Phenylalanine Binding Is Linked to Dimerization of the Regulatory Domain of Phenylalanine Hydroxylase

[Image: see text] Analytical ultracentrifugation has been used to analyze the oligomeric structure of the isolated regulatory domain of phenylalanine hydroxylase. The protein exhibits a monomer–dimer equilibrium with a dissociation constant of ∼46 μM; this value is unaffected by the removal of the 2...

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Autores principales: Zhang, Shengnan, Roberts, Kenneth M., Fitzpatrick, Paul F.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2014
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4251497/
https://www.ncbi.nlm.nih.gov/pubmed/25299136
http://dx.doi.org/10.1021/bi501109s
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author Zhang, Shengnan
Roberts, Kenneth M.
Fitzpatrick, Paul F.
author_facet Zhang, Shengnan
Roberts, Kenneth M.
Fitzpatrick, Paul F.
author_sort Zhang, Shengnan
collection PubMed
description [Image: see text] Analytical ultracentrifugation has been used to analyze the oligomeric structure of the isolated regulatory domain of phenylalanine hydroxylase. The protein exhibits a monomer–dimer equilibrium with a dissociation constant of ∼46 μM; this value is unaffected by the removal of the 24 N-terminal residues or by phosphorylation of Ser16. In contrast, phenylalanine binding (K(d) = 8 μM) stabilizes the dimer. These results suggest that dimerization of the regulatory domain of phenylalanine hydroxylase is linked to allosteric activation of the enzyme.
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spelling pubmed-42514972015-10-09 Phenylalanine Binding Is Linked to Dimerization of the Regulatory Domain of Phenylalanine Hydroxylase Zhang, Shengnan Roberts, Kenneth M. Fitzpatrick, Paul F. Biochemistry [Image: see text] Analytical ultracentrifugation has been used to analyze the oligomeric structure of the isolated regulatory domain of phenylalanine hydroxylase. The protein exhibits a monomer–dimer equilibrium with a dissociation constant of ∼46 μM; this value is unaffected by the removal of the 24 N-terminal residues or by phosphorylation of Ser16. In contrast, phenylalanine binding (K(d) = 8 μM) stabilizes the dimer. These results suggest that dimerization of the regulatory domain of phenylalanine hydroxylase is linked to allosteric activation of the enzyme. American Chemical Society 2014-10-09 2014-10-28 /pmc/articles/PMC4251497/ /pubmed/25299136 http://dx.doi.org/10.1021/bi501109s Text en Copyright © 2014 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Zhang, Shengnan
Roberts, Kenneth M.
Fitzpatrick, Paul F.
Phenylalanine Binding Is Linked to Dimerization of the Regulatory Domain of Phenylalanine Hydroxylase
title Phenylalanine Binding Is Linked to Dimerization of the Regulatory Domain of Phenylalanine Hydroxylase
title_full Phenylalanine Binding Is Linked to Dimerization of the Regulatory Domain of Phenylalanine Hydroxylase
title_fullStr Phenylalanine Binding Is Linked to Dimerization of the Regulatory Domain of Phenylalanine Hydroxylase
title_full_unstemmed Phenylalanine Binding Is Linked to Dimerization of the Regulatory Domain of Phenylalanine Hydroxylase
title_short Phenylalanine Binding Is Linked to Dimerization of the Regulatory Domain of Phenylalanine Hydroxylase
title_sort phenylalanine binding is linked to dimerization of the regulatory domain of phenylalanine hydroxylase
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4251497/
https://www.ncbi.nlm.nih.gov/pubmed/25299136
http://dx.doi.org/10.1021/bi501109s
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