| First Author | Fernández-Cañón JM | Year | 1999 |
| Journal | Genomics | Volume | 58 |
| Issue | 3 | Pages | 263-9 |
| PubMed ID | 10373324 | Mgi Jnum | J:56027 |
| Mgi Id | MGI:1339892 | Doi | 10.1006/geno.1999.5832 |
| Citation | Fernandez-Canon JM, et al. (1999) Gene structure, chromosomal location, and expression pattern of maleylacetoacetate isomerase. Genomics 58(3):263-9 |
| abstractText | The gene for maleylacetoacetate isomerase (MAAI) (EC 5.2.1.2) was the last gene in the mammalian phenylalanine/ tyrosine catabolic pathway to be cloned. We have isolated the human and murine genes and determined their genomic structure. The human gene spans a genomic region of similar to 10 kb, has 9 exons ranging from 50 to 528 bp in size, and was mapped to 14q24.314q31.1 using fluorescence in situ hybridization. The complete catabolic pathway of phenylalanine/tyrosine is normally restricted to liver and kidney, but the maleylacetoacetate isomerase gene is expressed ubiquitously. This suggests a possible second role for the MAAI protein different from phenylalanine/ tyrosine catabolism. We have searched for mutations in the maleylacetoacetate isomerase gene in four cases of unexplained severe liver failure in infancy with clinical similarities to hereditary tyrosinemia type I (pseudotyrosinemia). Several amino acid changes were identified, but all were found to retain MAAI activity and thus represent protein polymorphisms. We conclude that MAAI deficiency is not a common cause of the pseudotyrosinemic phenotype. (C) 1999 Academic Press. |
