Title : Substrate specificity and mechanism from the structure of Pyrococcus furiosus galactokinase.

Pub. Date : 2004 Mar 19

PMID : 15003454






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Galactokinase (GalK) catalyses the first step of the Leloir pathway of galactose metabolism, the ATP-dependent phosphorylation of galactose to galactose-1-phosphate. Galactose galactokinase 1 Homo sapiens
2 Galactokinase (GalK) catalyses the first step of the Leloir pathway of galactose metabolism, the ATP-dependent phosphorylation of galactose to galactose-1-phosphate. Galactose galactokinase 1 Homo sapiens
3 The crystal structure of GalK from Pyrococcus furiosus in complex with MgADP and galactose has been determined to 2.9 A resolution to provide insights into the substrate specificity and catalytic mechanism of the enzyme. Galactose galactokinase 1 Homo sapiens
4 Inspection of the substrate binding pocket identifies the amino acid residues involved in galactose and nucleotide binding and points to both structural and mechanistic similarities with other enzymes of the GHMP kinase superfamily to which GalK belongs. Galactose galactokinase 1 Homo sapiens
5 Comparison of the sequence of the Gal3p inducer protein, which is related to GalK and which forms part of the transcriptional activation of the GAL gene cluster in the yeast Saccharomyces cerevisiae, has led to an understanding of the molecular basis of galactose and nucleotide recognition. Galactose galactokinase 1 Homo sapiens