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 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.
Ledley
F D
FD
DiLella
A G
AG
Kwok
S C
SC
Woo
S L
SL
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003062:Codon; D004247:DNA / Q000032:analysis; D000939:Epitopes / Q000032:analysis; D006801:Humans; D007700:Kinetics; D010651:Phenylalanine Hydroxylase / Q000235:genetics* / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics; D051381:Rats; D012984:Software; D013045:Species Specificity; D014446:Tyrosine 3-Monooxygenase / Q000235:genetics* / Q000378:metabolism
D003062:Codon; D000939:Epitopes; D012333:RNA, Messenger; D004247:DNA; D010651:Phenylalanine Hydroxylase; D014446:Tyrosine 3-Monooxygenase