Tags

Type your tag names separated by a space and hit enter

Genetic basis of galactosemia.
Hum Mutat. 1992; 1(3):190-6.HM

Abstract

Classic galactosemia is an inborn error of galactose metabolism and results from deficiency of the ubiquitously expressed enzyme galactose-1-phosphate uridyltransferase (GALT). Nine missense mutations, three splicing mutations, three GALT protein polymorphisms, and one silent nucleotide substitution have been identified to date. Most of the disease-causing mutations are rare among patients. The most common mutation, Q188R, has a frequency of only one-fourth in the patient population examined. Three classes of disease-causing mutations have been reported: CRM+ missense mutations (the most common class), CRM- missense mutations, and splicing mutations. Thus, galactosemia is heterogeneous at the molecular level, which is noteworthy in light of the well-documented clinical variability observed in this disorder. It has also been shown that eight of nine galactosemia missense mutations occur in evolutionarily well-conserved domains, suggesting that they affect functionally and/or structurally important residues. In contrast, all protein polymorphisms alter variable amino acids which presumably are not important for the enzyme's function.

Authors+Show Affiliations

Howard Hughes Medical Institute, Baylor College of Medicine, Texas Medical Center, Houston 77030-3498.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

1301925

Citation

Reichardt, J K.. "Genetic Basis of Galactosemia." Human Mutation, vol. 1, no. 3, 1992, pp. 190-6.
Reichardt JK. Genetic basis of galactosemia. Hum Mutat. 1992;1(3):190-6.
Reichardt, J. K. (1992). Genetic basis of galactosemia. Human Mutation, 1(3), 190-6.
Reichardt JK. Genetic Basis of Galactosemia. Hum Mutat. 1992;1(3):190-6. PubMed PMID: 1301925.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Genetic basis of galactosemia. A1 - Reichardt,J K, PY - 1992/1/1/pubmed PY - 1992/1/1/medline PY - 1992/1/1/entrez SP - 190 EP - 6 JF - Human mutation JO - Hum Mutat VL - 1 IS - 3 N2 - Classic galactosemia is an inborn error of galactose metabolism and results from deficiency of the ubiquitously expressed enzyme galactose-1-phosphate uridyltransferase (GALT). Nine missense mutations, three splicing mutations, three GALT protein polymorphisms, and one silent nucleotide substitution have been identified to date. Most of the disease-causing mutations are rare among patients. The most common mutation, Q188R, has a frequency of only one-fourth in the patient population examined. Three classes of disease-causing mutations have been reported: CRM+ missense mutations (the most common class), CRM- missense mutations, and splicing mutations. Thus, galactosemia is heterogeneous at the molecular level, which is noteworthy in light of the well-documented clinical variability observed in this disorder. It has also been shown that eight of nine galactosemia missense mutations occur in evolutionarily well-conserved domains, suggesting that they affect functionally and/or structurally important residues. In contrast, all protein polymorphisms alter variable amino acids which presumably are not important for the enzyme's function. SN - 1059-7794 UR - https://www.unboundmedicine.com/medline/citation/1301925/Genetic_basis_of_galactosemia_ L2 - https://doi.org/10.1002/humu.1380010303 DB - PRIME DP - Unbound Medicine ER -