Biochemical characterization of Drosophila gamma-glutamyl carboxylase and its role in fly development

Insect Molecular Biology
Pradip K BandyopadhyayY S Rong

Abstract

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.

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Citations

Mar 1, 2007·Blood·Aihua ZhuDavid Ginsburg
Mar 12, 2015·Yakugaku zasshi : Journal of the Pharmaceutical Society of Japan·Wataru Nomura
Jan 24, 2019·Biotechnology Letters·Samira BahramiAlireza Zomorodipour
Aug 15, 2006·The Journal of Biological Chemistry·Baldomero M Olivera
Aug 9, 2008·Journal of Health Care Chaplaincy·Lauren C VanderwerkerJohn P Bauman

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