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

FEBS Lett. 2005 Aug 1;579(19):4107-12. doi: 10.1016/j.febslet.2005.06.038.


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. Km parameters of YdcW for gamma-aminobutyraldehyde, NAD+ and NADP+ were 41+/-7, 54+/-10 and 484+/-72 microM, 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.

MeSH terms

  • Aldehyde Oxidoreductases / chemistry
  • Aldehyde Oxidoreductases / isolation & purification
  • Aldehyde Oxidoreductases / metabolism*
  • Amino Acid Sequence
  • Chromatography, High Pressure Liquid
  • Escherichia coli / enzymology
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / isolation & purification
  • Escherichia coli Proteins / metabolism*
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid


  • Escherichia coli Proteins
  • Aldehyde Oxidoreductases
  • aminobutyraldehyde dehydrogenase