title: Gastropod mollusc aliphatic alcohol oxidase: subcellular localisation and properties.
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.
authors.affiliation: School of Applied Sciences, University of Wolverhampton, UK.
authors.forename: N
authors.initials: N
authors.lastname: Grewal
authors.forename: Z
authors.initials: Z
authors.lastname: Parveen
authors.forename: A
authors.initials: A
authors.lastname: Large
authors.forename: C
authors.initials: C
authors.lastname: Perry
authors.forename: M
authors.initials: M
authors.lastname: Connock
mesh_terms: D000429:Alcohol Oxidoreductases / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*; D000438:Alcohols / Q000378:metabolism; D000818:Animals; D004064:Digestive System / Q000201:enzymology; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism; D008974:Mollusca / Q000201:enzymology*; D010100:Oxygen / Q000378:metabolism; D013347:Subcellular Fractions; D013379:Substrate Specificity
chemical_list: D000438:Alcohols; D005182:Flavin-Adenine Dinucleotide; D000429:Alcohol Oxidoreductases; C019643:alcohol oxidase; C077759:aryl-alcohol oxidase; D010100:Oxygen