anti-Galactokinase 1 (GALK1) Antibodies

Human Galactokinase 1 (GALK1) interaction partners

1. Some of the single consensus variants (M60V, D268E, A334S and G373S) increased the catalytic turnover of the enzyme, but none resulted in improved stability. When all six changes were introduced into the protein (M60V/M180V/D268E/A334S/R366Q/G373S), thermal stability was increased.

2. Focussing on four residues (Leu-231, Gln-242, Glu-244 and Glu-245) this study conducted molecular dynamics simulations to explore the effects of changing these residues to glycine or serine. The four serine variants were expressed as recombinant proteins. All had altered steady state enzyme kinetic parameters with alpha-d-galactose as a substrate.

3. Mutation in the GALK gene is associated with mental disorders in galactosemia.

4. The GALK1 gene was included in this interval and direct sequencing.

5. Data indicate taht the interactions between galactokinase (GALK) and its potential inhibitors by molecular dynamics simulations.

6. The study highlighted the importance of GALK gene analysis in diagnosis of galactosemia in Indian population.

7. A possible mechanism for the unfolding caused by the Pro(28)Thr point mutation of human galactokinase.

8. Pathogenic mutations in GALK1 that are responsible for autosomal recessive congenital cataracts in consanguineous Pakistani families, are reported.

9. 2 new GALK1 mutations near the ATP-binding site were found in a homozygotic Turkish immigrant: S142I and G148C.

10. Has ordered ternary complex mechanism with ATP being the first substrate to bind.

11. In this northern Italian population age-related cataract does not appear to be associated with GALK1 alleles.

12. structure and function of galactokinase, and role in type II galactosemia [review]

13. Structure of the human enzyme complexed with MgAMP.PNP and galactose

14. Mutations in GALK1 resulted in reduction of GALK activity and caused GALK deficiency.

15. These results suggest that the elevated GALK1 activity resulted from enhanced gene expression, due to nucleotide variation within GALK1 promoter

16. The disease-causing point mutations in the human enzyme are mapped onto the structure of the protein from Pyrococcus furiosus and speculations made about the structural consequences.

17. 2-deoxy-D-galactose is a substrate for this enzyme. D-glucose, D-fucose, L-arabinose and N-acetyl-D-galactosamine are not. Mutations H44A, H44I, E43G/H44I are insoluble, D46A is inactive, E43G has reduced activity and E43A has wild-type activity.

Mouse (Murine) Galactokinase 1 (GALK1) interaction partners

1. Egr-1 and galactokinase have roles in a developmentally regulated chain to prepare the neonate for suckling