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

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 structu...

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Bibliographic Details
Published in:Biochemistry (Easton) 1985-07, Vol.24 (14), p.3389-3394
Main Authors: Ledley, Fred D, DiLella, Anthony G, Kwok, Simon C. M, Woo, Savio L. C
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Animals
Base Sequence
Biological and medical sciences
Codon
DNA - analysis
Enzymes and enzyme inhibitors
Epitopes - analysis
evolution
Fundamental and applied biological sciences. Psychology
Humans
Kinetics
man
phenylalanine hydroxylase
Phenylalanine Hydroxylase - genetics
Phenylalanine Hydroxylase - metabolism
primary structure
Rats
RNA, Messenger - genetics
Software
Species Specificity
Transferases
Tyrosine 3-Monooxygenase - genetics
Tyrosine 3-Monooxygenase - metabolism
tyrosine hydroxylase
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Summary: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.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00335a001