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

Authors :: Samsonova, Natalya N.
Smirnov, Sergey V.
Novikova, Anna E.
Ptitsyn, Leonid R.
Source :: FEBS Letters; Aug2005, Vol. 579 Issue 19, p4107-4112, 6p
Publication Year :: 2005
Abstract: Abstract: 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±29kDa in the native state, a molecular mass of one subunit was determined as 51±3kDa. K <subscript>m</subscript> parameters of YdcW for γ-aminobutyraldehyde, NAD<superscript>+</superscript> and NADP<superscript>+</superscript> were 41±7, 54±10 and 484±72μM, 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. [Copyright &y& Elsevier]

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