allosteric responses are delivered through protein-protein interactions, allowing enhanced metabolic control.

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Reaction Mechanism of Prephenate Dehydrogenase from the Alternative Tyrosine Biosynthesis Pathway in Plants

Holland

Jez

2018

ChemBioChem

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Unlike metazoans, plants, bacteria, and fungi retain the enzymatic machinery necessary to synthesize the three aromatic amino acids l-phenylalanine, l-tyrosine, and l-tryptophan de novo. In legumes, such as soybean, alfalfa, and common bean, prephenate dehydrogenase (PDH) catalyzes the tyrosine-insensitive biosynthesis of 4-hydroxyphenylpyruvate, a precursor to tyrosine. The three-dimensional structure of soybean PDH1 was recently solved in complex with the NADP cofactor. This structure allowed for the identification of both the cofactor- and ligand-binding sites. Here, we present steady-state kinetic analysis of twenty site-directed active-site mutants of soybean (Glycine max) PDH compared to wild-type. Molecular docking of the substrate, prephenate, into the active site of the enzyme revealed its potential interactions with the active site residues and made a case for the importance of each residue in substrate recognition and/or catalysis, most likely through transition state stabilization. Overall, these results suggested that the active site of the enzyme is highly sensitive to any changes, as even subtle alterations substantially reduced the catalytic efficiency of the enzyme.

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Structural Evolution of Differential Amino Acid Effector Regulation in Plant Chorismate Mutases

Cited by 44 publications

References 40 publications

Non-plastidic, tyrosine-insensitive prephenate dehydrogenases from legumes

Non-plastidic, tyrosine-insensitive prephenate dehydrogenases from legumes

Complex Formation between Two Biosynthetic Enzymes Modifies the Allosteric Regulatory Properties of Both

Reaction Mechanism of Prephenate Dehydrogenase from the Alternative Tyrosine Biosynthesis Pathway in Plants

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