Enzymes of delta 1-pyrroline-5-carboxylate metabolism in the camel tick Hyalomma dromedarii during embryogenesis. Purification and characterization of delta 1-pyrroline-5-carboxylate dehydrogenases.

The activity of P5C metabolizing enzymes: OAT, P5CR, PO, and P5CD, in the camel tick Hyalomma dromedarii has been followed throughout embryogenesis. The profiles of enzymatic activity showed clear differences in the four enzymes as the embryos grew older. During purification of P5CD to homogeneity the ion exchange chromatography steps lead to two separate forms (termed A and B) with different molecular weights (60,000-59,000 and 50,000-52,000 for the native and denatured enzymes, respectively), amino acid composition, Km for P5C and coenzymes, varying dehydrogenase activities with different substrate specificity when supplied with various aldehyde substrates. Both P5CD A and B exhibited sharp optima at pH 7.5. The effect of different divalent cations and competitive and noncompetitive inhibitors was examined. The changes in P5C metabolizing enzymes during embryogenesis suggest that H. dromedarii has the metabolic potential to convert ornithine into proline and glutamate.