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Substrate specificity of membrane-bound alcohol oxidase from the tobacco hornworm moth (Manduca sexta) female pheromone glands
- 1.0038947 - ÚOCHB 2007 RIV NL eng J - Journal Article
Luxová, Anna - Svatoš, Aleš
Substrate specificity of membrane-bound alcohol oxidase from the tobacco hornworm moth (Manduca sexta) female pheromone glands.
[Substrátová specifita membránové alkohol-oxidasy z feromonálních žláz samic lišaje tabákového.]
Journal of Molecular Catalysis B-Enzymatic. Roč. 38, č. 1 (2006), s. 37-42. ISSN 1381-1177
Institutional research plan: CEZ:AV0Z40550506
Keywords : alcohol oxidase * insects * aldehydes
Subject RIV: CC - Organic Chemistry
Impact factor: 2.149, year: 2006
A putative alcohol oxidase (AO) from abdominal tips (ATs) of Manduca sexta virgin females was studied in a biphasic system hexane/aqueous phosphate buffer. The pH optimum closest to neutral range (6.8) and the temperature optimum closest to room temperature (25+/-3 C) were measured for the highest AO activity. A high selectivity for primary alcohols of benzylic, saturated, and allylic type was observed.
Alkohol-oxidasa z feromonálních žláz samic lišaje tabákového byla studována v systému hexan/fosfátový pufr. Bylo nalezeno pH optimum 6,8 a optimální teplota 25+/-3 C pro maximální enzymovou aktivitu. Byla nalezena vysoká selektivita pro primární alkoholy jak nasycené, tak benzylového či allylového typu.
Permanent Link: http://hdl.handle.net/11104/0133153
Number of the records: 1