Cephalopod alcohol dehydrogenase: purification and enzymatic characterization.

Abstract:

:Octopus, squid and cuttle-fish organs were examined for alcohol dehydrogenase activity. Only one form was detectable, with properties typical of mammalian class III alcohol dehydrogenase. The corresponding protein was purified from octopus and enzymatically characterized. Ion-exchange and affinity chromatography produced a pure protein in excellent yield (73%) after 1600-fold purification. Enzymatic parameters with several substrates were similar to those for the human class III alcohol dehydrogenase, demonstrating a largely conserved function of the enzyme through wide lines of divergence covering vertebrates, cephalopods and bacteria. The results establish the universal occurrence of class III alcohol dehydrogenase and its strictly conserved functional properties in separate living forms. The absence of other alcohol dehydrogenases in cephalopods is compatible with the emergence of the ethanol-active class I type at a later stage, in lineages leading to vertebrates.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Rosario Fernández M,Jörnvall H,Moreno A,Kaiser R,Parés X

doi

10.1016/0014-5793(93)80934-m

subject

Has Abstract

pub_date

1993-08-16 00:00:00

pages

235-8

issue

3

eissn

0014-5793

issn

1873-3468

pii

001457939380934M

journal_volume

328

pub_type

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