Substituting Tyr138 in the active site loop of human phenylalanine hydroxylase affects catalysis and substrate activation-Reference-Cited by-同舟云学术

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Substituting Tyr138 in the active site loop of human phenylalanine hydroxylase affects catalysis and substrate activation

Published:2017-06-12 Issue:7 Volume:7 Page:1026-1036
ISSN:2211-5463
Container-title:FEBS Open Bio
language:en
Short-container-title:FEBS Open Bio

Author:

Leandro João¹²,Stokka Anne J.¹³,Teigen Knut¹,Andersen Ole A.¹⁴,Flatmark Torgeir¹

Affiliation:

1. Department of Biomedicine; University of Bergen; Norway

2. Metabolism and Genetics Group; Research Institute for Medicines (iMed.ULisboa); Faculty of Pharmacy; University of Lisbon; Portugal

3. The Biotechnology Centre of Oslo; University of Oslo; Norway

4. Evotec (UK) Ltd.; Abingdon UK

Funder

Universitetet i Bergen

Publisher

Wiley

Subject

General Biochemistry, Genetics and Molecular Biology

Reference35 articles.

1. Pterin-dependent amino acid hydroxylases;Kappock;Chem Rev,1996

2. Structural insight into the aromatic amino acid hydroxylases and their disease-related mutant forms;Flatmark;Chem Rev,1999

3. Rat liver phenylalanine hydroxylase. A method for the measurement of activity, with particular reference to the distinctive features of the enzyme and pteridine cofactor;Nielsen;Eur J Biochem,1969

4. Substrate activation of phenylalanine hydroxylase. A kinetic characterization;Shiman;J Biol Chem,1980

5. Structural basis of autoregulation of phenylalanine hydroxylase;Kobe;Nat Struct Biol,1999

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