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Identification of Escherichia coli K12 YdcW protein as a γ‐aminobutyraldehyde dehydrogenase
Author(s) -
Samsonova Natalya N.,
Smirnov Sergey V.,
Novikova Anna E.,
Ptitsyn Leonid R.
Publication year - 2005
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/j.febslet.2005.06.038
Subject(s) - escherichia coli , tetramer , biochemistry , dehydrogenase , nad+ kinase , molecular mass , chemistry , protein subunit , microbiology and biotechnology , biology , enzyme , gene
γ‐Aminobutyraldehyde dehydrogenase (ABALDH) from wild‐type E. coli K12 was purified to apparent homogeneity and identified as YdcW by MS‐analysis. YdcW exists as a tetramer of 202 ± 29 kDa in the native state, a molecular mass of one subunit was determined as 51 ± 3 kDa. K m parameters of YdcW for γ‐aminobutyraldehyde, NAD + and NADP + were 41 ± 7, 54 ± 10 and 484 ± 72 μM, respectively. YdcW is the unique ABALDH in E. coli K12. A coupling action of E. coli YgjG putrescine transaminase and YdcW dehydrogenase in vitro resulted in conversion of putrescine into γ‐aminobutyric acid.