Literature DB >> 2412578

Homology between phenylalanine and tyrosine hydroxylases reveals common structural and functional domains.

F D Ledley, A G DiLella, S C Kwok, S L Woo.   

Abstract

Phenylalanine hydroxylase (PAH) and tyrosine hydroxylase (TYH) are mixed-function oxidases that share many characteristic biochemical and immunological properties. The recent cloning and sequencing of full-length cDNAs for both human PAH and rat TYH allow detailed comparison of their primary structures. There is a high degree of homology between PAH and TYH on nucleic acid and amino acid levels. The pattern of homology suggests that these molecules are comprised of a homologous core containing the determinants for enzymatic activity and a nonhomologous region that contributes to substrate specificity and regulation. The degree of homology also suggests that these two proteins evolved from a common ancestor.

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Year:  1985        PMID: 2412578     DOI: 10.1021/bi00335a001

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  23 in total

Review 1.  Mechanism of aromatic amino acid hydroxylation.

Authors:  Paul F Fitzpatrick
Journal:  Biochemistry       Date:  2003-12-09       Impact factor: 3.162

2.  Genetic mapping of the human tryptophan hydroxylase gene on chromosome 11, using an intronic conformational polymorphism.

Authors:  D A Nielsen; M Dean; D Goldman
Journal:  Am J Hum Genet       Date:  1992-12       Impact factor: 11.025

Review 3.  Tyrosine hydroxylase and regulation of dopamine synthesis.

Authors:  S Colette Daubner; Tiffany Le; Shanzhi Wang
Journal:  Arch Biochem Biophys       Date:  2010-12-19       Impact factor: 4.013

4.  Single-strand conformation polymorphism for detection of mutations and base substitutions in phenylketonuria.

Authors:  P Labrune; D Melle; F Rey; M Berthelon; C Caillaud; J Rey; A Munnich; S Lyonnet
Journal:  Am J Hum Genet       Date:  1991-06       Impact factor: 11.025

5.  Effects of ligands on the mobility of an active-site loop in tyrosine hydroxylase as monitored by fluorescence anisotropy.

Authors:  Giri R Sura; Mauricio Lasagna; Vijay Gawandi; Gregory D Reinhart; Paul F Fitzpatrick
Journal:  Biochemistry       Date:  2006-08-08       Impact factor: 3.162

6.  Kinetic mechanism of phenylalanine hydroxylase: intrinsic binding and rate constants from single-turnover experiments.

Authors:  Kenneth M Roberts; Jorge Alex Pavon; Paul F Fitzpatrick
Journal:  Biochemistry       Date:  2013-01-29       Impact factor: 3.162

Review 7.  The human tyrosine hydroxylase gene.

Authors:  T Nagatsu
Journal:  Cell Mol Neurobiol       Date:  1989-09       Impact factor: 5.046

8.  Full-length cDNA for rabbit tryptophan hydroxylase: functional domains and evolution of aromatic amino acid hydroxylases.

Authors:  H E Grenett; F D Ledley; L L Reed; S L Woo
Journal:  Proc Natl Acad Sci U S A       Date:  1987-08       Impact factor: 11.205

9.  Molecular cloning of cDNA coding for brain-specific 14-3-3 protein, a protein kinase-dependent activator of tyrosine and tryptophan hydroxylases.

Authors:  T Ichimura; T Isobe; T Okuyama; N Takahashi; K Araki; R Kuwano; Y Takahashi
Journal:  Proc Natl Acad Sci U S A       Date:  1988-10       Impact factor: 11.205

10.  Single turnover kinetics of tryptophan hydroxylase: evidence for a new intermediate in the reaction of the aromatic amino acid hydroxylases.

Authors:  Jorge Alex Pavon; Bekir Eser; Michaela T Huynh; Paul F Fitzpatrick
Journal:  Biochemistry       Date:  2010-09-07       Impact factor: 3.162

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