Title : Characterization of the human fumarylacetoacetate hydrolase gene and identification of a missense mutation abolishing enzymatic activity.

Pub. Date : 1993 Jul

PMID : 8364576






4 Functional Relationships(s)
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1 Sequencing of the liver FAH cDNA of the patient revealed a C to A transversion in the FAH mRNA, which predicted the replacement of an alanine (A) residue with an aspartic acid (D) residue at position 134 (A134D) of the amino acid sequence of the corresponding protein. Alanine fumarylacetoacetate hydrolase Homo sapiens
2 Sequencing of the liver FAH cDNA of the patient revealed a C to A transversion in the FAH mRNA, which predicted the replacement of an alanine (A) residue with an aspartic acid (D) residue at position 134 (A134D) of the amino acid sequence of the corresponding protein. Alanine fumarylacetoacetate hydrolase Homo sapiens
3 Sequencing of the liver FAH cDNA of the patient revealed a C to A transversion in the FAH mRNA, which predicted the replacement of an alanine (A) residue with an aspartic acid (D) residue at position 134 (A134D) of the amino acid sequence of the corresponding protein. Aspartic Acid fumarylacetoacetate hydrolase Homo sapiens
4 Sequencing of the liver FAH cDNA of the patient revealed a C to A transversion in the FAH mRNA, which predicted the replacement of an alanine (A) residue with an aspartic acid (D) residue at position 134 (A134D) of the amino acid sequence of the corresponding protein. Aspartic Acid fumarylacetoacetate hydrolase Homo sapiens