Gastropod mollusc aliphatic alcohol oxidase: subcellular localisation and properties
Related Experiment Video
Updated: Oct 15, 2026

A Toolkit to Enable Hydrocarbon Conversion in Aqueous Environments
Published on: October 2, 2012
Abstract:
The digestive gland and other tissues of several species of terrestrial gastropod mollusc contain an aliphatic alcohol oxidase activity (EC1.1.3.13). The enzyme is FAD dependent, consumes oxygen and generates hydrogen peroxide and the corresponding aldehyde. Saturated primary alcohols are favoured as substrates with octanol preferred with an apparent Km of 3-4 microM. The activity is clearly distinguishable from previously reported molluscan aromatic alcohol oxidase (EC1.1.3.7) on the basis of FAD dependence, sensitivity to heat treatment and high salt concentration and with regard to substrate preferences. The aliphatic alcohol oxidase is membrane associated and most likely localised to the endoplasmic reticulum. Extraction of membranes with 1% Igipal solubilises the enzyme in active form. This enzyme is a further example of an oxidase apparently restricted to molluscs.
More Related Videos
Related Concept Videos
Oxidation of Alcohols
The process of oxidation in a chemical reaction is observed in any of the three forms:
Oxidations of Aldehydes and Ketones to Carboxylic Acids
Aldehydes readily undergo oxidation in strong oxidizing agents such as potassium permanganate and chromic acid. The oxidation can also be carried out using mild oxidizing agents such as silver oxide. In fact, aldehydes can be easily oxidized...
Radical Oxidation of Allylic and Benzylic Alcohols
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,...
Lipid Catabolism
Reactions of Aldehydes and Ketones: Baeyer–Villiger Oxidation
The carbonyl center is activated by...

