Fluorescence Spectroscopy as a Probe of the Effect of Phosphorylation at Serine 40 of Tyrosine Hydroxylase on the Conformation of Its Regulatory Domain-Reference-Cited by-同舟云学术

Fluorescence Spectroscopy as a Probe of the Effect of Phosphorylation at Serine 40 of Tyrosine Hydroxylase on the Conformation of Its Regulatory Domain

Published:2011-02-22 Issue:12 Volume:50 Page:2364-2370
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Wang Shanzhi¹,Lasagna Mauricio¹,Daubner S. Colette²,Reinhart Gregory D.¹,Fitzpatrick Paul F.³

Affiliation:

1. Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, United States

2. Department of Biology, St. Mary’s University, San Antonio, Texas 78228, United States

3. Department of Biochemistry and Center for Biomolecular Neuroscience, University of Texas Health Science Center, San Antonio, Texas 78229, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi101844p

Reference32 articles.

1. Tetrahydropterin-Dependent Amino Acid Hydroxylases

2. Tyrosine hydroxylase phosphorylation: regulation and consequences

3. The metal requirement of rat tyrosine hydroxylase

4. Characterization of the Active Site Iron in Tyrosine Hydroxylase

5. Reduction and Oxidation of the Active Site Iron in Tyrosine Hydroxylase: Kinetics and Specificity

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