NDLI: Cloning of Quail Tyrosine Hydroxylase: Amino Acid Homology with Other Hydroxylases Discloses Functional Domains

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Cloning of Quail Tyrosine Hydroxylase: Amino Acid Homology with Other Hydroxylases Discloses Functional Domains

Content Provider	Scilit
Author	Fauquet, Mireille Grima, Brigitte Lamouroux, Annie Mallet, Jacques
Copyright Year	1988
Description	Journal: Journal of Neurochemistry A cDNA clone containing the entire coding region of quail tyrosine hydroxylase (TH) has been isolated and analyzed. Comparison with rat and human THs and phenylalanine hydroxylases reveals several highly conserved domains. Two of them, shared by all these hydroxylases, are localized in the central and C-terminal parts of the molecules, and most probably include the active site. Two others are found only in the TH molecules. One contains putative sites of phosphorylation and is implicated in the posttranslational regulation of the enzyme. The second highly preserved domain, consisting of a stretch of 21 amino acids, is presumably associated with an important feature of the enzyme that remains to be identified.
Related Links	http://onlinelibrary.wiley.com/doi/10.1111/j.1471-4159.1988.tb13241.x/pdf
Ending Page	148
Page Count	7
Starting Page	142
e-ISSN	14714159
DOI	10.1111/j.1471-4159.1988.tb13241.x
Journal	Journal of Neurochemistry
Issue Number	1
Volume Number	50
Language	English
Publisher	Wiley-Blackwell
Publisher Date	1988-01-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Neurochemistry Biochemistry and Molecular Biology Quail Tyrosine Hydroxylase Phenylalanine Hydroxylase Cdna Cloning Sequence Homology
Content Type	Text
Resource Type	Article

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