Identification of Escherichia coli K12 YdcW protein as a γ-aminobutyraldehyde dehydrogenase

gamma-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. parameters of YdcW for gamma-aminobutyraidehyde, NAD(+) and NADP(+) were 41 +/- 7, 54 +/- 10 and 484 +/- 72 mu M, 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 gamma-aminobutyric acid. (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.