Differential characterization of two leucine aminopeptidases in Drosophila melanogaster

Two leucine aminopeptidases from Drosophila melanogaster larvae have been partially purified. The LAP A and D enzymes have similar biochemical characteristics including molecular weights of approximately equal to 280,000 daltons. Michaelis-Menten constants of approximately equal to 0.05 mM, associat...

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Bibliographic Details
Published in:Biochemical genetics 1981-02, Vol.19 (1-2), p.47-60
Main Authors: Walker, V K, Williamson, J H, Church, R B
Format: Article
Language:English
Subjects:
Animals
Drosophila melanogaster - enzymology
Electrophoresis, Starch Gel
Hydrogen-Ion Concentration
Kinetics
Larva
Leucyl Aminopeptidase - antagonists & inhibitors
Leucyl Aminopeptidase - isolation & purification
Leucyl Aminopeptidase - metabolism
Molecular Weight
Substrate Specificity
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Summary:Two leucine aminopeptidases from Drosophila melanogaster larvae have been partially purified. The LAP A and D enzymes have similar biochemical characteristics including molecular weights of approximately equal to 280,000 daltons. Michaelis-Menten constants of approximately equal to 0.05 mM, associations with metal cofactors, and specificities toward natural and chromogenic substrates. They differ in their pH optima and spatial distributions. If the closely linked genes that code for these enzymes have resulted from a tandem gene duplication event, it is suggested that there has been subsequent evolutionary divergence. This would provide Drosophila larvae with two related, but functionally distinct enzymes.
ISSN:0006-2928
1573-4927
DOI:10.1007/BF00486136