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11‐Hydroxythromboxane B 2 dehydrogenase is identical to cytosolic aldehyde dehydrogenase
Author(s) -
Westlund Pär,
Fylling Ann Catrin,
Cederlund Ella,
Jörnvall Hans
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00409-9
Subject(s) - aldehyde dehydrogenase , hemiacetal , dehydrogenase , biochemistry , enzyme , aldehyde , chemistry , stereochemistry , cytosol , branched chain alpha keto acid dehydrogenase complex , protein subunit , substrate (aquarium) , lactate dehydrogenase , biology , ecology , gene , catalysis
11 ‐Hydroxythromboxane B 2 dehydrogenase purified from porcine kidney has been identified as cytosolic aldehyde dehydrogenase (EC 1.2.1.3). This identification is based on protein characteristics, sequence analysis of one proteolytic digest, blocked N‐terminus, subunit molecular mass of 55 kDa, and enzymatic activities. The sequence difference with the human enzyme is 7.5% in the fragments analyzed (29 exchanges of 388 positions, corresponding to the expected species variability for cytosolic aldehyde dehydrogenase The substrate thromboxane B 2 contains a hemiacetal in its ring structure, but the reaction most likely proceeds via the aldehyde form of the substrate. This finding is in agreement with the proposed metabolism of 4‐hydroxycyclophosphamide and highlights the possibility that molecules containing a hemiacetal structure can function as substrates for aldehyde dehydrogenase.