Classical galactosemia is an autosomal recessive inborn error of metabolism due to mutations of the GALT gene leading to toxic accumulation of galactose and derived metabolites.
Whereas classic galactosemia has been hypothesized to result from GALT misfolding, a thorough functional-structural characterization of GALT most prevalent variants was still lacking, hampering the development of alternative therapeutic approaches.
Deficiency of GALT activity in humans caused by deleterious variations in the GALT gene can cause a potentially lethal disease called classic galactosemia.
Samples (n = 243) submitted for confirmatory testing for classical galactosaemia were analysed simultaneously for GALT enzyme activity and allele-specific PCR/fragment analysis for seven mutations and two polymorphisms in the GALT gene (mutations IVS2-2A>G, p.S135L, p.T138M, p.L195P, p.K285N, p.Q188R, p.Y209C; polymorphisms p.N314D, p.L218L).
The spectrum of mutations in the Galactose-1-phosphate uridyl transferase (GALT) gene is described in 11 cases of classic galactosemia and 38 of Duarte-2 type identified by the Texas Newborn Screening Program.
Identification of mutations in the galactose-1-phosphate uridyltransferase (GALT) gene in 16 Turkish patients with galactosemia, including a novel mutation of F294Y. Mutation in brief no. 235. Online.
Classical galactosemia is caused by one common missense mutation (Q188R) and by several rare mutations in the galactose-1-phosphate uridyltransferase (GALT) gene.
Three new mutations (P183T, V150L, 528insG) and eleven sequence polymorphisms in Italian patients with galactose-1-phosphate uridyltransferase (GALT) deficiency.
We characterized two novel mutations of the galactose-1-phosphate uridyltransferase (GALT) gene in two Japanese patients with GALT deficiency and identified N314D and R333W mutations, previously found in Caucasians.
Identification and functional analysis of three distinct mutations in the human galactose-1-phosphate uridyltransferase gene associated with galactosemia in a single family.
Molecular characterization of two galactosemia mutations and one polymorphism: implications for structure-function analysis of human galactose-1-phosphate uridyltransferase.