Biochemical characterization of Drosophila gamma-glutamyl carboxylase and its role in fly development
| Autor: | J. E. Rivier, Bradford J. Stevenson, Kathleen A. Clark, Kent G. Golic, Y. S. Rong, Pradip K. Bandyopadhyay, Baldomero M. Olivera |
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| Rok vydání: | 2006 |
| Předmět: |
Vitamin K
medicine.disease_cause Gamma-glutamyl carboxylase Cell Line Insertional mutagenesis Genetics medicine Animals Humans Cysteine Protein precursor Molecular Biology chemistry.chemical_classification Mutation Alanine biology biology.organism_classification Pyruvate carboxylase Enzyme Fertility chemistry Biochemistry Amino Acid Substitution Carbon-Carbon Ligases Insect Science Mutagenesis Site-Directed Drosophila Drosophila melanogaster Peptides |
| Zdroj: | Insect molecular biology. 15(2) |
| ISSN: | 0962-1075 |
| Popis: | To investigate structure-function relationships in gamma-glutamyl carboxylases, the enzyme from Drosophila melanogaster was characterized. Four cysteine residues were shown to be important determinants for enzymatic activity. Native Drosophila substrates have not yet been identified, but propeptides of human prothrombin and factor IX are recognized by the Drosophila enzyme. The presence of the propeptide region increased apparent affinity by approximately 200-fold, and mutation of a hydrophobic residue of factor IX propeptide (F-16A) decreased carboxylation by 90%, as in the human enzyme. Substrate recognition appears to be highly conserved between the human and Drosophila gamma-glutamyl carboxylases. Inactivation of Drosophila gamma-glutamyl carboxylase by non-sense mutations or insertional mutagenesis by P-element insertion have no apparent effects on growth and fertility under laboratory conditions. |
| Databáze: | OpenAIRE |
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