The hepatopancreas of the terrestrial gastropod Cepaea nemoralis has a cytoplasmic β-hydroxybutyrate dehydrogenase specific for L-β-hydroxybutyrate. No dehydrogenation of Dβ-hydroxybutyrate by the enzyme was detected under our experimental conditions. The apparent K m for L-β-hydroxybutyrate is simi
Subcellular organization of intermediary metabolism in the hepatopancreas of the terrestrial snail,Cepaea nemoralis: A cytosolic β-hydroxybutyrate dehydrogenase
✍ Scribed by Stuart, J.A.; Ballantyne, J.S.
- Publisher
- John Wiley and Sons
- Year
- 1996
- Tongue
- English
- Weight
- 862 KB
- Volume
- 274
- Category
- Article
- ISSN
- 0022-104X
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✦ Synopsis
The subcellular distributions of key enzymes of the tricarboxylic acid cycle, electron transport chain, ketone body, amino acid, and carbohydrate metabolism were studied in the hepatopancreas of the terrestrial snail Cepaea nemoralis. The presence of mitochondria1 carnitine octanoyl transferase, carnitine palmitoyl transferase, and 3-hydroxyacyl-CoA dehydrogenase indicate an active lipid catabolic pathway in this tissue. Activities of enzymes of ketone body metabolism are similar in magnitude to those of carbohydrate metabolism, suggesting an important metabolic role for ketone bodies in C. nemoralis. Two enzymes that, in mammals, catalyze the synthesis of ketone bodies, hydroxymethylglutaryl-CoA synthase and hydroxymethylglutaryl-CoA lyase, are not detectable in Cepaea hepatopancreas. The activity of 3-oxoacid-CoA transferase and a portion of acetoacetyl-CoA thiolase activity are found in the mitochondria. f3-hydroxybutyrate dehydrogenase is a cytosolic enzyme in this tissue, and preferentially oxidizes the 1,-isomer of phydroxybutyrate. A portion of glutamate dehydrogenase activity is also cytosolic. The subcellular organization distribution of enzymes of intermediary metabolism in Cepaea hepatopancreas suggests adaptation to periodic anoxia. @
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β-hydroxybutyrate dehydrogenase (BHBDH) catalyzes the interconversion of the ketone bodies acetoacetate (Acac) and D-b-hydroxybutyrate (BHB). In virtually all animals, including mammals and fish (Newsholme and Leech, '83) and freshwater molluscs (Meyer et al., '86), BHBDH exists within the mitochond