Aconitase from the oyster Crassostrea virginica
Abstract:
1. The presence of aconitase activity in the oyster. Crassostrea virginica, has been demonstrated. 2. Low levels of activity were found in the different tissues with highest level in digestive diverticular and lowest level in muscle. 3. The conversion of both citrate and iso-citrate to cis-aconitate suggests the presence of an enzyme system capable of utilizing these compounds at a slow but demonstrable rate to give classically expected results. 4. Comparison of the oyster enzyme with aconitase from mammalian tissue indicated great similarity between the two enzyme systems.
Related Concept Videos
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
ATP Synthase: Mechanism
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
α-Hydroxy Ketones via Reductive Coupling of Esters: Acyloin Condensation Overview
Esters to β-Ketoesters: Claisen Condensation Mechanism
Alkylation of β-Diester Enolates: Malonic Ester Synthesis


