| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2052717 | FEBS Letters | 2005 | 6 Pages |
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 ± 29 kDa in the native state, a molecular mass of one subunit was determined as 51 ± 3 kDa. Km 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.
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Authors
Natalya N. Samsonova, Sergey V. Smirnov, Anna E. Novikova, Leonid R. Ptitsyn,