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Purification of an α,β‐ketoalkene double bond reductase from Salmonella typhimurium
Author(s) -
Ishida Mitsuhiro,
Kitamura Shigeyuki,
Tatsumi Kiyoshi
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201342
Subject(s) - salmonella , chemistry , microbiology and biotechnology , biochemistry , biology , bacteria , genetics
Abstract An α,β‐ketoalkene double bond reductase was purified from the cell‐free extract of Salmonella typhimurium. The purified enzyme was homogeneous by the criterion of sodium dodecyl sulfate‐polyacrylamide gel electrophoresis. The molecular weight of the enzyme was estimated to be 24,700 by the electrophoresis and 23,900 by HPLC gel filtration, respectively. The isoelectric point is pH 7.2. The enzyme in the presence of NAD(P)H exhibited double bond reductase activity toward α,β‐ketoalkenes such as trans‐phenyl‐1‐propenyl ketone, trans‐benzylideneacetophenone and 15‐ketoprostaglandins. The enzyme activity was markedly inhibited by dicumarol.