Mouse phenylalanine hydroxylase. Homology and divergence from human phenylalanine hydroxylase.
The laboratory mouse represents an important model for the study of phenylalanine metabolism and the pathochemistry of phenylketonuria, yet mouse phenylalanine hydroxylase (PAH) has not been extensively studied. We report the cloning and sequencing of a mouse PAH cDNA, the expression of enzymic activity from the mouse PAH cDNA clone and the identification of mouse PAH and human PAH by two-dimensional PAGE of liver samples. These data confirm the expected homology of mouse PAH and human PAH and suggest differences in the primary sequence and the phosphorylation state of the two enzymes.
Ledley
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FD
Howard Hughes Medical Institute, Baylor College of Medicine, Houston, TX 77030.
Grenett
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HE
Dunbar
B S
BS
Woo
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SL
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002460:Cell Line; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D015180:Electrophoresis, Gel, Two-Dimensional; D006801:Humans; D008099:Liver / Q000201:enzymology; D051379:Mice; D008810:Mice, Inbred C57BL; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010651:Phenylalanine Hydroxylase / Q000235:genetics* / Q000302:isolation & purification; D011487:Protein Conformation; D051381:Rats; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid; D014162:Transfection
D004247:DNA; D010651:Phenylalanine Hydroxylase