Gastropod mollusc aliphatic alcohol oxidase: subcellular localisation and properties

Citation
N. Grewal et al., Gastropod mollusc aliphatic alcohol oxidase: subcellular localisation and properties, COMP BIOC B, 125(4), 2000, pp. 543-554
Citations number
31
Categorie Soggetti
Biochemistry & Biophysics
Journal title
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
ISSN journal
03050491 → ACNP
Volume
125
Issue
4
Year of publication
2000
Pages
543 - 554
Database
ISI
SICI code
0305-0491(200004)125:4<543:GMAAOS>2.0.ZU;2-I
Abstract
The digestive gland and other tissues of several species of terrestrial gas tropod mollusc contain an aliphatic alcohol oxidase activity (EC1.1.3.13). The enzyme is FAD dependent, consumes oxygen and generates hydrogen peroxid e and the corresponding aldehyde. Saturated primary alcohols are favoured a s substrates with octanol preferred with an apparent K-m of 3-4 mu M. The a ctivity is clearly distinguishable from previously reported molluscan aroma tic 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 wit h 1% Igipal solubilises the enzyme in active form. This enzyme is a further example of an oxidase apparently restricted to molluscs. (C) 2000 Elsevier Science Inc. All rights reserved.