Effects of various metabolites on two phosphoglucomutase allozyme activities fromDrosophila melanogaster

✍ Scribed by Giovanni Pontecorvo; Mario Carfagna; Laura Fucci; Luciano Gaudio

• Publisher: Springer
• Year: 1986
• Tongue: English
• Weight: 299 KB
• Volume: 24
• Category: Article
• ISSN: 0006-2928
• DOI: 10.1007/bf00499095

✦ Synopsis

The effects of various metabolites on the two most common phosphoglucomutase allozymes (PGM A and PGM 8) in Drosophila melanogaster have been investigated in vitro. 2,3-Diphosphoglycerate (2,3DPG) inhibited PGM A and PGM ~ to the same degree in the presence of 25 NM glucose-l,6-diphosphate (G1,6P2). However a higher concentration of G1,6P2 partially reversed the inhibition of PGM A exerted by 2,3DPG, so that in the presence of 150 #M G1,6P2 the inhibition of PGM A was half that of PGM B at pH 6.0. Glycerol-3-phosphate (G3P) had no significant effect at pH 7.4 but exerted an activating effect at pH 6.0 which was more pronounced in the case of P G M 8. ATP, citrate, and fructose-I, 6-diphosphate (F1,6P2) inhibited both PGM A and PGM B. The differences found in vitro between these two allozymes can have a significant impact on in vivo function and, therefore, on the maintenance of PGM polymorphism in experimental populations of D. melanogas- ter studied in the laboratory.